\r\n\tThe surgical approach to prostate cancer is traditionally considered a milestone in the treatment of this disease. To date, minimally invasive procedures like laparoscopy and robotic surgery are a gold-standard and will be described in the book. Also, there is a growing interest among the investigators on conservative techniques. For this reason, there are chapters on non-surgical techniques, like radiotherapy and brachitherapy and on experimental techniques, like high-intensity focused ultrasound or electroporation.
\r\n\tIt is well known that the key to success in treatment of prostate cancer is the ability to perform the best treatment available, but not all patients are good candidates to the same treatment. This book intends to provide the reader with a comprehensive overview of the wide range of treatments available for prostate cancer and aims to give more insight on the opportunities related to a multimodal approach.
Liquid biopsies may contain a wide variety of biomolecules including DNA, RNA, proteins and metabolites. When considering the presentation of the numerous proteins within a liquid biopsy, these can be free in the plasma, encapsulated within or on the surface of extracellular vesicles (EVs) or still inside cells within the biopsy (such as in the case of circulating tumour cells (CTCs)).
\nOne class of proteins garnering particular interest as part of liquid biopsies are extracellular heat shock proteins (HSPs), and their post-translational modifications (PTMs), mainly because they should not be present in body fluids at the concentrations observed due to their lack of an export sequence and also as a result of the growing evidence supporting the notion that these proteins can mediate intercellular crosstalk and act as messengers that activate signalling pathways during stress conditions.
\nHSPs are a class of chaperone proteins ubiquitously expressed in the cells of both prokaryotic and eukaryotic organisms. HSPs have been traditionally named and subdivided into six groups or families based on their molecular weight, namely, the small HSPs (which include HSP27), HSP40, HSP60, HSP70, HSP90 and HSP100 family. However, more recently, a new nomenclature and classification system based on the naming issued by the Human Genome Organisation (HUGO) Gene Nomenclature Committee (HGNC) has been proposed for classifying human HSPs into the following groups: HSPA (HSP70), HSPB (small HSPs including HSP27), HSPC (HSP90), HSPD/HSPE (HSP60/HSP10), HSPH (HSP110) and DnaJ (HSP40) [1]. Each of these families has members that are constitutively expressed and others that are inducible upon stress.
\nUnder normal physiological conditions, constitutive HSPs fulfil important regulatory roles in a wide range of cellular processes including the synthesis, folding, translocation, assembly and in some cases activation of the proteins they interact with. On the other hand, after an episode of cellular stress, inducible HSPs help to refold and prevent aggregation of misfolded proteins, as well as assist in the proteasomal degradation of misfolded proteins which cannot be recovered. Moreover, HSPs can block apoptotic signalling and increase tolerance to subsequent insults [2].
\nHowever, it is now starting to emerge that during stress, the role of HSPs goes beyond what is expected to be their intracellular chaperoning functions for recovery from multiple stress conditions. Despite HSPs acting predominantly intracellularly, they have also been found expressed in the cell plasma membrane and in the extracellular space. Numerous HSPs have been reported to be present in the extracellular space and general circulation, activating a range of signalling pathways depending on the effector cell type or target organ. The role of such extracellular HSPs appears to be that of a systemic warning system of stressful events or chronic conditions, acting by priming the body, of which the immune system is a major effector, in order to prepare for and counteract the spread of the stress insult. Extracellular HSPs thus seem to act as a form of intercellular communication system during stress conditions, particularly those responses linked to oxidative stress, immunity or inflammation [3].
\nWhen HSPs are present outside cells, they can be found as free proteins in solution or forming part of EVs. EVs can be of various types, with distinct structural and biochemical properties as well as intracellular site of origin. These include large microvesicles (up to 1500 nm) that are heterogeneous in shape and produced from the plasma membrane, small (50–100 nm) and more uniformly shaped exosomes released from endosomes via the endocytic pathway and apoptotic vesicles produced upon cell death [4, 5].
\nEVs are released by almost all cell types, both healthy and diseased (including tumour cells). Such vesicles carry a wide range of biologically active molecules including growth factors, cytokines, mRNAs and microRNAs, extracellular matrix constituents and also proteins [6]. The protein fraction consists of cytosolic or plasma membrane components, either inside or on the surface. Their molecular contents have been shown to mediate intercellular communication in a variety of cellular processes, in both normal and pathological conditions, with the transfer of such biomolecules altering the function of the target cells. In the context of cancer, for example, EVs can modulate both the tumour microenvironment and cells and tissues which are located at a distance, affecting the immunity in the area, promoting angiogenesis and bringing about metastasis [7, 8].
\nEVs are also released by cells in response to being exposed to a stressor or as a result of chronic cellular stress. Such EVs contain particular molecules, including HSPs, whose expression level is directly linked to or induced by the stress insult. Upon reaching their effector cells, and especially when interacting with cells of the immune system, some EV components act as signalling molecules, activating a response in the effector cells which pre-empts the stress insult prior to its spread [3].
\nProteomic studies have shown that EVs from serum, saliva, milk or plural effusions contain HSP27, HSP60, HSP70 and HSP90 [9, 10, 11, 12, 13, 14, 15, 16] at high concentrations, with the ability to synergise with other encapsulated factors [3]. The delivery of HSPs in EVs provides a much stronger signal to effector cells as exemplified by EVs containing HSP70 producing a 250-fold higher activation of macrophages than an equal concentration of HSP70 in solution [17].
\nThe HSPs encapsulated within or presented on the surface of such EVs, together with changing levels in free HSPs, can thus be valuable disease biomarkers for early detection, diagnosis and therapy selection. However, in order to access them, these proteins need to be purified from the body fluids of patients, characterised, quantified and compared to what is known in the healthy condition.
\nWhen cells are exposed to a stressor, which includes but is not limited to heat shock, osmotic stress, exposure to heavy metals, hypoxia, ischemia or pathogens, these release signalling molecules in order to alert the rest of the system that a stressful condition is being experienced in some part of the organism and which might potentially lead to a situation of systemic damage. Among the stress signals which can be released by cells in response to an incidence of cellular stress are HSPs and other components of the chaperone (Figure 1). It is worth noting that most HSPs lack the consensus signal required for secretion via the classical endoplasmic reticulum (ER)-Golgi pathway [3, 18]. So far, it appears that the secretion of HSPs is achieved via a number of alternative pathways; however, these are still not well defined. Presently, the HSP release mechanisms identified are (but might not be limited to) processes via:
Cell lysis—where the process can be the result of a physiologically regulated release of cytokines or necrosis resulting from a pathological condition. Extracellular HSP70 has been suggested to be released into circulation under a variety of pathological conditions which cause widespread cell death as well as the following necrosis of tumour cells [19].
Endolysosomal pathway—where the HSP is translocated into lysosomes and instead of being degraded is translocated out of the cell via endocytosis. HSP27 (dephosphorylated at S15 and S82) [20] and HSP70 [21] have been shown to enter endolysosomes, which are then secreted extracellularly in an ATP-dependent manner, from both tumuor cells and macrophages possibly via some pathway analogous to the ATP-binding cassette (ABC) transport system [21].
Exosomal pathway—where the HSP is contained in secretory vesicles (exosome lumen) which rupture or are lysed once present in the extracellular space. A number of HSPs have been detected within extracellular vesicles including HSP27, HSP70, HSC70, GRP75, GRP78 and HSP90 [22, 23, 24, 25].
Inclusion in the exosomal membrane—where the HSP is inserted into the membrane of the secretory vesicles rather than being in the lumen. The isolation of HSP70-containing vesicles, derived from the plasma membrane, indicates that the surface of the vesicle can be used as an export system [17, 26, 27].
Secretory-like granules—where the vesicles used to transport the HSP are neither lipid bodies, nor endosomes, or lysosomes. Tumour cells were found to release HSP70 in structures that were only positive for chromogranin A, which is a marker of secretory granules [28].
Heat shock proteins (HSPs) are exported into the extracellular space and general circulation via a number of different processes including cell lysis, secretory vesicles, lysosomal endosomes or export vesicles. Once these extracellular HSPs reach the target tissues, they bind to a variety of receptors, which initiate an alarm response. When these extracellular HSPs are collected from patients with chronic diseases and quantified, they can have diagnostic or prognostic value.
Once in the extracellular space or general circulation, these HSPs can stimulate a wide range of cell types. However, similar to the secretion mechanisms, the recognition and uptake of HSPs by cells, as well as the role that extracellular HSPs play in cell activation, are poorly understood. HSPs have been reported to bind to a wide variety of receptors on target cells, among which are:
Low-density lipoprotein (LDL) receptor-related protein 1 (LRP1; CD91)—a receptor involved in receptor-mediated endocytosis, which is found on numerous cell types including antigen-presenting cells (APCs), known to bind to HSP70, HSP90 and calreticulin [29, 30].
CD40—a member of the tumour necrosis factor (TNF) receptor family that is essential in mediating a broad variety of immune and inflammatory responses and can bind to HSP70 [31, 32].
C-C chemokine receptor type 5 (CCR5; CD195)—a receptor on white blood cells involved in the process by which T cells are attracted to target areas via cytokines, which has also been shown to bind to mycobacterial HSP70 [33].
Toll-like receptors (TLRs)—of the ten TLR receptors found in humans, only TLR2 and TLR4 are so far known to act as HSP receptors. They are known to bind to HSP60, HSP70 and HSP90 [34, 35, 36, 37]. It has been suggested that TLR activation by HSP is most likely not the result of a direct binding of HSP70 to these receptors but rather either a low affinity interaction or a secondary activation involving the prior binding of HSP to another receptor [38].
CD14—a co-receptor for TLR4 activation, which was found to be also required for HSP70 induction of cytokines [35].
Scavenger receptors (SR)—a family of receptors currently classified into ten subclasses (A–J) based on structure and biological function [39]. At least three SRs bind to and internalise HSPs, namely, lectin-like oxidised LDL receptor 1 (LOX-1), scavenger receptor expressed by endothelial cell 1 (SREC-1) and fasciclin and EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1(FEEL-1)/common lymphatic endothelial and vascular endothelial receptor 1 (CLEVER-1), with HSP70 binding to all three, HSP60 binding to LOX-1, HSP90 binding to LOX-1 and SREC-1 and calreticulin binding SREC-1 but not LOX-1 [38, 40, 41, 42, 43]. Furthermore, scavenger receptor-A (SR-A) can bind to and internalise HSP90 and calreticulin as well as HSP110 and GRP170 [42, 44]. The sialic acid-binding immunoglobulin-type lectin (Siglec) receptors Siglec-5 and Siglec-14 have also been found to bind to HSP70 [45, 46].
Changes in extracellular HSPs have been detected and implied to be actively involved in many chronic pathological conditions including arthritis, cardiovascular disease, cancer, type 2 diabetes mellitus (T2DM), chronic obstructive pulmonary disease (COPD) and neurodegenerative diseases. However, in order for these extracellular proteins to be used as biomarkers for early diagnosis, prognostic assessment, disease progression monitoring, therapy selection or treatment response, it is essential to characterise their functions and quantify their levels in the selected body fluids for liquid biopsies under both normal physiological conditions and the various pathological contexts.
\nFor example, with respect to cancer, a wide range of studies have linked changes in extracellular HSPs to key mechanisms involved in either the process of malignant transformation or the progression of a tumour via evasion of apoptosis, increased cell proliferation and immortality, invasiveness and metastasis. On the other hand, when it comes to T2DM, because the biochemical mechanisms are not well understood, it is more difficult to link extracellular HSPs to the aetiology of the condition. However, T2DM patients present a two- to fourfold higher risk of developing macrovascular diseases, including coronary artery disease, stroke and peripheral vascular disease, making episodes of cardiovascular complications the major fatality in such patients [47]. Moreover, the sustained hyperglycaemia brings about cellular dysfunction via systematic biochemical changes due to oxidative stress, accumulation of advanced glycated end products (AGEs) and chronic inflammation [48], which are processes highly associated with HSPs.
\nExtracellular HSP27 has been so far linked to three major functions, immune response modulation, angiogenesis and atheroprotection through a number of mechanisms, which in the contexts of cancer and T2DM can have a significant contribution to the aetiology or progression of the disease.
\nImmune signalling is activated by extracellular HSP27 via interaction with receptors on the surface of immune or endothelial cells, leading to the differential production and release of cytokines and growth factors, in order to modulate the immune response, cellular migration and proliferation. Extracellular HSP27 interacts with TLR2, TLR3 and TLR4, bringing about NF-κB transcriptional activation and the upregulation of intercellular adhesion molecule-1 (ICAM-1) and monocyte chemoattractant protein-1 (MCP-1), leading to the secretion of TNF-α, IL-6, IL-8, IL-10, IL-1β, IL-12p35 and IL-12p40, colony-stimulating factor 2 (CSF2) and vascular endothelial growth factor (VEGF) [49, 50, 51, 52]. The release of IL-10 induced by extracellular HSP27 was found to involve the phosphorylation of p38 and MAPKAPK-2, whilst the upregulation of TNF-α was attributed to the activation of both p38 and ERK1/ERK2 signalling pathways [53]. HSP27 was also found to interact with oestrogen receptor-β (ER-β) [54, 55].
\nIn cancer, extracellular Hsp27 has been reported to exert pro-angiogenic effects via the stimulation of the transcription of the vascular endothelial growth factor (VEGF) gene [50]. Increased VEGF expression promoted HSP27 phosphorylation through the stress-activated protein kinase 2 (SAPK-2)/p38 pathway, resulting in cytoskeletal rearrangements and endothelial cell migration [56]. Furthermore, HSP27 phosphorylation not only reduced the release of HSP27 in the extracellular space, where the released HSP27 binds to and blocks VEGF [20], but also enhanced intracellular VEGF expression by interacting with the TLR3 on endothelial cells [50].
\nIn the context of diabetes, T2DM patients with cardiovascular disease presented no significant change in serum HSP27 than non-diabetic controls [57]. However, extracellular HSP27 levels were found to be inversely correlated to progression, complexity and instability of plaques found in atherosclerotic human coronary arteries [54, 58], with HSP27 secretion being greatly reduced in atherosclerotic lesions and almost absent in complicated plaques [59]. Lower levels of serum HSP27 were described as being predictive of subsequent heart attacks, strokes or cardiovascular death within the following 5 years [60]. Atheroprotection is thought to be mediated through oestrogen (for the extracellular release of HSP27) as well as via modulation of various processes involved in atherosclerosis, such as cholesterol homeostasis and trafficking, regional inflammation (including mobility of immune cells in plaques and macrophage activation into foam cells) and plaque remodelling by extracellular HSP27 [61]. Extracellular HSP27 seems to be involved in reduced lipid engulfment by macrophages and foam cell formation through the blocking and downregulation of macrophage scavenger receptor A [62, 63], as well as the promotion of cholesterol efflux by enhancing ATP-binding cassette (ABC) transporter activity via the TLR4-induced and NF-κB-mediated release of CSF2 [64]. A similar activation of NF-κB in endothelial cells via TLR2, TLR3 and TLR4 may further worsen the condition [50, 51]. Moreover, patients with T2DM presented accelerated platelet aggregation correlated with the release of phosphorylated HSP27 from platelets induced by thrombin receptor-activating protein (TRAP) activation of Akt and p38 MAP kinase [65, 66].
\nTill now, extracellular HSP60 has not been linked to any specific function. What has been explored so far is mostly related to its release mechanism. It has been shown that HSP60 is released into the extracellular space via the exosomal pathway, with most of the HSP60 tightly bound to (as opposed to embedded in) the exosomal membrane, rather than housed in the lumen of the exosomes. Moreover, evidence indicates that exosomal HSP60 is at least in part ubiquitinated (but not poly-ubiquitinated, i.e. not marked for degradation), which might act as a signal for the sorting of HSP60 to exosomes [12]. This ties in with its presence in cancer and T2DM, although the significance of its role in the aetiology or disease progression have not been well investigated.
\nWhen looking at the cancer context, tumours often tend to present HSP60 in the cell membrane [67] as well as secreted via exosomes [68]. It is hypothesised that cellular stress results in ubiquitination and possibly other post-translational modifications on cytosolic HSP60, which lead to its localisation in the cell membrane and consequently internalisation via lipid rafts, accumulation in multivesicular bodies and release into the extracellular space via the exosomal pathway [12]. Once secreted (either alone or in conjunction with other biomolecules), it then fulfils an as-yet unspecified but probably immunomodulatory extracellular function [69, 70]. Bioinformatic analysis of colorectal cancer (CRC) pointed at the HSP60 gene as one of the best indicators for diagnosis [71] and proteomic studies have corroborated this finding [72] giving it diagnostic and prognostic value. Similarly, HSP60 has also been found to be linked to Crohn’s disease and ulcerative colitis [73], two conditions with a high risk for CRC development, probably having a pro-inflammatory role in the remodelling of the colonic mucosa via a TLR4-ERK-dependent mechanism [74].
\nExtracellular HSP60 is also thought to play a role in diabetes, as stresses associated with diabetes result in the expression of HSP60 on the cell surface as well as its extracellular release, such that it has been detected in both the serum and the saliva of T2DM patients [75, 76]. Moreover, T2DM patients with cardiovascular disease were associated with higher levels of circulating HSP60 compared to control subjects without cardiovascular disease [77]. Extracellular HSP60 has been associated with the severity of atherosclerosis and has been proposed as a biomarker for coronary heart disease [78, 79].
\nExtracellular HSP70 has been shown to have important immunostimulatory properties, activating macrophages, monocytes, dendritic cells (DCs) and natural killer (NK) cells, by acting either as a cross presenter of immunogenic peptides via major histocompatibility complex (MHC) antigens, as a chaperone stimulating both innate and adaptive immunities, or as a stimulator and target for innate immune responses mediated by NK cells [35, 80, 81]. In contrast, some studies have shown that it can also have anti-inflammatory effects by activating both immunosuppressive regulatory T cells (Tregs) and Siglec receptors that block the inflammatory process by interacting with TLRs [82]. Moreover, extracellular HSP70 bound to vesicle membranes has been shown to induce an immunosuppressive effect [27], supporting the notion that HSP70 fulfils different roles depending on the composition, source and effector of the vesicles it is associated with.
\nApart from immunity, extracellular HSP70 has been implicated in a wide array of conditions including cancer, diabetes, chronic inflammation, cardiovascular disease, hypertension, pre-eclampsia, Alzheimer’s disease (inhibiting amyloid β aggregation) and ischemia [3, 83, 84].
\nWhen it comes to the cancer setting, serum HSP70 levels have been correlated with treatment response and tumour volume [85], making extracellular HSP70 a potential biomarker for cancer [86] both as a candidate biomarker for tumour detection and monitoring clinical outcome of radiotherapy [87], as well as a prognostic marker, such as in CRC, associated with rapid disease progression and poor survival [88]. In some contexts, extracellular HSP70 has even shown potential in discriminating between infection or inflammation and cancer (e.g. chronic hepatitis, liver cirrhosis and hepatocellular carcinoma) [89]. Extracellular HSP70 has been found to increase MMP9 expression by activating NF-κB and AP-1 and that the subsequent increase in pro-MMP9 secretion results in enhanced cell motility and invasiveness [90]. HSP70 was also isolated from the surface of tumour-derived exosomes [26], in which setting it can interact with myeloid-derived suppressor cells, so as to suppress T-cell activation and promote cancer development [27]. Extracellular HSP70 has also been used as a cancer vaccine, such that immunisation of mice with a vaccine made of HSP70-peptide complexes extracted from fusions between DCs and radiation-enriched tumour cells resulted in a T-cell-mediated immune response against radioresistant tumour cells [91].
\nIn vitro experiments of diabetes have shown that extracellular HSP70 plays a role in diabetic nephropathy in T2DM by promoting inflammation in the proximal tubule cells via a TLR4-NF-κB pathway. HSP70 release induced by the albumin in the proximal tubule cells triggered the overexpression of the inflammatory cytokines monocyte chemoattractant protein’ 1 (MCP-1), tumour necrosis factor alpha (TNF-α) and macrophage inflammatory protein 2 (MIP2) [92]. Similar results were obtained in diabetic mice where TLR4 deletion or HSP70 inhibition reduced albuminuria and markers of inflammation and tubular injury [92]. Further supporting these findings, patients with T2DM with albuminuria showed higher serum HSP70 levels [93] as well as an association between urinary HSP70 levels and albuminuria [94]. Serum HSP70 was also found to be higher in patients with diabetic retinopathy, together with HIF-1α compared with subjects without [95] and correlated well with asymmetric dimethylarginine (ADMA) and C-reactive protein (CRP) levels in T2DM patients compared with healthy controls [96].
\nAn inverse association has been reported between levels of HSP70 with the presence and severity of cardiovascular disease [97, 98, 99, 100]. Moreover, an inverse correlation was found between HSP70 levels and the risk of future development of atherosclerosis in subjects with established hypertension [101]. Extracellular Hsp70 levels have also been inversely correlated with the risk of cardiovascular disease [97, 101, 102] and the severity and survival after chronic heart failure [103].
\nExtracellular GRP78 has been documented [104, 105], but it has been studied much more extensively at the cell surface than in the extracellular space or in circulation. GRP78 could be detected in plasma as both full-length and C-terminus fragments [106]. GRP78 is secreted from cells via exosomes, and the release appears to be at least partly controlled by acetylation since the use of histone deacetylase (HDAC) inhibitors could block GRP78 release, causing aggregation in the ER. Suppression of HDAC6 activity leads to GRP78 acetylation, which is then bound to vacuolar protein sorting 34 (VPS34), a class III phosphoinositide-3 kinase, preventing GRP78 from being sorted into multivesicular bodies [107]. Since it has been shown that ER stress can actively promote the expression of GRP78 on the cell surface, and that over-expression of GRP78 can result in similar cell surface localisation, independent of ER stress [102], this might also hold true for extracellular release of GRP78. Once in the plasma membrane GRP78 binds to a wide selection of proteins, which in turn causes signalling cascades through multiple pathways that can result both in cell survival and cell death [108, 109], however the potential interaction or competition of extracellular GRP78 has not been explored. Interestingly, HSP40 (DnaJ) seems to be involved in GRP78 cell surface localisation and silencing of the murine homolog, MTJ-1 abolished cell surface localisation of GRP78 [110], but so far its possible involvement in extracellular release instead has not been investigated.
\nWhen looking at cancers, extracellular GRP78 is not commonly investigated; however, some tumours secrete significant levels of GRP78 into the tumour microenvironment [105], and in one study, extracellular GRP78 was identified exclusively in the sera of 28% of gastric cancer patients but not in healthy controls [111]. It is speculated that ER stress and activation of the unfolded protein response (UPR), an evolutionarily conserved mechanism in which survival or apoptotic pathways are activated in response to ER stress, induce GRP78 in tumour cells leading to increased secretion of GRP78, and by binding to cell surface receptors of endothelial cells, extracellular GRP78 activates ERK and AKT pathways [105].
\nUseful inferences could be made by looking at cell surface GRP78 which is expressed significantly in human tumours and generally associated with cell proliferation, cell survival, angiogenesis and metastasis [112]. Cell surface GRP78 interacts with α2-macroglobulin, a plasma protease inhibitor, through its amino-terminal domain-activating the PI3K/Akt, ERK1/ERK2 and p38 MAPK pathways, promoting cell proliferation and cell survival via Akt and NF-kB signalling cascades, by inducing the UPR [105, 113, 114]. Moreover, interaction of cell surface GRP78 with teratocarcinoma-derived growth factor 1 (TDGF1; Cripto-1), a small, glycosylphosphatidylinositol (GPI)-anchored protein, modulates activin-A, activin-B, nodal and transforming growth factor-b (TGF-b)-dependent signalling of several ligands via the MAPK/PI3K and Smad2/3 pathway and promotes cell proliferation, downregulates E-cadherin (which decreased cell adhesion) and promotes pro-proliferative responses to activin-A and nodal [115, 116]. Of particular interest is that specifically on the surface of cancer cells but not healthy cells, GRP78 interacts via its amino-terminal domain with extracellular prostate apoptosis response 4 (Par-4), which together with tumour necrosis factor-related apoptosis-inducing ligand or Apo 2 ligand (TRAIL/Apo2L) mediates apoptosis via an extrinsic apoptotic pathway (dependent on ER stress and the Fas-associated death domain (FADD)/caspase-8/caspase-3 pathway) [117]. Similarly, plasminogen kringle 5 (K5), an angiogenesis inhibitor, interacts with cell surface GRP78 via the carboxy-terminal domain, on hypoxic and cytotoxic stressed tumour cells, mediating anti-angiogenic and pro-apoptotic activity following the internalisation of GRP78 by the scavenger receptor low-density lipoprotein receptor-related protein 1 (LRP1) and activation of p38 mitogen-activated protein kinase [118, 119].
\nThe isolation of a tumour-specific variant of GRP78 containing an O-linked carbohydrate moiety with a molecular weight of 82 kDa opens up numerous therapeutic possibilities not only of targeting tumours by specific variants of GRP78 [120] but also of searching for the presence of tumour-specific variants in circulation, as a diagnostic marker.
\nOnce again in the context of diabetes, extracellular GRP78 is poorly investigated. However, data from cell surface expression of GRP78 indicates that the extracellular counterpart might play some role in the cardiovascular complications linked to T2DM. GRP78 has been detected on microparticles shed from activated endothelial cells indicating that GRP78 expression may be involved in regulating thrombosis [121]. Expression of cell surface GRP78 in arterial atherosclerotic lesions negatively regulates the initiation of the tissue factor(TF)-mediated coagulation cascade [122, 123], attenuating procoagulant activity similar to the effect observed from the binding of K5 to cell surface GRP78 on stimulated endothelial cells [119]. Atherosclerotic lesions also present an increase in truncated cadherin (T-cadherin) expression, which interacts with cell surface GRP78, similar to the interaction on vascular endothelial cells [124] and on endothelial cells during tumour angiogenesis [125], promoting cell survival and indicating that this interaction plays a role in vascular tissue remodelling related to stress.
\nAs with most other HSPs, extracellular HSP90 has been mainly studied in relation to inflammation and immunity [126]. However, no specific roles, processes or mechanisms have been elucidated yet.
\nIn the context of cancer, extracellular HSP90 (mainly not only HSP90a but also HSP90b) is known to be involved in tumour cell migration, invasion and metastasis [127, 128, 129, 130, 131]. Serum levels of extracellular Hsp90a were significantly higher in the patient groups with tumour burden, with a positive correlation with tumour malignancy and metastasis [132]. The interaction of extracellular Hsp90 with the LRP1 receptor as well as HER-2 activates AKT1/AKT2 (in the phosphatidylinositol-3-kinase (PI3K) signalling pathway) and ERK1/ERK2 signalling cascades giving rise to increased cell migration, supporting growth and survival [128, 133, 134]. AKT activation is sustained by the phosphorylation of the receptor tyrosine kinase ephrin type-A receptor 2 (EPHA2), which is a downstream product of the interaction between LRP1 and extracellular Hsp90 [135]. Also, critical for cell migration is the presence of extracellular HSP90 for the interaction between Src and integrin β1 at focal adhesion points between the cell and ECM [130]. The interaction of extracellular HSP90 with TLR4 also signals through Src, and this transactivates the epithelial growth factor receptor (EGFR), which increases cell migration [136]. It has also been shown that extracellular HSP90 can have a role in ECM remodelling or stabilisation via its direct interaction with fibronectin [137]. Work in colorectal cancer cells showed that extracellular Hsp90 promotes epithelial-to-mesenchymal transition (EMT) via an LRP1-NF-κB pathway [138], whilst exposure of prostate cancer cells to extracellular Hsp90 promoted EMT via a process requiring both matrix metalloprotein 9 (MMP9) and ERK activity [139]. Extracellular Hsp90 was also shown to interact with MMP2 [140]. The activation of ERK by extracellular Hsp90 has also been shown to increase expression of the polycomb repressor complex methyltransferase enhancer of zeste homologue 2 (EZH2), bringing about the epigenetic repression of E-cadherin [141], further supporting the EMT process.
\nExtracellular HSP90 has not been studied much in the context of diabetes, with the majority of studies investigating HSP90 inhibition in general and thus focusing on intracellular mechanisms whilst not excluding effects by extracellular HSP90. In response to oxidative stress, vascular smooth muscle cells secrete HSP90a, and the stimulation of these cells by HSP90a induces MAPK activity [142]. Similarly, endothelial cells also secrete HSP90 upon activation, and this stimulates angiogenesis [143]. Experiments in diabetic rats have shown that annexin II on endothelial cells interacts with extracellular HSP90a, modulating plasminogen activation to plasmin [144]. Furthermore, HSP90 levels were found to be higher in the serum of patients with atherosclerosis [145]. Exosomes collected from cultured fibrocytes contained HSP90a (among other biomolecules) and enhanced cellular migration and proliferation as well as secretion of type I collagen (COL1) and type III collagen (COL3) and expression of α-smooth muscle actin (α-SMA) [146]. Inhibition of total HSP90 disrupts the IKK complex [147] and JAK2 protein stability [148], blocking the activity of the transcription factors NF-kB [149] and STAT [150], respectively, together with a downregulation in the expression of proatherogenic cytokines and chemokines. Dysregulated NF-kB and STAT pathways contribute to diabetic nephropathy [150, 151] and atherosclerosis [152, 153]. The inhibition of HSP90 thus modulates inflammation and oxidative stress, improving diabetes-associated renal damage and atheroprogression [154], insulin sensitivity [155], high-fat-diet-induced renal failure [156] and diabetic peripheral neuropathy [157].
\nThe need to identify biomarkers for complex systemic and chronic diseases is pressing, with an increasing push towards the successful development of therapies aimed at modulating serum levels, blocking receptor binding or inhibiting signalling cascades. HSPs hold great potential as therapeutic targets for those conditions with underlying mechanisms involving accumulation of misfolded or damaged proteins, oxidative stress, altered mitochondrial bioenergetics or dysregulated apoptosis, particularly as a result of their non-chaperoning functions. Studies presented herein suggest that circulating HSP levels may be exploited as biomarkers of such conditions, with cancer and cardiovascular complications linked to T2DM being the contexts used to exemplify.
\nA major limitation of most studies performed on extracellular HSPs is that their functions and roles in disease have not been elucidated yet. As a result the biochemistry and signalling are investigated very poorly, such as testing for a single downstream product of a complex cascade which can be affected by multiple inputs. Similarly, the PTMs on extracellular HSPs are still in their majority obscure both in abundance and functional significance. Studies conducted retrospectively, on single HSPs in isolation, using small patient groups and without adjustment for confounding effects offer a very poor analysis of the predictive power of HSPs for early diagnosis or prognostic assessment. Thus, in future research, it is important to take into consideration that HSPs do not work in isolation, but act within a network, rather than just detect changes in the total extracellular expression levels of individual HSPs and analyse changes in both total HSP and specific PTMs within groups of chaperone proteins that are functionally relevant to either the development of or resultant from the progression of the condition under investigation. Furthermore, this needs to be performed in large cohorts of well-characterised patients, with prospective validation of promising biomarker panels, if the intent is really their application in a clinical setting.
\nThe author declares no conflict of interest.
Optical control of biological reactions is one of the most recently studied fields of research because light facilitates highly spatial and temporal manipulation. In particular, optogenetics, that is, the specific and noninvasive control of biological activities such as neural activities by light stimulus of photoreceptor proteins heterogeneously expressed in targeted neurons or other related cells, has a significant impact in the field of neuroscience [1, 2, 3, 4, 5, 6, 7, 8] and has attracted the interest of myriad researchers in the life sciences. Over the past 15 years since the first report on optogenetics in 2005 [1], the development of tools for this interesting technique has been rapidly progressing [9, 10, 11, 12, 13, 14]. Recently, various types of photosensitive proteins have been employed for optogenetics [15, 16, 17]. Nevertheless, retinal-based proteins found in microbes (referred to as microbial rhodopsins), which were first applied to optogenetics, are still overriding toolkits [18, 19].
Microbial rhodopsins (also termed type-I rhodopsins) are seven transmembrane α-helical proteins that bind to the retinal chromophore, similar to animal rhodopsins (also termed type-II rhodopsins) [20]. A distinctive property of animal rhodopsins is the difference in their chromophore configurations; retinals in microbial and animal rhodopsins adopt all-
Microbial rhodopsins are classified into two categories of ion carriers. One is a light-gated ion channel, and the other is a light-driven ion pump. The former group includes channelrhodopsins (ChRs) [8, 25, 26, 27] and anion channelrhodopsins (ACRs) [28, 29, 30], which are the principal tools for optogenetics. Upon illumination, ChRs become permeable to various monovalent or divalent cations, such as H+, K+, Na+, and Ca2+ [8, 25, 26, 27]. Therefore, in nerve cells expressing ChRs, the influx of Na+ induced by light activation of ChRs causes depolarization in these cells, leading to neural activation [1, 2, 3, 4, 5, 6, 7, 8, 25, 26, 27]. Conversely, light activation of ACRs, which act as anion-selective channels, can drive the hyperpolarization of ACR-expressing cells to suppress neural activity [28, 31]. The ion pump group includes light-driven outward H+- [32, 33], Na+- [34], and inward Cl−-pumps [35, 36, 37, 38]. As these proteins can generate negative membrane potential in their incorporated cells by illumination, they can be utilized as neural silencers similar to ACRs [39, 40]. Microbial rhodopsins, as ion channels or pumps, can lead to changes in membrane potential by absorption of a photon without going through complicated reactions. This simple light-activated machinery makes them more easily applicable to optogenetics, together with repeatable properties through their photocycle.
Among the three types of ion-pumping rhodopsins, proton-pumping rhodopsins have a distinct feature from the other two. Proton translocation across the cell membrane induced by light activation of these pigments is accompanied by a change in intracellular pH. Hence, these proteins have the potential for various applications, for example, photoinduced pH control in cells or all sorts of organelles, as well as their use as neural silencers. To date, genes encoding H+-pumping rhodopsins have been identified from the genomes of many microorganisms, irrespective of species [41], which enables us to gain the most plentiful genetic information from the database of the microbial rhodopsin family. Therefore, these types of rhodopsins may be applicable for exploring better candidates for optogenetics in various respects, such as the strength of neural inhibition, spectral properties (maximum absorption wavelength for activation), and kinetics.
Chow et al. screened efficient neuronal silencing rhodopsins and showed that the magnitude of photocurrents evoked by the activation of H+-pump-type rhodopsins was on average higher than those evoked by the activation of inward Cl−-pump halorhodopsins (HRs) [39]. Moreover, the rates of activation upon light irradiation and recovery from inactivation after light cessation tended to be faster, as observed for archaerhodopsin-3 from
Among all microbial rhodopsins, the first H+-pumping rhodopsin reported was bacteriorhodopsin (BR), which was discovered in
Following the discovery of BR, the second H+-pump identified was archaerhodopsin (aR). Two homologous proteins, archaerhodopsin-1 and -2 (aR-1 and aR-2), were simultaneously identified from
The history of microbial rhodopsin research has been confined to the archaebacterial world for about three decades since the first discovery of BR. However, since the 2000s, rapid technical advances in metagenomics have led to the discovery of unknown microbial H+-pumping rhodopsins from various eubacteria [58, 59]. A representative example is proteorhodopsin (PR) from marine bacteria [60, 61].
In 2000, PR was first identified in the genome of uncultivated marine γ-proteobacteria, which is a member of the SAR86 clade, from a sea sample collected from Monterey Bay in California [62]. Thus, the nomenclature of this protein, i.e., “proteo-,” originates from the name of the hosting bacterium. Sequencing of a bacterial artificial chromosome vector into which a fragmented DNA extracted from samples was cloned revealed the presence of a gene encoding rhodopsin-like protein (EBAC31A08) [62]. Furthermore, after transformation by this gene and successive induction of protein expression with exogenous retinal in
PR-related proteins were also discovered from non-marine bacteria present in various environments, such as freshwater [76], high mountains [77], hot springs [78], and permafrost [79]. For example, a PR-like protein identified from actinobacteria living in freshwater is called actinorhodopsin (ActR) because it is classified into a phylogenetically different clade from PR [76]. A halophilic eubacterium
In 1999, the presence of a gene encoding eukaryotic microbial rhodopsin (
Phylogenetic tree of microbial rhodopsins. RpActR represents ActR from actinobacterium Rhodoluna planktonica strain MWH-Dar1.
When the molecular mechanism of microbial H+-pumping rhodopsins is considered, the scenario of proton transportation in BR is often used as a prototype. Detailed descriptions of the H+-pumping mechanism of BR from various aspects can be found in excellent previously published reviews (refer to relevant refs. [32, 33, 43, 44, 45, 46, 47, 48]). We present only a brief outline here.
The photocycle of BR is initiated by photoisomerization of the retinal from all-
Amino-acid alignment of various microbial H+-pumping rhodopsins. Analysis was performed using a multiple sequence alignment program (CLUSTALW). The numbers shown in the top row represent the numbering of amino acid residues in BR. The dotted line represents the missing residues in the determined structure. The amino acid residues with maximum homological numbers at each position are marked with a black or gray background depending on their numbers: The monochrome tone becomes darker as the number of homological residues increases. Notes: cR-2, cR from Haloarcula sp. arg-2; cR-3, cR from Haloarcula vallismortis; dR-2, dR from Haloterrigena turkmenica JCM9743; dR-3, dR from Haloterrigena thermotolerans; GPR, γ-proteobacterium (EBAC31A08) GPR; BPR, γ-proteobacterium (Hot75m4) BPR; ActR, RpActR.
A proton releasing complex (PRC) comprising several internal H2O and various residues on the EC surface such as Tyr57BR, Arg82BR, Tyr83BR, Ser193BR, Glu194BR, Glu204BR, and Thr205BR also participates in the proton transfer reaction of BR [98, 99], although it is not always an indispensable component for proton pumping. The p
Two threonine residues, Thr89BR and Thr46BR, are also important, although these residues do not belong to the series of proton transfer events due to nonionizable residues. Thr89BR is within the active center and includes PSB, Asp85BR, and some water molecules [102], where this residue forms a hydrogen bond with Asp85BR [103], indirectly contributing to the initial proton transfer from PSB to Asp85BR during M-formation [102, 103]. In contrast, Thr46BR forms an interhelical hydrogen bond with Asp96BR in the CP region, which is associated with the regulation of p
In most outward H+-pumping microbial rhodopsins identified to date, the residues corresponding to three main groups (PSB [Lys216BR as the retinal binding site], Asp85BR, and Asp96BR) described above are highly conserved. By checking their presence, we can therefore forecast whether each protein in the microbial rhodopsin family acts as an H+-pump like BR. Figure 2 shows a comparison between important amino acid residues for proton transport among representative H+-pumping rhodopsins. As shown in this figure, almost all primal residues relevant to proton transport in archaeal-type H+-pumps agree with the residues corresponding to BR. Similarly, both fungal and algal H+-pumps from eukaryotes retain the residues corresponding to Asp85BR and Asp96BR; however, a difference exists in the components of PRC in BR. In both types of eukaryotic H+-pumps, the residue corresponding to Glu194BR of two EC glutamates in PRC is replaced by glycine, whereas another residue corresponding to Glu204BR is conserved. In contrast, in the eubacterial H+-pump, the residues corresponding to Asp96BR are substituted by conservative carboxylate glutamic acid, although there are several exceptions. Another significant aspartate corresponding to Asp85BR is perfectly conserved, similar to other types of H+-pumps. Furthermore, these H+-pumps lack both glutamic acids in the components of PRC: Glu194BR and Glu204BR. Thus, a comparison of the amino acid sequences among various H+-pumping rhodopsins can reveal the superconservation of the proton acceptor (Asp85BR) and the diversity of the proton donor (Asp96BR) and the residues in the EC proton releasing pathway. These differences could lead to different methods of proton transfer among varying H+-pumps.
During a single photocycle induced by the absorption of one photon, ion-pump-type rhodopsins can transport ions as substrates. The number of photocycle turnover under illumination, therefore, affects the amount of ions transported by these proteins, in other words, the ion-pumping activity of these rhodopsins. In general, the turnover rate of the photocycle in ion-pumping rhodopsins tends to be relatively higher than those of photosensor-type rhodopsins to transport numerous ions per illumination. The speed of their photocycle completion can be used to analyze the H+-pump, in addition to actually measuring H+-pumping activity that is usually examined by measuring the photoinduced pH change in a suspension of cells expressing these rhodopsins. Furthermore, the identification of photointermediates during the photocycle of respective rhodopsins and the estimation of their rise/decay kinetics together with the measurement of transient proton transfer during their photocycles enable us to understand the timing of proton movement. Thus, detailed investigations of the photocycles are important for understanding the H+-pumping mechanism.
Among the H+-pumping rhodopsins identified so far, the next well-characterized proton pump following BR is GPR. In many studies, the first identified PR variant (EBAC31A08) was employed as a sample. As soon as GPR was discovered in 2000, various spectroscopic approaches such as static and time-resolved transient UV–visible, FTIR, and FT-Raman spectroscopies were applied to characterize the photochemistry of this protein, as previously performed for the research of BR [105, 106, 107, 108, 109, 110]. These experimental results revealed that the photocycle of GPR was similar to that of BR but also concomitantly contained several differences. Using the same kinetically analytical method as previously applied to the transient absorbance data of BR, where the possibilities of parallel or branch models were also considered [111], Váró et al. determined the photocycles of GPR at acidic and alkaline pH values [108, 109]. Their proposed photocycle at alkaline pH (9.5) is in accordance with the following scheme: GPR → K↔M1 → M2↔N↔GPR’(O) → GPR [108]. As shown in the above scheme, one of the apparent differences from the BR photocycle is the absence of L after K, which is thought to be probably due to kinetic reasons. A remarkably retarded (ca. 10-100-fold slower) decay of K compared with that of BR was observed in GPR [105]. Because of such slow K-decay, low-temperature Raman spectroscopic data presented by Fujisawa et al. demonstrated that the chromophore structure in GPR in the K state is less distorted compared to that of BR in the same state and is rather close to that of L in BR, which possess a more relaxed chromophore structure [112]. Therefore, the formation of a longer stable K state may obscure the appearance of L in the GPR along with the fast formation of the following M-state. Another difference from BR can be observed in the spectral characteristics of the latter photoproducts, N and GPR’(O). The N-intermediate in PR was red-shifted with 13-
The photocycles of other eubacterial H+-pumping rhodopsins, including XR, GR, ESR, and ActR, were also investigated by time-resolved absorption spectroscopy [80, 83, 114, 115, 116]. Their photocycles go through the K, L, M, N, and O states, similar to BR or GPR. For many eubacterial H+-pumps including GPR, structural information obtained by multiple approaches such as X-ray crystallography, NMR, and atomic force microscopy has also been reported [117, 118, 119, 120, 121, 122, 123], providing structural insights into their photochemistry.
Recent genome analysis revealed that numerous eukaryotic fungi possess rhodopsin-like protein-encoding genes (RDs) and opsin-related genes (ORPs) [124]. Nevertheless, unlike archaeal or bacterial H+-pumping rhodopsins, reports on the photochemistry of eukaryotic H+-pumps are extremely limited because the protein expression in
For two algal H+-pumps, ARI and ARII, the establishment of a large-scale sample preparation method using a unique
As described above, the proton acceptor residue from PSB corresponding to Asp85BR is superconserved in all H+-pump-type rhodopsins, suggesting the significance of this residue in the proton pumping mechanism. The negative charge of deprotonated Asp85BR interacts with another deprotonated aspartate Asp212BR and three water molecules through hydrogen bonds, forming a pentagonal cluster that electrostatically stabilizes two positive charges of PSB and Arg82BR [47]. The same cluster structure has also been observed in H+-pumping rhodopsins other than BR [22, 131]. In this sense, two aspartates also play an important role in counterions to PSB, in which Asp85BR and Asp212BR are referred to as primary and secondary counterions, respectively. The aspartate residue, which is the proton acceptor, is deprotonated in the unphotolyzed state under physiological conditions. At pH values below the p
In contrast, the p
The primary and secondary counterions (corresponding to Asp85BR and Asp212BR, respectively) are located near and arranged symmetrically around the PSB, resulting in forming a part of the proton acceptor cluster. The secondary counterion is also deprotonated like the primary counterion (proton acceptor) because the p
In contrast, a question that could arise would be how p
Through low-temperature FTIR experiments, it was suggested that PSB forms a stronger hydrogen bond with Asp227GPR rather than Asp97GPR within the pentagonal cluster around PSB upon K-formation [144]. In addition to this observation, the p
Following the EC proton transfer in the first half of the photocycle, the CP proton transfer events via the SB proton donor in the second half of the photocycle after M-decay are the next critical steps. The proton transfer mechanism at this stage varies among the three types of H+-pumping rhodopsins—archaeal, bacterial, and eukaryotic. In the latter half of the BR photocycle, the deprotonated SB first accepts a proton from its proton donor, Asp96BR, located in the CP channel during the M–N transition. The p
As described above, in GPR, the residue corresponding to Asp96BR is the conservative carboxylate, Glu108GPR. This residue can function as a proton donor to SB; however, the proton movement from Glu108GPR to SB and the subsequent reprotonation of Glu108GPR from the CP bulk are indistinguishable, unlike BR; two sequential proton transfer events in the CP channel concurrently take place upon the M–N transition [105]. The difference in CP proton migration in eubacterial H+-pumps, including PR from BR, seems to be related to the difference in the environment around the proton donor in the intracellular part of the protein between them. In many eubacterial H+-pumping rhodopsins, the interhelical hydrogen bonding pair corresponding to the Asp-Thr interaction in BR is replaced by the Glu-Ser interaction. The X-ray crystal structure of XR in the dark state revealed that the proton donor (Glu107XR) in the CP channel connects to the peptide carbonyl of the lysine residue (Lys240XR) in SB; therefore, the CP H-bonded chain via water is already formed in the unphotolyzed state [118]. Thus, the difference in the CP proton transfer scheme from BR may be due to the formation of the hydrophilic CP pathway in eubacterial H+-pumps.
We also observed a further interesting characteristic in the CP proton transfer of the PR-like H+-pump ESR. The residue positioned at the site of the proton donor in ESR is the cationic residue Lys96ESR (see Figure 2). Nevertheless, Lys96ESR seems to be involved in the CP proton transfer from the intracellular aqueous space to the inner deprotonated SB because the replacement of this residue by other nonionizable residues resulted in a significant delay of the M-intermediate [114]. This observation exploded a conventional concept, the so-called carboxyl rule, that the functional proton-donating residue is confined to two carboxylates (Asp or Glu). Some distinct structural features of BR can be observed in the X-ray crystal structure of the ESR. One of the differences is the presence of a cavity around Lys96ESR located close to the CP bulk media [122]. Although Lys96ESR is surrounded by hydrophobic residues in the CP channel in the dark state similar to BR, the cavity in the vicinity of Lys96ESR is separated only by a polar side chain of Thr43ESR (corresponding to Phe42BR), in contrast to BR, whose proton donor residue is completely separated from the CP bulk solvent by a hydrophobic barrier composed of multiple hydrophobic residues including Phe42BR [122]. Connectivity with the CP bulk facilitates direct access of the protons from the CP solvent in Lys96ESR. Another difference is the flexibility of the side chain of Lys96ESR, which may allow the smooth repositioning of this residue by donating to SB and reprotonation. Given that these structural properties are present in the CP region together with the time-resolved spectroscopic data using D2O, it may be plausible that the CP proton transfer scheme in ESR is as follows [114]: Lys96ESR adopts an unprotonated form at the resting state to be buried within the hydrophobic CP region. Upon M-decay, Lys96ESR transiently catches a proton from the CP bulk solvent (at M1↔M2), and then, a little later, it donates a proton to SB (at M2↔N1). Hence, Lys96ESR acts as a residue facilitating proton delivery from the CP bulk to the SB, which is an apparently different proton donating mechanism from the conventional one.
Another unique example of CP proton transfer was found in two types of gram-negative rod-shaped Proteobacteria in soil:
Among eukaryotic H+-pumps, both fungal and algal H+-pumps possess the same proton donor aspartate residue as BR. For two algal H+-pump homologs ARI and ARII, however, the residue corresponding to Thr46BR is replaced by asparagine, which may cause different interactions with the proton donor and its p
pKa estimation of critical residues for a proton pump by the SnO2 (or ITO) electrode method. (A) Photoinduced voltage changes representing proton uptake/release at varying pH values [
Among the three photointermediates M, N, and O produced in the latter half of the photocycle in H+-pumping rhodopsins, two spectrally silent substates are known for each photoproduct [33, 132]. Because the transitions between these substates occur without apparent spectral changes, they are usually observed by kinetic analysis for transient absorbance changes measured using various spectroscopic techniques. Three critical events for proton translocation occur during these silent transitions. As is known in BR, the first crucial event was observed upon the transition between two successive M-states, M1 and M2, which is accompanied by the accessibility switch of SB from the EC side to the CP side. This switching is important for unidirectional proton transport because it causes the conversion of the direction of proton movement from toward EC at M to toward CP at N.
The second event occurs during the N1-to-N2 transition, where the accessibility of the proton donor changes. In BR, the proton donor Asp96BR connects to the SB but not the CP bulk during the M–N transition, thus hampering the misdirected transfer of a proton of Asp96BR toward the CP solvent. Then, the connection of Asp96BR to SB is switched toward the CP side upon the N1–N2 transition, facilitating the reprotonation of Asp96BR from the CP surface [33, 45]. Although the detailed mechanism of this accessibility switch upon N1–N2 transition remains incompletely understood, even in the most well-known BR, a previous computational study by Wang et al. proposed a model in which the further opening of the proton uptake pathway in the CP channel, which remains closed even in the M-state with the opening of the F-helix by the presence of a hydrophobic barrier composed of Phe42BR and multiple other hydrophobic residues, is triggered by the deprotonation of Asp96BR during the M–N transition, leading to the connection of Asp96BR to the CP aqueous space [155]. In contrast, for the algal H+-pump ARII, it was presumed that the change in the unique interhelical interaction between Asp92ARII and Cys218ARII located in the CP domain acts as a switch for opening the gate of the CP channel for H+-uptake [133].
In contrast to M and N, the molecular events in the O-state have not been completely examined because the stable trapping of O produced in the latter stages of the photocycle is difficult. In the early stages of studies on BR, Haupts et al. hypothesized that during the N–O transition, the reisomerization of the retinal from the 13-
As described above, PRC located on the EC surface is not necessarily indispensable for proton pumping because of the presence of a PRC-deficient type (eubacterial or eukaryotic) H+-pumping rhodopsins, although PRC alters the timing of proton release during the photocycle. The replacement of either Glu194BR, Glu204BR, or both by nonionizable residues, however, caused a delay in O-decay with a late proton release from the protonated Asp85BR toward the EC surface as well as the absence of the initial proton release upon the L–M transition. In addition, when the residues corresponding to three of PRC-constituting residues (Ser193BR, Glu194BR, and Thr205BR) in a sensory-type rhodopsin from
As described previously, sequential proton transfer events during the photocycles in various microbial H+-pumping rhodopsins, including BR, are successfully accomplished by regulating rigorous p
As a method for measuring proton movement transiently occurring during the photocycles of these pigments, the conventional method of using various pH-indicator dyes is frequently employed [44]. This method is highly time-resolved because the transient pH changes of the media with photoinduced proton uptake and release in rhodopsins are monitored based on the real-time transient absorbance changes of these pH-sensitive dyes in the sample suspension. The use of this method, therefore, enables us to precisely identify the timing of proton uptake and release together with the rise and decay kinetics of photoproducts. However, the pH range for measurement is confined to the pH values around its p
Schematic representation of the photocycle and accompanying proton transfer of three types of H+-pumping rhodopsins. (A) Schematic diagram of the photochemistry of BR. The stepwise proton transfer reactions are depicted by thin blue arrows and overlaid on the crystal structure of BR at the dark state (PDB 1c3w). The timing of H+-release differs depending on pH values. The expected configuration changes of chromophore retinal (RET) and PSB in each photocycle intermediate are also depicted. (B) Summary of pKa changes in the residues participating in the proton transfer reactions during the photocycle. A transient pKa increase and decrease of respective residues upon each transition are shown in upward and downward thin arrows. The reverse of pKa values between two adjacent residues leads to a unidirectional proton movement from a (protonated) residue with a lowered pKa value to another (unprotonated) residue with an elevated pKa value. Such proton migrations are expressed in thick blue arrows. The values in parentheses represent our previous estimated pKa values by the SnO2 electrode method [
As described at the beginning of this chapter, outward H+-pumping microbial rhodopsins can evoke stronger light-induced neural suppression and quicker recovery from the inactivated state formed upon illumination than inward Cl−-pump HRs. Hence, optical neural control using H+-pumping rhodopsins may also be an effective alternative for optogenetics, although neural inhibition with light-gated anion channel ACRs has recently attracted attention. The rational design based on the functional molecular basis of these rhodopsins described in this chapter may allow the creation of “neo-type” H+-pumping microbial rhodopsins by introducing several mutations to further enhance the effect of neural silencing upon illumination, resulting in the acceleration of the development of more efficient tools for optogenetics along with developing color variants with various spectral properties. Further increases in protein expression and stability in targeted neural cells could also lead to the improvement of optogenetic tools. For this purpose, taking advantage of the abundance of these H+-pumping rhodopsins, the exploration of new microbial H+-pumping rhodopsins with novel properties (e.g., high thermal stability [165, 166]) from nature may be useful for producing mutants.
In addition, studies on H+-pumping microbial rhodopsins are required to develop novel optical cellular control methods because these types of pigments can simultaneously induce alkalization of the intracellular pH by illumination-induced outward proton transport. As is generally known, the maintenance of an appropriate cellular pH is necessary to ensure that each requisite enzyme for various biological reactions functions properly. Because the drainage of acids produced by cellular metabolism is controlled through the Na+/H+ antiporter or the Cl−/HCO3− exchanger to maintain the cellular pH near neutral, failure in these transporting systems affects the normal function of cells. Therefore, the application of optogenetics to cells with abnormal pH values, that is, light-induced manipulation of the cells specifically expressing H+-pumping microbial rhodopsins, may allow the restoration of the functions of these cells. As an example of intracellular pH regulation by optogenetics, Matsui et al. reported that the photoinduced intracellular pH increase in glial cells expressing aR-3 (Arch) suppressed the release of glutamate from these cells, which was triggered by glial acidosis upon brain ischemia, thereby ameliorating the effects of ischemic brain damage [167]. Moreover, the optical regulation of the function of varying organelles expressing H+-pumping rhodopsins has recently been attempted. Rost et al. demonstrated that selective Arch expression on synaptic vesicles together with a pH-sensitive indicator and successive illumination led to vesicular acidification via Arch instead of vacuolar-type H+-ATPases (V-ATPases), enabling neurotransmitter accumulation within synaptic vesicles driven by the proton motive force (PMF) generated through light-activated Arch [168]. In addition, Hara et al. achieved dR-2-mediated optical partial suppression of cell death induced by the inhibition of respiratory PMF generation in the mitochondria of mammalian cells [169]. More recently, a method for topological inversion of microbial rhodopsins as optogenetic tools was also developed [170]. Hence, the application of this technique together with the use of recently discovered natural inward H+-pumping rhodopsins [171, 172] as optogenetic tools may allow the induction of both light-activated acidification and alkalization in various types of cells or organelles such as mitochondria, vesicles, and lysosomes. Hence, the combination of an outward H+-pumping rhodopsin and the topological reversal technique described above may allow various types of optogenetics. For instance, the use of outward H+-pumping rhodopsin might lead to the following optogenetics: in general, the pH values of lysosomes in normal cells are regulated to be approximately 5, whereas those of lysosomes in cancer cells with acquired resistance to carcinostatic agents tend to be lower [173, 174]. The efficacy of carcinostatic agents for these cancer cells is degraded because they get trapped in acidified organelles; therefore, specific expression of H+-pumping rhodopsins in lysosomes of drug-resistant cancer cells and optical pH control (photoinduced alkalization) of these cellular organelles might lead to the restoration of the original effect of drugs. Thus, optogenetics using H+-pumping microbial rhodopsins may lead to the establishment of new optical therapies in the future.
Proton pump-type microbial rhodopsins are not only effective neural suppressors but also optical tools for pH control of various cells or organelles that specifically incorporate these pigments, which makes them a dual optogenetic tool. Rational protein engineering based on molecular mechanisms is required to further develop these rhodopsins into more effective tools. Considering the photochemical reaction and accompanying proton transfer mechanism in various H+-pumping rhodopsins described previously, mutations that increase their photocycle kinetics may be effective for enhancing the respective H+-pumping abilities. To increase their H+-pumping efficiency via their photocycles, for example, a mutation that lowers the p
The authors declare no competing financial interests.
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In particular, the main classes of soil pollutants in Europe (heavy metals, mineral oils, polycyclic aromatic hydrocarbons (PAHs), monoaromatic hydrocarbons, phenols and chlorinated hydrocarbons (CHCs)), together with the emerging contaminants (i.e. endocrine-disrupting chemicals (EDCs) and pharmaceutical-personal care products (PPCPs)) are considered. A description of the fungal species (saprotrophic and biotrophic basidiomycetes) and biodegradative extracellular (laccases and class II peroxidases) and intracellular (cytochrome P450 monooxygenases and glutathione transferases) enzyme classes is reported. Moreover, the chemical-physical parameters that influence the biodegradation process are examined, and the biostimulation and bioaugmentation strategies are described. A specific attention is paid to the microcosm studies, at the laboratory scale, which are an essential approach to evaluate the feasibility of a biodegradation process.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Francesca Bosco and Chiara Mollea",authors:[{id:"93865",title:"Dr.",name:"Francesca",middleName:null,surname:"Bosco",slug:"francesca-bosco",fullName:"Francesca Bosco"},{id:"96159",title:"Dr.",name:"Chiara",middleName:null,surname:"Mollea",slug:"chiara-mollea",fullName:"Chiara Mollea"}]},{id:"68347",doi:"10.5772/intechopen.88339",title:"Bioremediation of Heavy Metals",slug:"bioremediation-of-heavy-metals",totalDownloads:1508,totalCrossrefCites:4,totalDimensionsCites:9,abstract:"Exposure to lead (Pb), zinc (Zn), cadmium (Cd), copper (Cu), and selenite (SeO3−2) consider the main heavy metals that threat human health. These heavy metals can interfere with the function of vital cellular components. Soil heavy metal contamination represents risks to humans and the ecosystem through drinking of contaminated groundwater, direct ingestion or the food chain, and reduction in food quality. Bioremediation means cleanup of polluted environment via transformation of toxic heavy metals into less toxic form by microbes or its enzymes. Otherwise, bioremediation by microbes has limitations like production of toxic metabolites. The efflux of metal ions outside the cell, biosorption to the cell walls and entrapment in extracellular capsules, precipitation, and reduction of the heavy metal ions to a less toxic state are mechanisms to metals’ resistance.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Medhat Rehan and Abdullah S. Alsohim",authors:[{id:"175766",title:"Dr.",name:"Medhat",middleName:null,surname:"Rehan",slug:"medhat-rehan",fullName:"Medhat Rehan"}]},{id:"68268",doi:"10.5772/intechopen.88207",title:"Arsenic Phytoremediation: Finally a Feasible Approach in the Near Future",slug:"arsenic-phytoremediation-finally-a-feasible-approach-in-the-near-future",totalDownloads:1097,totalCrossrefCites:2,totalDimensionsCites:8,abstract:"Arsenic, a class-1 carcinogenic, is a ubiquitous metalloid found in the atmosphere, soils, natural waters, and organisms. The World Health Organization (WHO) estimates that hundred million people worldwide might be chronically exposed to arsenic in drinking water at concentrations above the safety standard. Conventionally applied techniques to remove arsenic species show low removal efficiency, high operational costs, and high-energy requirements. The biological methods, especially phytoremediation, could be cost-effective for protecting human health and the environment from toxic metal contamination. Plants, as sessile organisms, have developed an extraordinary capacity to tolerate arsenic through three main strategies: uptake repression, sequestration into the vacuole, or extrusion. Therefore, arsenic perception and tolerance require a coordinated response that involves arsenic transporters, extrusion pumps, vacuole transporters, and the activation of the phytochelatin biosynthetic pathway. For phytoremediation to become a feasible strategy for arsenic removal from contaminated sites, it is essential to completely understand the molecular mechanisms of arsenic uptake, extrusion, and sequestration, as well as how this response is coordinated. The new genome-wide technologies provide a unique opportunity to understand the molecular mechanisms underlying arsenic perception and accumulation in plants that will open up new possibilities for phytoremediation of arsenic-contaminated waters and soils.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Cristian Mateo, Micaela Navarro, Cristina Navarro and Antonio Leyva",authors:null},{id:"69539",doi:"10.5772/intechopen.84208",title:"Greenhouse Gas Emissions of Agriculture: A Comparative Analysis",slug:"greenhouse-gas-emissions-of-agriculture-a-comparative-analysis",totalDownloads:735,totalCrossrefCites:1,totalDimensionsCites:6,abstract:"Greenhouse gas emissions are accounted by greenhouse gases inventories, which must be produced by common accounting rules, called Guidelines, which are endorsed by the United Nations Framework Convention on Climate Change (UNFCCC). These inventories are fundamental to analyze the impact of agriculture on emissions, and as example of the difficulty and complexity of implementation of the guidelines, a comparative study is made on emissions from Agricultural Soil Management (CRF category 3D source) utilizing biological nitrogen fixation. The analysis carried out for the N2O emissions under this section of the agrarian sector of Spain, Europe, New Zealand, Canada and the USA, inventories and national communications from Argentina and Brazil permit to observe the wide spectrum of approaches and the importance of the management of the accounting rules to be used mainly if we need that the impact of mitigation policies are captured in a direct way by the inventory. New technologies could introduce changes in the rules and can be utilized for reducing emissions, and examples are also analyzed.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Dionisio Rodríguez",authors:null},{id:"65795",doi:"10.5772/intechopen.84548",title:"Progressive Research in the Molecular Mechanisms of Chronic Fluorosis",slug:"progressive-research-in-the-molecular-mechanisms-of-chronic-fluorosis",totalDownloads:1126,totalCrossrefCites:2,totalDimensionsCites:3,abstract:"Long-term excessive intake of fluoride (F) leads to chronic fluorosis, resulting in dental fluorosis and skeletal fluorosis. Chronic exposure to high doses of fluoride can also cause damage to soft tissues, especially when it passes through the blood-brain, blood-testis, and blood-placenta barrier, causing damage to the corresponding tissues. Fluorosis has become a public health problem in some countries or regions around the world. Understanding the pathogenesis of fluorosis is very important. Although the exact mechanism of fluorosis has not been fully elucidated, various mechanisms of fluoride-induced toxicity have been proposed. In this chapter, we will introduce the research progress of the mechanism of fluorosis, focusing on dental fluorosis, skeletal fluorosis, nervous and reproductive system toxicity, and influential factors related to fluoride toxicity (i.e., genetic background, co-exposure with other element). In addition, the application of proteomics and metabolomics in the study of the pathogenesis of fluorosis is also introduced. Currently, there is still no specific treatment for fluorosis. However, since fluorosis is caused by excessive intake of fluoride, avoiding excessive fluoride intake is the critical measure to prevent the disease. In endemic regions, health education and supplement diet with vitamins C, D and E, and calcium and antioxidant compounds are important.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Liming Shen, Chengyun Feng, Sijian Xia, Yan Wei, Hua Zhang, Danqing Zhao, Fang Yao, Xukun Liu, Yuxi Zhao and Huajie Zhang",authors:null}],mostDownloadedChaptersLast30Days:[{id:"68347",title:"Bioremediation of Heavy Metals",slug:"bioremediation-of-heavy-metals",totalDownloads:1508,totalCrossrefCites:4,totalDimensionsCites:9,abstract:"Exposure to lead (Pb), zinc (Zn), cadmium (Cd), copper (Cu), and selenite (SeO3−2) consider the main heavy metals that threat human health. These heavy metals can interfere with the function of vital cellular components. Soil heavy metal contamination represents risks to humans and the ecosystem through drinking of contaminated groundwater, direct ingestion or the food chain, and reduction in food quality. Bioremediation means cleanup of polluted environment via transformation of toxic heavy metals into less toxic form by microbes or its enzymes. Otherwise, bioremediation by microbes has limitations like production of toxic metabolites. The efflux of metal ions outside the cell, biosorption to the cell walls and entrapment in extracellular capsules, precipitation, and reduction of the heavy metal ions to a less toxic state are mechanisms to metals’ resistance.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Medhat Rehan and Abdullah S. Alsohim",authors:[{id:"175766",title:"Dr.",name:"Medhat",middleName:null,surname:"Rehan",slug:"medhat-rehan",fullName:"Medhat Rehan"}]},{id:"68504",title:"Biological Remediation of Phenoxy Herbicide-Contaminated Environments",slug:"biological-remediation-of-phenoxy-herbicide-contaminated-environments",totalDownloads:1008,totalCrossrefCites:2,totalDimensionsCites:2,abstract:"Phenoxy herbicides such as 2,4-dichlorophenoxyacetic acid (2,4-D) and 2-methyl-4-chlorophenoxyacetic acid (MCPA) are widely used in agriculture to control broadleaf weeds. Although their application has helped to increase the yield and value of crops, they are also recognized as a source of emerging environmental contamination. Their extensive use may promote contamination of soil, surface, and groundwater and lead to increased inhibition of plant development and soil toxicity. Hence, there is an urgent need to identify nature-based methods based on appropriate biological remediation techniques, such as bio-, phyto-, and rhizoremediation, that enable the effective elimination of phenoxy herbicides from the environment. Bioremediation typically harnesses microorganisms and their ability to utilize recalcitrant contaminants in complete degradation processes, while phytoremediation is a cost-effective, environmentally friendly strategy that uses plants to transform or mineralize xenobiotics to less or nontoxic compounds. Rhizoremediation (microbe-assisted phytoremediation), in turn, is based on the interactions between plant roots, root exudates enriched in plant secondary metabolites, soil, and microorganisms. Based on the above, this chapter presents current knowledge on the properties of phenoxy herbicides, as well as the concentrations detected in the environment, their toxicity, and the biological remediation techniques used for safe removal of the compounds of interest from the environment.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Magdalena Urbaniak and Elżbieta Mierzejewska",authors:null},{id:"70249",title:"Bioremediation of Petroleum-Contaminated Soil",slug:"bioremediation-of-petroleum-contaminated-soil",totalDownloads:1137,totalCrossrefCites:1,totalDimensionsCites:2,abstract:"Petroleum is not only an important energy resource to boost the economic development, but also a major pollutant of the soil. The toxicity of petroleum can cause a negative impact on ecosystem, as well as the negative effects related to its carcinogenic for both animals and humans. In the present study, bioremediation as an alternative tool for restoration petroleum-contaminated soils was set forth, and focusing on the phytoremediatior plants, petroleum-biodegradable microorganism are responsible for the biodegradation of petroleum. In the present chapter, the bioremediation of petroleum-contaminated soil, as well as the influence factors of bioremediation are elaborated based on the recently studies. This will provide a novel understanding on bioremediation and help improve strategies for petroleum-contaminated soils remediation.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Shuisen Chen and Ming Zhong",authors:null},{id:"63252",title:"Adsorptive Removal of Fluoride onto Different Waste Materials: Orange Juice Residue, Waste Seaweed, and Spent Cation-Exchange Resin",slug:"adsorptive-removal-of-fluoride-onto-different-waste-materials-orange-juice-residue-waste-seaweed-and",totalDownloads:1084,totalCrossrefCites:0,totalDimensionsCites:0,abstract:"To effectively use waste materials in developing a sustainable society, adsorbents for removing trace or low concentrations of fluoride, which is difficult to be removed by conventional techniques, were prepared from three waste materials: orange juice residue, waste sea weed, and spent cation exchange resin. These adsorbents were loaded with tri- or tetravalent metal ions such as iron(III) and zirconium(IV), of which zirconium(IV) was found to be most suitable as the loaded metal ion. From the pH effect on adsorption, the adsorption mechanism was inferred, and adsorption and desorption was found to be controlled by changing pH values. The maximum adsorption capacities on zirconium(IV)-loaded orange juice residue, waste sea weed, and spent cation exchange resin were evaluated as 33.1, 18.1, and 37.6 mg/g, respectively, which were higher than those of most other adsorbents reported in literatures. They exhibited high selectivity for fluoride over other anionic species and high durability. Tests to remove trace concentrations of fluoride from actual waste plating solutions revealed that the concentration could be reduced below the acceptable level using small amounts of these adsorbents, i.e., it was reduced lower than 1.5 mg/dm3 (WHO standard) by adding 1 g of the adsorbents into 1 dm3 test solution.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Katsutoshi Inoue, Hari Paudyal, Hidetaka Kawakita and Keisuke Ohto",authors:null},{id:"63393",title:"Characterization of the Youssoufia-Morocco-MineFluoride-Contaminated Water and Their Detrimental Effects on Human Health",slug:"characterization-of-the-youssoufia-morocco-minefluoride-contaminated-water-and-their-detrimental-eff",totalDownloads:852,totalCrossrefCites:1,totalDimensionsCites:2,abstract:"In Youssoufia, the second phosphate mining center of our country (Morocco), the drinking water needs of the rural population are of underground origins. Indeed, most of Youssoufia’s rural areas feed on traditional wells. The main purpose of this chapter is to evaluate the degree of contamination of mine water along the pumping canal by fluoride. Wells located near this channel were also analyzed to see the influence of the existence of black phosphate in this region on these wells. At the end of this analytical part, it is obvious to conclude that the dewatering waters of the black phosphate mines of Youssoufia, known as dewatering water along the canal, contain significant fluoride concentrations in the order of 3–4 mg/l on average and the waters of the wells located near this canal have fluoride concentrations higher than the standard recommended by the National Office of Drinking Water in Morocco and the World Health Organization which is 1.5 mg/l. Indeed, a number of residents residing in Youssoufia suffer from fluorosis.",book:{id:"8796",slug:"environmental-chemistry-and-recent-pollution-control-approaches",title:"Environmental Chemistry and Recent Pollution Control Approaches",fullTitle:"Environmental Chemistry and Recent Pollution Control Approaches"},signatures:"Moufti Ahmed",authors:null}],onlineFirstChaptersFilter:{topicId:"887",limit:6,offset:0},onlineFirstChaptersCollection:[],onlineFirstChaptersTotal:0},preDownload:{success:null,errors:{}},subscriptionForm:{success:null,errors:{}},aboutIntechopen:{},privacyPolicy:{},peerReviewing:{},howOpenAccessPublishingWithIntechopenWorks:{},sponsorshipBooks:{sponsorshipBooks:[],offset:8,limit:8,total:0},allSeries:{pteSeriesList:[{id:"14",title:"Artificial Intelligence",numberOfPublishedBooks:9,numberOfPublishedChapters:89,numberOfOpenTopics:6,numberOfUpcomingTopics:0,issn:"2633-1403",doi:"10.5772/intechopen.79920",isOpenForSubmission:!0},{id:"7",title:"Biomedical Engineering",numberOfPublishedBooks:12,numberOfPublishedChapters:104,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2631-5343",doi:"10.5772/intechopen.71985",isOpenForSubmission:!0}],lsSeriesList:[{id:"11",title:"Biochemistry",numberOfPublishedBooks:31,numberOfPublishedChapters:314,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2632-0983",doi:"10.5772/intechopen.72877",isOpenForSubmission:!0},{id:"25",title:"Environmental Sciences",numberOfPublishedBooks:1,numberOfPublishedChapters:11,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2754-6713",doi:"10.5772/intechopen.100362",isOpenForSubmission:!0},{id:"10",title:"Physiology",numberOfPublishedBooks:11,numberOfPublishedChapters:141,numberOfOpenTopics:4,numberOfUpcomingTopics:0,issn:"2631-8261",doi:"10.5772/intechopen.72796",isOpenForSubmission:!0}],hsSeriesList:[{id:"3",title:"Dentistry",numberOfPublishedBooks:8,numberOfPublishedChapters:129,numberOfOpenTopics:2,numberOfUpcomingTopics:0,issn:"2631-6218",doi:"10.5772/intechopen.71199",isOpenForSubmission:!0},{id:"6",title:"Infectious Diseases",numberOfPublishedBooks:13,numberOfPublishedChapters:113,numberOfOpenTopics:3,numberOfUpcomingTopics:1,issn:"2631-6188",doi:"10.5772/intechopen.71852",isOpenForSubmission:!0},{id:"13",title:"Veterinary Medicine and Science",numberOfPublishedBooks:11,numberOfPublishedChapters:105,numberOfOpenTopics:3,numberOfUpcomingTopics:0,issn:"2632-0517",doi:"10.5772/intechopen.73681",isOpenForSubmission:!0}],sshSeriesList:[{id:"22",title:"Business, Management and Economics",numberOfPublishedBooks:1,numberOfPublishedChapters:18,numberOfOpenTopics:2,numberOfUpcomingTopics:1,issn:"2753-894X",doi:"10.5772/intechopen.100359",isOpenForSubmission:!0},{id:"23",title:"Education and Human Development",numberOfPublishedBooks:0,numberOfPublishedChapters:5,numberOfOpenTopics:1,numberOfUpcomingTopics:1,issn:null,doi:"10.5772/intechopen.100360",isOpenForSubmission:!0},{id:"24",title:"Sustainable Development",numberOfPublishedBooks:0,numberOfPublishedChapters:14,numberOfOpenTopics:5,numberOfUpcomingTopics:0,issn:null,doi:"10.5772/intechopen.100361",isOpenForSubmission:!0}],testimonialsList:[{id:"13",text:"The collaboration with and support of the technical staff of IntechOpen is fantastic. The whole process of submitting an article and editing of the submitted article goes extremely smooth and fast, the number of reads and downloads of chapters is high, and the contributions are also frequently cited.",author:{id:"55578",name:"Antonio",surname:"Jurado-Navas",institutionString:null,profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRisIQAS/Profile_Picture_1626166543950",slug:"antonio-jurado-navas",institution:{id:"720",name:"University of Malaga",country:{id:null,name:"Spain"}}}},{id:"6",text:"It is great to work with the IntechOpen to produce a worthwhile collection of research that also becomes a great educational resource and guide for future research endeavors.",author:{id:"259298",name:"Edward",surname:"Narayan",institutionString:null,profilePictureURL:"https://mts.intechopen.com/storage/users/259298/images/system/259298.jpeg",slug:"edward-narayan",institution:{id:"3",name:"University of Queensland",country:{id:null,name:"Australia"}}}}]},series:{item:{id:"14",title:"Artificial Intelligence",doi:"10.5772/intechopen.79920",issn:"2633-1403",scope:"Artificial Intelligence (AI) is a rapidly developing multidisciplinary research area that aims to solve increasingly complex problems. In today's highly integrated world, AI promises to become a robust and powerful means for obtaining solutions to previously unsolvable problems. This Series is intended for researchers and students alike interested in this fascinating field and its many applications.",coverUrl:"https://cdn.intechopen.com/series/covers/14.jpg",latestPublicationDate:"June 11th, 2022",hasOnlineFirst:!0,numberOfPublishedBooks:9,editor:{id:"218714",title:"Prof.",name:"Andries",middleName:null,surname:"Engelbrecht",slug:"andries-engelbrecht",fullName:"Andries Engelbrecht",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRNR8QAO/Profile_Picture_1622640468300",biography:"Andries Engelbrecht received the Masters and PhD degrees in Computer Science from the University of Stellenbosch, South Africa, in 1994 and 1999 respectively. He is currently appointed as the Voigt Chair in Data Science in the Department of Industrial Engineering, with a joint appointment as Professor in the Computer Science Division, Stellenbosch University. Prior to his appointment at Stellenbosch University, he has been at the University of Pretoria, Department of Computer Science (1998-2018), where he was appointed as South Africa Research Chair in Artifical Intelligence (2007-2018), the head of the Department of Computer Science (2008-2017), and Director of the Institute for Big Data and Data Science (2017-2018). 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Travieso-González received his MSc degree in Telecommunication Engineering at Polytechnic University of Catalonia (UPC), Spain in 1997, and his Ph.D. degree in 2002 at the University of Las Palmas de Gran Canaria (ULPGC-Spain). He is a full professor of signal processing and pattern recognition and is head of the Signals and Communications Department at ULPGC, teaching from 2001 on subjects on signal processing and learning theory. His research lines are biometrics, biomedical signals and images, data mining, classification system, signal and image processing, machine learning, and environmental intelligence. He has researched in 52 international and Spanish research projects, some of them as head researcher. He is co-author of 4 books, co-editor of 27 proceedings books, guest editor for 8 JCR-ISI international journals, and up to 24 book chapters. He has over 450 papers published in international journals and conferences (81 of them indexed on JCR – ISI - Web of Science). He has published seven patents in the Spanish Patent and Trademark Office. He has been a supervisor on 8 Ph.D. theses (11 more are under supervision), and 130 master theses. He is the founder of The IEEE IWOBI conference series and the president of its Steering Committee, as well as the founder of both the InnoEducaTIC and APPIS conference series. He is an evaluator of project proposals for the European Union (H2020), Medical Research Council (MRC, UK), Spanish Government (ANECA, Spain), Research National Agency (ANR, France), DAAD (Germany), Argentinian Government, and the Colombian Institutions. He has been a reviewer in different indexed international journals (<70) and conferences (<250) since 2001. He has been a member of the IASTED Technical Committee on Image Processing from 2007 and a member of the IASTED Technical Committee on Artificial Intelligence and Expert Systems from 2011. \n\nHe has held the general chair position for the following: ACM-APPIS (2020, 2021), IEEE-IWOBI (2019, 2020 and 2020), A PPIS (2018, 2019), IEEE-IWOBI (2014, 2015, 2017, 2018), InnoEducaTIC (2014, 2017), IEEE-INES (2013), NoLISP (2011), JRBP (2012), and IEEE-ICCST (2005)\n\nHe is an associate editor of the Computational Intelligence and Neuroscience Journal (Hindawi – Q2 JCR-ISI). He was vice dean from 2004 to 2010 in the Higher Technical School of Telecommunication Engineers at ULPGC and the vice dean of Graduate and Postgraduate Studies from March 2013 to November 2017. He won the “Catedra Telefonica” Awards in Modality of Knowledge Transfer, 2017, 2018, and 2019 editions, and awards in Modality of COVID Research in 2020.\n\nPublic References:\nResearcher ID http://www.researcherid.com/rid/N-5967-2014\nORCID https://orcid.org/0000-0002-4621-2768 \nScopus Author ID https://www.scopus.com/authid/detail.uri?authorId=6602376272\nScholar Google https://scholar.google.es/citations?user=G1ks9nIAAAAJ&hl=en \nResearchGate https://www.researchgate.net/profile/Carlos_Travieso",institutionString:null,institution:{name:"University of Las Palmas de Gran Canaria",institutionURL:null,country:{name:"Spain"}}},editorTwo:null,editorThree:null},{id:"23",title:"Computational Neuroscience",coverUrl:"https://cdn.intechopen.com/series_topics/covers/23.jpg",isOpenForSubmission:!0,annualVolume:11419,editor:{id:"14004",title:"Dr.",name:"Magnus",middleName:null,surname:"Johnsson",slug:"magnus-johnsson",fullName:"Magnus Johnsson",profilePictureURL:"https://mts.intechopen.com/storage/users/14004/images/system/14004.png",biography:"Dr Magnus Johnsson is a cross-disciplinary scientist, lecturer, scientific editor and AI/machine learning consultant from Sweden. \n\nHe is currently at Malmö University in Sweden, but also held positions at Lund University in Sweden and at Moscow Engineering Physics Institute. \nHe holds editorial positions at several international scientific journals and has served as a scientific editor for books and special journal issues. \nHis research interests are wide and include, but are not limited to, autonomous systems, computer modeling, artificial neural networks, artificial intelligence, cognitive neuroscience, cognitive robotics, cognitive architectures, cognitive aids and the philosophy of mind. \n\nDr. Johnsson has experience from working in the industry and he has a keen interest in the application of neural networks and artificial intelligence to fields like industry, finance, and medicine. \n\nWeb page: www.magnusjohnsson.se",institutionString:null,institution:{name:"Malmö University",institutionURL:null,country:{name:"Sweden"}}},editorTwo:null,editorThree:null},{id:"24",title:"Computer Vision",coverUrl:"https://cdn.intechopen.com/series_topics/covers/24.jpg",isOpenForSubmission:!0,annualVolume:11420,editor:{id:"294154",title:"Prof.",name:"George",middleName:null,surname:"Papakostas",slug:"george-papakostas",fullName:"George Papakostas",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002hYaGbQAK/Profile_Picture_1624519712088",biography:"George A. Papakostas has received a diploma in Electrical and Computer Engineering in 1999 and the M.Sc. and Ph.D. degrees in Electrical and Computer Engineering in 2002 and 2007, respectively, from the Democritus University of Thrace (DUTH), Greece. Dr. Papakostas serves as a Tenured Full Professor at the Department of Computer Science, International Hellenic University, Greece. Dr. Papakostas has 10 years of experience in large-scale systems design as a senior software engineer and technical manager, and 20 years of research experience in the field of Artificial Intelligence. Currently, he is the Head of the “Visual Computing” division of HUman-MAchines INteraction Laboratory (HUMAIN-Lab) and the Director of the MPhil program “Advanced Technologies in Informatics and Computers” hosted by the Department of Computer Science, International Hellenic University. He has (co)authored more than 150 publications in indexed journals, international conferences and book chapters, 1 book (in Greek), 3 edited books, and 5 journal special issues. His publications have more than 2100 citations with h-index 27 (GoogleScholar). His research interests include computer/machine vision, machine learning, pattern recognition, computational intelligence. \nDr. Papakostas served as a reviewer in numerous journals, as a program\ncommittee member in international conferences and he is a member of the IAENG, MIR Labs, EUCogIII, INSTICC and the Technical Chamber of Greece (TEE).",institutionString:null,institution:{name:"International Hellenic University",institutionURL:null,country:{name:"Greece"}}},editorTwo:null,editorThree:null},{id:"25",title:"Evolutionary Computation",coverUrl:"https://cdn.intechopen.com/series_topics/covers/25.jpg",isOpenForSubmission:!0,annualVolume:11421,editor:{id:"136112",title:"Dr.",name:"Sebastian",middleName:null,surname:"Ventura Soto",slug:"sebastian-ventura-soto",fullName:"Sebastian Ventura Soto",profilePictureURL:"https://mts.intechopen.com/storage/users/136112/images/system/136112.png",biography:"Sebastian Ventura is a Spanish researcher, a full professor with the Department of Computer Science and Numerical Analysis, University of Córdoba. Dr Ventura also holds the positions of Affiliated Professor at Virginia Commonwealth University (Richmond, USA) and Distinguished Adjunct Professor at King Abdulaziz University (Jeddah, Saudi Arabia). Additionally, he is deputy director of the Andalusian Research Institute in Data Science and Computational Intelligence (DaSCI) and heads the Knowledge Discovery and Intelligent Systems Research Laboratory. He has published more than ten books and over 300 articles in journals and scientific conferences. Currently, his work has received over 18,000 citations according to Google Scholar, including more than 2200 citations in 2020. In the last five years, he has published more than 60 papers in international journals indexed in the JCR (around 70% of them belonging to first quartile journals) and he has edited some Springer books “Supervised Descriptive Pattern Mining” (2018), “Multiple Instance Learning - Foundations and Algorithms” (2016), and “Pattern Mining with Evolutionary Algorithms” (2016). He has also been involved in more than 20 research projects supported by the Spanish and Andalusian governments and the European Union. He currently belongs to the editorial board of PeerJ Computer Science, Information Fusion and Engineering Applications of Artificial Intelligence journals, being also associate editor of Applied Computational Intelligence and Soft Computing and IEEE Transactions on Cybernetics. Finally, he is editor-in-chief of Progress in Artificial Intelligence. He is a Senior Member of the IEEE Computer, the IEEE Computational Intelligence, and the IEEE Systems, Man, and Cybernetics Societies, and the Association of Computing Machinery (ACM). Finally, his main research interests include data science, computational intelligence, and their applications.",institutionString:null,institution:{name:"University of Córdoba",institutionURL:null,country:{name:"Spain"}}},editorTwo:null,editorThree:null},{id:"26",title:"Machine Learning and Data Mining",coverUrl:"https://cdn.intechopen.com/series_topics/covers/26.jpg",isOpenForSubmission:!0,annualVolume:11422,editor:{id:"24555",title:"Dr.",name:"Marco Antonio",middleName:null,surname:"Aceves Fernandez",slug:"marco-antonio-aceves-fernandez",fullName:"Marco Antonio Aceves Fernandez",profilePictureURL:"https://mts.intechopen.com/storage/users/24555/images/system/24555.jpg",biography:"Dr. Marco Antonio Aceves Fernandez obtained his B.Sc. (Eng.) in Telematics from the Universidad de Colima, Mexico. He obtained both his M.Sc. and Ph.D. from the University of Liverpool, England, in the field of Intelligent Systems. He is a full professor at the Universidad Autonoma de Queretaro, Mexico, and a member of the National System of Researchers (SNI) since 2009. Dr. Aceves Fernandez has published more than 80 research papers as well as a number of book chapters and congress papers. He has contributed in more than 20 funded research projects, both academic and industrial, in the area of artificial intelligence, ranging from environmental, biomedical, automotive, aviation, consumer, and robotics to other applications. He is also a honorary president at the National Association of Embedded Systems (AMESE), a senior member of the IEEE, and a board member of many institutions. His research interests include intelligent and embedded systems.",institutionString:"Universidad Autonoma de Queretaro",institution:{name:"Autonomous University of Queretaro",institutionURL:null,country:{name:"Mexico"}}},editorTwo:null,editorThree:null},{id:"27",title:"Multi-Agent Systems",coverUrl:"https://cdn.intechopen.com/series_topics/covers/27.jpg",isOpenForSubmission:!0,annualVolume:11423,editor:{id:"148497",title:"Dr.",name:"Mehmet",middleName:"Emin",surname:"Aydin",slug:"mehmet-aydin",fullName:"Mehmet Aydin",profilePictureURL:"https://mts.intechopen.com/storage/users/148497/images/system/148497.jpg",biography:"Dr. Mehmet Emin Aydin is a Senior Lecturer with the Department of Computer Science and Creative Technology, the University of the West of England, Bristol, UK. His research interests include swarm intelligence, parallel and distributed metaheuristics, machine learning, intelligent agents and multi-agent systems, resource planning, scheduling and optimization, combinatorial optimization. Dr. Aydin is currently a Fellow of Higher Education Academy, UK, a member of EPSRC College, a senior member of IEEE and a senior member of ACM. In addition to being a member of advisory committees of many international conferences, he is an Editorial Board Member of various peer-reviewed international journals. He has served as guest editor for a number of special issues of peer-reviewed international journals.",institutionString:null,institution:{name:"University of the West of England",institutionURL:null,country:{name:"United Kingdom"}}},editorTwo:null,editorThree:null}]},overviewPageOFChapters:{paginationCount:43,paginationItems:[{id:"82374",title:"The Potential of the Purinergic System as a Therapeutic Target of Natural Compounds in Cutaneous Melanoma",doi:"10.5772/intechopen.105457",signatures:"Gilnei Bruno da Silva, Daiane Manica, Marcelo Moreno and Margarete Dulce Bagatini",slug:"the-potential-of-the-purinergic-system-as-a-therapeutic-target-of-natural-compounds-in-cutaneous-mel",totalDownloads:4,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Purinergic System",coverURL:"https://cdn.intechopen.com/books/images_new/10801.jpg",subseries:{id:"17",title:"Metabolism"}}},{id:"82103",title:"The Role of Endoplasmic Reticulum Stress and Its Regulation in the Progression of Neurological and Infectious Diseases",doi:"10.5772/intechopen.105543",signatures:"Mary Dover, Michael Kishek, Miranda Eddins, Naneeta Desar, Ketema Paul and Milan Fiala",slug:"the-role-of-endoplasmic-reticulum-stress-and-its-regulation-in-the-progression-of-neurological-and-i",totalDownloads:5,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Updates on Endoplasmic Reticulum",coverURL:"https://cdn.intechopen.com/books/images_new/11674.jpg",subseries:{id:"14",title:"Cell and Molecular Biology"}}},{id:"82212",title:"Protein Prenylation and Their Applications",doi:"10.5772/intechopen.104700",signatures:"Khemchand R. 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Waisundara",profilePictureURL:"https://mts.intechopen.com/storage/users/194281/images/system/194281.jpg",biography:"Dr. Viduranga Waisundara obtained her Ph.D. in Food Science\nand Technology from the Department of Chemistry, National\nUniversity of Singapore, in 2010. She was a lecturer at Temasek Polytechnic, Singapore from July 2009 to March 2013.\nShe relocated to her motherland of Sri Lanka and spearheaded the Functional Food Product Development Project at the\nNational Institute of Fundamental Studies from April 2013 to\nOctober 2016. She was a senior lecturer on a temporary basis at the Department of\nFood Technology, Faculty of Technology, Rajarata University of Sri Lanka. She is\ncurrently Deputy Principal of the Australian College of Business and Technology –\nKandy Campus, Sri Lanka. She is also the Global Harmonization Initiative (GHI)",institutionString:"Australian College of Business & Technology",institution:null}]},{type:"book",id:"6820",title:"Keratin",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/6820.jpg",slug:"keratin",publishedDate:"December 19th 2018",editedByType:"Edited by",bookSignature:"Miroslav Blumenberg",hash:"6def75cd4b6b5324a02b6dc0359896d0",volumeInSeries:2,fullTitle:"Keratin",editors:[{id:"31610",title:"Dr.",name:"Miroslav",middleName:null,surname:"Blumenberg",slug:"miroslav-blumenberg",fullName:"Miroslav Blumenberg",profilePictureURL:"https://mts.intechopen.com/storage/users/31610/images/system/31610.jpg",biography:"Miroslav Blumenberg, Ph.D., was born in Subotica and received his BSc in Belgrade, Yugoslavia. He completed his Ph.D. at MIT in Organic Chemistry; he followed up his Ph.D. with two postdoctoral study periods at Stanford University. Since 1983, he has been a faculty member of the RO Perelman Department of Dermatology, NYU School of Medicine, where he is codirector of a training grant in cutaneous biology. Dr. Blumenberg’s research is focused on the epidermis, expression of keratin genes, transcription profiling, keratinocyte differentiation, inflammatory diseases and cancers, and most recently the effects of the microbiome on the skin. He has published more than 100 peer-reviewed research articles and graduated numerous Ph.D. and postdoctoral students.",institutionString:null,institution:{name:"New York University Langone Medical Center",institutionURL:null,country:{name:"United States of America"}}}]},{type:"book",id:"7978",title:"Vitamin A",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/7978.jpg",slug:"vitamin-a",publishedDate:"May 15th 2019",editedByType:"Edited by",bookSignature:"Leila Queiroz Zepka, Veridiana Vera de Rosso and Eduardo Jacob-Lopes",hash:"dad04a658ab9e3d851d23705980a688b",volumeInSeries:3,fullTitle:"Vitamin A",editors:[{id:"261969",title:"Dr.",name:"Leila",middleName:null,surname:"Queiroz Zepka",slug:"leila-queiroz-zepka",fullName:"Leila Queiroz Zepka",profilePictureURL:"https://mts.intechopen.com/storage/users/261969/images/system/261969.png",biography:"Prof. Dr. Leila Queiroz Zepka is currently an associate professor in the Department of Food Technology and Science, Federal University of Santa Maria, Brazil. She has more than fifteen years of teaching and research experience. She has published more than 550 scientific publications/communications, including 15 books, 50 book chapters, 100 original research papers, 380 research communications in national and international conferences, and 12 patents. She is a member of the editorial board of five journals and acts as a reviewer for several national and international journals. 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Prof. Sarfraz is also an editor-in-chief and editor of various international journals.",institutionString:"Kuwait University",institution:{name:"Kuwait University",country:{name:"Kuwait"}}},{id:"32650",title:"Prof.",name:"Lukas",middleName:"Willem",surname:"Snyman",slug:"lukas-snyman",fullName:"Lukas Snyman",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/32650/images/4136_n.jpg",biography:"Lukas Willem Snyman received his basic education at primary and high schools in South Africa, Eastern Cape. He enrolled at today's Nelson Metropolitan University and graduated from this university with a BSc in Physics and Mathematics, B.Sc Honors in Physics, MSc in Semiconductor Physics, and a Ph.D. in Semiconductor Physics in 1987. After his studies, he chose an academic career and devoted his energy to the teaching of physics to first, second, and third-year students. After positions as a lecturer at the University of Port Elizabeth, he accepted a position as Associate Professor at the University of Pretoria, South Africa.\r\n\r\nIn 1992, he motivates the concept of 'television and computer-based education” as means to reach large student numbers with only the best of teaching expertise and publishes an article on the concept in the SA Journal of Higher Education of 1993 (and later in 2003). The University of Pretoria subsequently approved a series of test projects on the concept with outreach to Mamelodi and Eerste Rust in 1993. In 1994, the University established a 'Unit for Telematic Education ' as a support section for multiple faculties at the University of Pretoria. In subsequent years, the concept of 'telematic education” subsequently becomes well established in academic circles in South Africa, grew in popularity, and is adopted by many universities and colleges throughout South Africa as a medium of enhancing education and training, as a method to reaching out to far out communities, and as a means to enhance study from the home environment.\r\n\r\nProfessor Snyman in subsequent years pursued research in semiconductor physics, semiconductor devices, microelectronics, and optoelectronics.\r\n\r\nIn 2000 he joined the TUT as a full professor. Here served for a period as head of the Department of Electronic Engineering. Here he makes contributions to solar energy development, microwave and optoelectronic device development, silicon photonics, as well as contributions to new mobile telecommunication systems and network planning in SA.\r\n\r\nCurrently, he teaches electronics and telecommunications at the TUT to audiences ranging from first-year students to Ph.D. level.\r\n\r\nFor his research in the field of 'Silicon Photonics” since 1990, he has published (as author and co-author) about thirty internationally reviewed articles in scientific journals, contributed to more than forty international conferences, about 25 South African provisional patents (as inventor and co-inventor), 8 PCT international patent applications until now. Of these, two USA patents applications, two European Patents, two Korean patents, and ten SA patents have been granted. A further 4 USA patents, 5 European patents, 3 Korean patents, 3 Chinese patents, and 3 Japanese patents are currently under consideration.\r\n\r\nRecently he has also published an extensive scholarly chapter in an internet open access book on 'Integrating Microphotonic Systems and MOEMS into standard Silicon CMOS Integrated circuitry”.\r\n\r\nFurthermore, Professor Snyman recently steered a new initiative at the TUT by introducing a 'Laboratory for Innovative Electronic Systems ' at the Department of Electrical Engineering. The model of this laboratory or center is to primarily combine outputs as achieved by high-level research with lower-level system development and entrepreneurship in a technical university environment. Students are allocated to projects at different levels with PhDs and Master students allocated to the generation of new knowledge and new technologies, while students at the diploma and Baccalaureus level are allocated to electronic systems development with a direct and a near application for application in industry or the commercial and public sectors in South Africa.\r\n\r\nProfessor Snyman received the WIRSAM Award of 1983 and the WIRSAM Award in 1985 in South Africa for best research papers by a young scientist at two international conferences on electron microscopy in South Africa. He subsequently received the SA Microelectronics Award for the best dissertation emanating from studies executed at a South African university in the field of Physics and Microelectronics in South Africa in 1987. In October of 2011, Professor Snyman received the prestigious Institutional Award for 'Innovator of the Year” for 2010 at the Tshwane University of Technology, South Africa. This award was based on the number of patents recognized and granted by local and international institutions as well as for his contributions concerning innovation at the TUT.",institutionString:null,institution:{name:"University of South Africa",country:{name:"South Africa"}}},{id:"317279",title:"Mr.",name:"Ali",middleName:"Usama",surname:"Syed",slug:"ali-syed",fullName:"Ali Syed",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/317279/images/16024_n.png",biography:"A creative, talented, and innovative young professional who is dedicated, well organized, and capable research fellow with two years of experience in graduate-level research, published in engineering journals and book, with related expertise in Bio-robotics, equally passionate about the aesthetics of the mechanical and electronic system, obtained expertise in the use of MS Office, MATLAB, SolidWorks, LabVIEW, Proteus, Fusion 360, having a grasp on python, C++ and assembly language, possess proven ability in acquiring research grants, previous appointments with social and educational societies with experience in administration, current affiliations with IEEE and Web of Science, a confident presenter at conferences and teacher in classrooms, able to explain complex information to audiences of all levels.",institutionString:null,institution:{name:"Air University",country:{name:"Pakistan"}}},{id:"75526",title:"Ph.D.",name:"Zihni Onur",middleName:null,surname:"Uygun",slug:"zihni-onur-uygun",fullName:"Zihni Onur Uygun",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/75526/images/12_n.jpg",biography:"My undergraduate education and my Master of Science educations at Ege University and at Çanakkale Onsekiz Mart University have given me a firm foundation in Biochemistry, Analytical Chemistry, Biosensors, Bioelectronics, Physical Chemistry and Medicine. After obtaining my degree as a MSc in analytical chemistry, I started working as a research assistant in Ege University Medical Faculty in 2014. In parallel, I enrolled to the MSc program at the Department of Medical Biochemistry at Ege University to gain deeper knowledge on medical and biochemical sciences as well as clinical chemistry in 2014. In my PhD I deeply researched on biosensors and bioelectronics and finished in 2020. Now I have eleven SCI-Expanded Index published papers, 6 international book chapters, referee assignments for different SCIE journals, one international patent pending, several international awards, projects and bursaries. In parallel to my research assistant position at Ege University Medical Faculty, Department of Medical Biochemistry, in April 2016, I also founded a Start-Up Company (Denosens Biotechnology LTD) by the support of The Scientific and Technological Research Council of Turkey. Currently, I am also working as a CEO in Denosens Biotechnology. The main purposes of the company, which carries out R&D as a research center, are to develop new generation biosensors and sensors for both point-of-care diagnostics; such as glucose, lactate, cholesterol and cancer biomarker detections. My specific experimental and instrumental skills are Biochemistry, Biosensor, Analytical Chemistry, Electrochemistry, Mobile phone based point-of-care diagnostic device, POCTs and Patient interface designs, HPLC, Tandem Mass Spectrometry, Spectrophotometry, ELISA.",institutionString:null,institution:{name:"Ege University",country:{name:"Turkey"}}},{id:"267434",title:"Dr.",name:"Rohit",middleName:null,surname:"Raja",slug:"rohit-raja",fullName:"Rohit Raja",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/267434/images/system/267434.jpg",biography:"Dr. Rohit Raja received Ph.D. in Computer Science and Engineering from Dr. CVRAMAN University in 2016. His main research interest includes Face recognition and Identification, Digital Image Processing, Signal Processing, and Networking. Presently he is working as Associate Professor in IT Department, Guru Ghasidas Vishwavidyalaya (A Central University), Bilaspur (CG), India. He has authored several Journal and Conference Papers. He has good Academics & Research experience in various areas of CSE and IT. He has filed and successfully published 27 Patents. He has received many time invitations to be a Guest at IEEE Conferences. He has published 100 research papers in various International/National Journals (including IEEE, Springer, etc.) and Proceedings of the reputed International/ National Conferences (including Springer and IEEE). He has been nominated to the board of editors/reviewers of many peer-reviewed and refereed Journals (including IEEE, Springer).",institutionString:"Guru Ghasidas Vishwavidyalaya",institution:{name:"Guru Ghasidas Vishwavidyalaya",country:{name:"India"}}},{id:"246502",title:"Dr.",name:"Jaya T.",middleName:"T",surname:"Varkey",slug:"jaya-t.-varkey",fullName:"Jaya T. Varkey",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/246502/images/11160_n.jpg",biography:"Jaya T. Varkey, PhD, graduated with a degree in Chemistry from Cochin University of Science and Technology, Kerala, India. She obtained a PhD in Chemistry from the School of Chemical Sciences, Mahatma Gandhi University, Kerala, India, and completed a post-doctoral fellowship at the University of Minnesota, USA. She is a research guide at Mahatma Gandhi University and Associate Professor in Chemistry, St. Teresa’s College, Kochi, Kerala, India.\nDr. Varkey received a National Young Scientist award from the Indian Science Congress (1995), a UGC Research award (2016–2018), an Indian National Science Academy (INSA) Visiting Scientist award (2018–2019), and a Best Innovative Faculty award from the All India Association for Christian Higher Education (AIACHE) (2019). She Hashas received the Sr. Mary Cecil prize for best research paper three times. She was also awarded a start-up to develop a tea bag water filter. \nDr. Varkey has published two international books and twenty-seven international journal publications. She is an editorial board member for five international journals.",institutionString:"St. Teresa’s College",institution:null},{id:"250668",title:"Dr.",name:"Ali",middleName:null,surname:"Nabipour Chakoli",slug:"ali-nabipour-chakoli",fullName:"Ali Nabipour Chakoli",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/250668/images/system/250668.jpg",biography:"Academic Qualification:\r\n•\tPhD in Materials Physics and Chemistry, From: Sep. 2006, to: Sep. 2010, School of Materials Science and Engineering, Harbin Institute of Technology, Thesis: Structure and Shape Memory Effect of Functionalized MWCNTs/poly (L-lactide-co-ε-caprolactone) Nanocomposites. Supervisor: Prof. Wei Cai,\r\n•\tM.Sc in Applied Physics, From: 1996, to: 1998, Faculty of Physics & Nuclear Science, Amirkabir Uni. of Technology, Tehran, Iran, Thesis: Determination of Boron in Micro alloy Steels with solid state nuclear track detectors by neutron induced auto radiography, Supervisors: Dr. M. Hosseini Ashrafi and Dr. A. Hosseini.\r\n•\tB.Sc. in Applied Physics, From: 1991, to: 1996, Faculty of Physics & Nuclear Science, Amirkabir Uni. of Technology, Tehran, Iran, Thesis: Design of shielding for Am-Be neutron sources for In Vivo neutron activation analysis, Supervisor: Dr. M. Hosseini Ashrafi.\r\n\r\nResearch Experiences:\r\n1.\tNanomaterials, Carbon Nanotubes, Graphene: Synthesis, Functionalization and Characterization,\r\n2.\tMWCNTs/Polymer Composites: Fabrication and Characterization, \r\n3.\tShape Memory Polymers, Biodegradable Polymers, ORC, Collagen,\r\n4.\tMaterials Analysis and Characterizations: TEM, SEM, XPS, FT-IR, Raman, DSC, DMA, TGA, XRD, GPC, Fluoroscopy, \r\n5.\tInteraction of Radiation with Mater, Nuclear Safety and Security, NDT(RT),\r\n6.\tRadiation Detectors, Calibration (SSDL),\r\n7.\tCompleted IAEA e-learning Courses:\r\nNuclear Security (15 Modules),\r\nNuclear Safety:\r\nTSA 2: Regulatory Protection in Occupational Exposure,\r\nTips & Tricks: Radiation Protection in Radiography,\r\nSafety and Quality in Radiotherapy,\r\nCourse on Sealed Radioactive Sources,\r\nCourse on Fundamentals of Environmental Remediation,\r\nCourse on Planning for Environmental Remediation,\r\nKnowledge Management Orientation Course,\r\nFood Irradiation - Technology, Applications and Good Practices,\r\nEmployment:\r\nFrom 2010 to now: Academic staff, Nuclear Science and Technology Research Institute, Kargar Shomali, Tehran, Iran, P.O. Box: 14395-836.\r\nFrom 1997 to 2006: Expert of Materials Analysis and Characterization. Research Center of Agriculture and Medicine. Rajaeeshahr, Karaj, Iran, P. O. Box: 31585-498.",institutionString:"Atomic Energy Organization of Iran",institution:{name:"Atomic Energy Organization of Iran",country:{name:"Iran"}}},{id:"248279",title:"Dr.",name:"Monika",middleName:"Elzbieta",surname:"Machoy",slug:"monika-machoy",fullName:"Monika Machoy",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/248279/images/system/248279.jpeg",biography:"Monika Elżbieta Machoy, MD, graduated with distinction from the Faculty of Medicine and Dentistry at the Pomeranian Medical University in 2009, defended her PhD thesis with summa cum laude in 2016 and is currently employed as a researcher at the Department of Orthodontics of the Pomeranian Medical University. She expanded her professional knowledge during a one-year scholarship program at the Ernst Moritz Arndt University in Greifswald, Germany and during a three-year internship at the Technical University in Dresden, Germany. She has been a speaker at numerous orthodontic conferences, among others, American Association of Orthodontics, European Orthodontic Symposium and numerous conferences of the Polish Orthodontic Society. She conducts research focusing on the effect of orthodontic treatment on dental and periodontal tissues and the causes of pain in orthodontic patients.",institutionString:"Pomeranian Medical University",institution:{name:"Pomeranian Medical University",country:{name:"Poland"}}},{id:"252743",title:"Prof.",name:"Aswini",middleName:"Kumar",surname:"Kar",slug:"aswini-kar",fullName:"Aswini Kar",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/252743/images/10381_n.jpg",biography:"uploaded in cv",institutionString:null,institution:{name:"KIIT University",country:{name:"India"}}},{id:"204256",title:"Dr.",name:"Anil",middleName:"Kumar",surname:"Kumar Sahu",slug:"anil-kumar-sahu",fullName:"Anil Kumar Sahu",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/204256/images/14201_n.jpg",biography:"I have nearly 11 years of research and teaching experience. I have done my master degree from University Institute of Pharmacy, Pt. Ravi Shankar Shukla University, Raipur, Chhattisgarh India. I have published 16 review and research articles in international and national journals and published 4 chapters in IntechOpen, the world’s leading publisher of Open access books. I have presented many papers at national and international conferences. I have received research award from Indian Drug Manufacturers Association in year 2015. My research interest extends from novel lymphatic drug delivery systems, oral delivery system for herbal bioactive to formulation optimization.",institutionString:null,institution:{name:"Chhattisgarh Swami Vivekanand Technical University",country:{name:"India"}}},{id:"253468",title:"Dr.",name:"Mariusz",middleName:null,surname:"Marzec",slug:"mariusz-marzec",fullName:"Mariusz Marzec",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/253468/images/system/253468.png",biography:"An assistant professor at Department of Biomedical Computer Systems, at Institute of Computer Science, Silesian University in Katowice. Scientific interests: computer analysis and processing of images, biomedical images, databases and programming languages. He is an author and co-author of scientific publications covering analysis and processing of biomedical images and development of database systems.",institutionString:"University of Silesia",institution:null},{id:"212432",title:"Prof.",name:"Hadi",middleName:null,surname:"Mohammadi",slug:"hadi-mohammadi",fullName:"Hadi Mohammadi",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/212432/images/system/212432.jpeg",biography:"Dr. Hadi Mohammadi is a biomedical engineer with hands-on experience in the design and development of many engineering structures and medical devices through various projects that he has been involved in over the past twenty years. Dr. Mohammadi received his BSc. and MSc. degrees in Mechanical Engineering from Sharif University of Technology, Tehran, Iran, and his PhD. degree in Biomedical Engineering (biomaterials) from the University of Western Ontario. He was a postdoctoral trainee for almost four years at University of Calgary and Harvard Medical School. He is an industry innovator having created the technology to produce lifelike synthetic platforms that can be used for the simulation of almost all cardiovascular reconstructive surgeries. He’s been heavily involved in the design and development of cardiovascular devices and technology for the past 10 years. He is currently an Assistant Professor with the University of British Colombia, Canada.",institutionString:"University of British Columbia",institution:{name:"University of British Columbia",country:{name:"Canada"}}},{id:"254463",title:"Prof.",name:"Haisheng",middleName:null,surname:"Yang",slug:"haisheng-yang",fullName:"Haisheng Yang",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/254463/images/system/254463.jpeg",biography:"Haisheng Yang, Ph.D., Professor and Director of the Department of Biomedical Engineering, College of Life Science and Bioengineering, Beijing University of Technology. He received his Ph.D. degree in Mechanics/Biomechanics from Harbin Institute of Technology (jointly with University of California, Berkeley). Afterwards, he worked as a Postdoctoral Research Associate in the Purdue Musculoskeletal Biology and Mechanics Lab at the Department of Basic Medical Sciences, Purdue University, USA. He also conducted research in the Research Centre of Shriners Hospitals for Children-Canada at McGill University, Canada. Dr. Yang has over 10 years research experience in orthopaedic biomechanics and mechanobiology of bone adaptation and regeneration. He earned an award from Beijing Overseas Talents Aggregation program in 2017 and serves as Beijing Distinguished Professor.",institutionString:null,institution:{name:"Beijing University of Technology",country:{name:"China"}}},{id:"89721",title:"Dr.",name:"Mehmet",middleName:"Cuneyt",surname:"Ozmen",slug:"mehmet-ozmen",fullName:"Mehmet Ozmen",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/89721/images/7289_n.jpg",biography:null,institutionString:null,institution:{name:"Gazi University",country:{name:"Turkey"}}},{id:"243698",title:"M.D.",name:"Xiaogang",middleName:null,surname:"Wang",slug:"xiaogang-wang",fullName:"Xiaogang Wang",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/243698/images/system/243698.png",biography:"Dr. Xiaogang Wang, a faculty member of Shanxi Eye Hospital specializing in the treatment of cataract and retinal disease and a tutor for postgraduate students of Shanxi Medical University, worked in the COOL Lab as an international visiting scholar under the supervision of Dr. David Huang and Yali Jia from October 2012 through November 2013. Dr. Wang earned an MD from Shanxi Medical University and a Ph.D. from Shanghai Jiao Tong University. Dr. Wang was awarded two research project grants focused on multimodal optical coherence tomography imaging and deep learning in cataract and retinal disease, from the National Natural Science Foundation of China. He has published around 30 peer-reviewed journal papers and four book chapters and co-edited one book.",institutionString:"Shanxi Eye Hospital",institution:{name:"Shanxi Eye Hospital",country:{name:"China"}}},{id:"242893",title:"Ph.D. Student",name:"Joaquim",middleName:null,surname:"De Moura",slug:"joaquim-de-moura",fullName:"Joaquim De Moura",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/242893/images/7133_n.jpg",biography:"Joaquim de Moura received his degree in Computer Engineering in 2014 from the University of A Coruña (Spain). In 2016, he received his M.Sc degree in Computer Engineering from the same university. He is currently pursuing his Ph.D degree in Computer Science in a collaborative project between ophthalmology centers in Galicia and the University of A Coruña. His research interests include computer vision, machine learning algorithms and analysis and medical imaging processing of various kinds.",institutionString:null,institution:{name:"University of A Coruña",country:{name:"Spain"}}},{id:"294334",title:"B.Sc.",name:"Marc",middleName:null,surname:"Bruggeman",slug:"marc-bruggeman",fullName:"Marc Bruggeman",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/294334/images/8242_n.jpg",biography:"Chemical engineer graduate, with a passion for material science and specific interest in polymers - their near infinite applications intrigue me. \n\nI plan to continue my scientific career in the field of polymeric biomaterials as I am fascinated by intelligent, bioactive and biomimetic materials for use in both consumer and medical applications.",institutionString:null,institution:null},{id:"255757",title:"Dr.",name:"Igor",middleName:"Victorovich",surname:"Lakhno",slug:"igor-lakhno",fullName:"Igor Lakhno",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/255757/images/system/255757.jpg",biography:"Igor Victorovich Lakhno was born in 1971 in Kharkiv (Ukraine). \nMD – 1994, Kharkiv National Medical Univesity.\nOb&Gyn; – 1997, master courses in Kharkiv Medical Academy of Postgraduate Education.\nPh.D. – 1999, Kharkiv National Medical Univesity.\nDSC – 2019, PL Shupik National Academy of Postgraduate Education \nProfessor – 2021, Department of Obstetrics and Gynecology of VN Karazin Kharkiv National University\nHead of Department – 2021, Department of Perinatology, Obstetrics and gynecology of Kharkiv Medical Academy of Postgraduate Education\nIgor Lakhno has been graduated from international training courses on reproductive medicine and family planning held at Debrecen University (Hungary) in 1997. Since 1998 Lakhno Igor has worked as an associate professor in the department of obstetrics and gynecology of VN Karazin National University and an associate professor of the perinatology, obstetrics, and gynecology department of Kharkiv Medical Academy of Postgraduate Education. Since June 2019 he’s been a professor in the department of obstetrics and gynecology of VN Karazin National University and a professor of the perinatology, obstetrics, and gynecology department. He’s affiliated with Kharkiv Medical Academy of Postgraduate Education as a Head of Department from November 2021. Igor Lakhno has participated in several international projects on fetal non-invasive electrocardiography (with Dr. J. A. Behar (Technion), Prof. D. Hoyer (Jena University), and José Alejandro Díaz Méndez (National Institute of Astrophysics, Optics, and Electronics, Mexico). He’s an author of about 200 printed works and there are 31 of them in Scopus or Web of Science databases. Igor Lakhno is a member of the Editorial Board of Reproductive Health of Woman, Emergency Medicine, and Technology Transfer Innovative Solutions in Medicine (Estonia). He is a medical Editor of “Z turbotoyu pro zhinku”. Igor Lakhno is a reviewer of the Journal of Obstetrics and Gynaecology (Taylor and Francis), British Journal of Obstetrics and Gynecology (Wiley), Informatics in Medicine Unlocked (Elsevier), The Journal of Obstetrics and Gynecology Research (Wiley), Endocrine, Metabolic & Immune Disorders-Drug Targets (Bentham Open), The Open Biomedical Engineering Journal (Bentham Open), etc. He’s defended a dissertation for a DSc degree “Pre-eclampsia: prediction, prevention, and treatment”. Three years ago Igor Lakhno has participated in a training course on innovative technologies in medical education at Lublin Medical University (Poland). Lakhno Igor has participated as a speaker in several international conferences and congresses (International Conference on Biological Oscillations April 10th-14th 2016, Lancaster, UK, The 9th conference of the European Study Group on Cardiovascular Oscillations). His main scientific interests: are obstetrics, women’s health, fetal medicine, and cardiovascular medicine. \nIgor Lakhno is a consultant at Kharkiv municipal perinatal center. He’s graduated from training courses on endoscopy in gynecology. He has 28 years of practical experience in the field.",institutionString:null,institution:null},{id:"244950",title:"Dr.",name:"Salvatore",middleName:null,surname:"Di Lauro",slug:"salvatore-di-lauro",fullName:"Salvatore Di Lauro",position:null,profilePictureURL:"https://intech-files.s3.amazonaws.com/0030O00002bSF1HQAW/ProfilePicture%202021-12-20%2014%3A54%3A14.482",biography:"Name:\n\tSALVATORE DI LAURO\nAddress:\n\tHospital Clínico Universitario Valladolid\nAvda Ramón y Cajal 3\n47005, Valladolid\nSpain\nPhone number: \nFax\nE-mail:\n\t+34 983420000 ext 292\n+34 983420084\nsadilauro@live.it\nDate and place of Birth:\nID Number\nMedical Licence \nLanguages\t09-05-1985. Villaricca (Italy)\n\nY1281863H\n474707061\nItalian (native language)\nSpanish (read, written, spoken)\nEnglish (read, written, spoken)\nPortuguese (read, spoken)\nFrench (read)\n\t\t\nCurrent position (title and company)\tDate (Year)\nVitreo-Retinal consultant in ophthalmology. Hospital Clinico Universitario Valladolid. Sacyl. National Health System.\nVitreo-Retinal consultant in ophthalmology. Instituto Oftalmologico Recoletas. Red Hospitalaria Recoletas. Private practise.\t2017-today\n\n2019-today\n\t\n\t\nEducation (High school, university and postgraduate training > 3 months)\tDate (Year)\nDegree in Medicine and Surgery. University of Neaples 'Federico II”\nResident in Opthalmology. Hospital Clinico Universitario Valladolid\nMaster in Vitreo-Retina. IOBA. University of Valladolid\nFellow of the European Board of Ophthalmology. Paris\nMaster in Research in Ophthalmology. University of Valladolid\t2003-2009\n2012-2016\n2016-2017\n2016\n2012-2013\n\t\nEmployments (company and positions)\tDate (Year)\nResident in Ophthalmology. Hospital Clinico Universitario Valladolid. Sacyl.\nFellow in Vitreo-Retina. IOBA. University of Valladolid\nVitreo-Retinal consultant in ophthalmology. Hospital Clinico Universitario Valladolid. Sacyl. National Health System.\nVitreo-Retinal consultant in ophthalmology. Instituto Oftalmologico Recoletas. Red Hospitalaria Recoletas. \n\t2012-2016\n2016-2017\n2017-today\n\n2019-Today\n\n\n\t\nClinical Research Experience (tasks and role)\tDate (Year)\nAssociated investigator\n\n' FIS PI20/00740: DESARROLLO DE UNA CALCULADORA DE RIESGO DE\nAPARICION DE RETINOPATIA DIABETICA BASADA EN TECNICAS DE IMAGEN MULTIMODAL EN PACIENTES DIABETICOS TIPO 1. Grant by: Ministerio de Ciencia e Innovacion \n\n' (BIO/VA23/14) Estudio clínico multicéntrico y prospectivo para validar dos\nbiomarcadores ubicados en los genes p53 y MDM2 en la predicción de los resultados funcionales de la cirugía del desprendimiento de retina regmatógeno. Grant by: Gerencia Regional de Salud de la Junta de Castilla y León.\n' Estudio multicéntrico, aleatorizado, con enmascaramiento doble, en 2 grupos\nparalelos y de 52 semanas de duración para comparar la eficacia, seguridad e inmunogenicidad de SOK583A1 respecto a Eylea® en pacientes con degeneración macular neovascular asociada a la edad' (CSOK583A12301; N.EUDRA: 2019-004838-41; FASE III). Grant by Hexal AG\n\n' Estudio de fase III, aleatorizado, doble ciego, con grupos paralelos, multicéntrico para comparar la eficacia y la seguridad de QL1205 frente a Lucentis® en pacientes con degeneración macular neovascular asociada a la edad. (EUDRACT: 2018-004486-13). Grant by Qilu Pharmaceutical Co\n\n' Estudio NEUTON: Ensayo clinico en fase IV para evaluar la eficacia de aflibercept en pacientes Naive con Edema MacUlar secundario a Oclusion de Vena CenTral de la Retina (OVCR) en regimen de tratamientO iNdividualizado Treat and Extend (TAE)”, (2014-000975-21). Grant by Fundacion Retinaplus\n\n' Evaluación de la seguridad y bioactividad de anillos de tensión capsular en conejo. Proyecto Procusens. Grant by AJL, S.A.\n\n'Estudio epidemiológico, prospectivo, multicéntrico y abierto\\npara valorar la frecuencia de la conjuntivitis adenovírica diagnosticada mediante el test AdenoPlus®\\nTest en pacientes enfermos de conjuntivitis aguda”\\n. National, multicenter study. Grant by: NICOX.\n\nEuropean multicentric trial: 'Evaluation of clinical outcomes following the use of Systane Hydration in patients with dry eye”. Study Phase 4. Grant by: Alcon Labs'\n\nVLPs Injection and Activation in a Rabbit Model of Uveal Melanoma. Grant by Aura Bioscience\n\nUpdating and characterization of a rabbit model of uveal melanoma. Grant by Aura Bioscience\n\nEnsayo clínico en fase IV para evaluar las variantes genéticas de la vía del VEGF como biomarcadores de eficacia del tratamiento con aflibercept en pacientes con degeneración macular asociada a la edad (DMAE) neovascular. Estudio BIOIMAGE. IMO-AFLI-2013-01\n\nEstudio In-Eye:Ensayo clínico en fase IV, abierto, aleatorizado, de 2 brazos,\nmulticçentrico y de 12 meses de duración, para evaluar la eficacia y seguridad de un régimen de PRN flexible individualizado de 'esperar y extender' versus un régimen PRN según criterios de estabilización mediante evaluaciones mensuales de inyecciones intravítreas de ranibizumab 0,5 mg en pacientes naive con neovascularización coriodea secunaria a la degeneración macular relacionada con la edad. CP: CRFB002AES03T\n\nTREND: Estudio Fase IIIb multicéntrico, randomizado, de 12 meses de\nseguimiento con evaluador de la agudeza visual enmascarado, para evaluar la eficacia y la seguridad de ranibizumab 0.5mg en un régimen de tratar y extender comparado con un régimen mensual, en pacientes con degeneración macular neovascular asociada a la edad. CP: CRFB002A2411 Código Eudra CT:\n2013-002626-23\n\n\n\nPublications\t\n\n2021\n\n\n\n\n2015\n\n\n\n\n2021\n\n\n\n\n\n2021\n\n\n\n\n2015\n\n\n\n\n2015\n\n\n2014\n\n\n\n\n2015-16\n\n\n\n2015\n\n\n2014\n\n\n2014\n\n\n\n\n2014\n\n\n\n\n\n\n\n2014\n\nJose Carlos Pastor; Jimena Rojas; Salvador Pastor-Idoate; Salvatore Di Lauro; Lucia Gonzalez-Buendia; Santiago Delgado-Tirado. Proliferative vitreoretinopathy: A new concept of disease pathogenesis and practical\nconsequences. Progress in Retinal and Eye Research. 51, pp. 125 - 155. 03/2016. DOI: 10.1016/j.preteyeres.2015.07.005\n\n\nLabrador-Velandia S; Alonso-Alonso ML; Di Lauro S; García-Gutierrez MT; Srivastava GK; Pastor JC; Fernandez-Bueno I. Mesenchymal stem cells provide paracrine neuroprotective resources that delay degeneration of co-cultured organotypic neuroretinal cultures.Experimental Eye Research. 185, 17/05/2019. DOI: 10.1016/j.exer.2019.05.011\n\nSalvatore Di Lauro; Maria Teresa Garcia Gutierrez; Ivan Fernandez Bueno. Quantification of pigment epithelium-derived factor (PEDF) in an ex vivo coculture of retinal pigment epithelium cells and neuroretina.\nJournal of Allbiosolution. 2019. ISSN 2605-3535\n\nSonia Labrador Velandia; Salvatore Di Lauro; Alonso-Alonso ML; Tabera Bartolomé S; Srivastava GK; Pastor JC; Fernandez-Bueno I. Biocompatibility of intravitreal injection of human mesenchymal stem cells in immunocompetent rabbits. Graefe's archive for clinical and experimental ophthalmology. 256 - 1, pp. 125 - 134. 01/2018. DOI: 10.1007/s00417-017-3842-3\n\n\nSalvatore Di Lauro, David Rodriguez-Crespo, Manuel J Gayoso, Maria T Garcia-Gutierrez, J Carlos Pastor, Girish K Srivastava, Ivan Fernandez-Bueno. A novel coculture model of porcine central neuroretina explants and retinal pigment epithelium cells. Molecular Vision. 2016 - 22, pp. 243 - 253. 01/2016.\n\nSalvatore Di Lauro. Classifications for Proliferative Vitreoretinopathy ({PVR}): An Analysis of Their Use in Publications over the Last 15 Years. Journal of Ophthalmology. 2016, pp. 1 - 6. 01/2016. DOI: 10.1155/2016/7807596\n\nSalvatore Di Lauro; Rosa Maria Coco; Rosa Maria Sanabria; Enrique Rodriguez de la Rua; Jose Carlos Pastor. Loss of Visual Acuity after Successful Surgery for Macula-On Rhegmatogenous Retinal Detachment in a Prospective Multicentre Study. Journal of Ophthalmology. 2015:821864, 2015. DOI: 10.1155/2015/821864\n\nIvan Fernandez-Bueno; Salvatore Di Lauro; Ivan Alvarez; Jose Carlos Lopez; Maria Teresa Garcia-Gutierrez; Itziar Fernandez; Eva Larra; Jose Carlos Pastor. Safety and Biocompatibility of a New High-Density Polyethylene-Based\nSpherical Integrated Porous Orbital Implant: An Experimental Study in Rabbits. Journal of Ophthalmology. 2015:904096, 2015. DOI: 10.1155/2015/904096\n\nPastor JC; Pastor-Idoate S; Rodríguez-Hernandez I; Rojas J; Fernandez I; Gonzalez-Buendia L; Di Lauro S; Gonzalez-Sarmiento R. Genetics of PVR and RD. Ophthalmologica. 232 - Suppl 1, pp. 28 - 29. 2014\n\nRodriguez-Crespo D; Di Lauro S; Singh AK; Garcia-Gutierrez MT; Garrosa M; Pastor JC; Fernandez-Bueno I; Srivastava GK. Triple-layered mixed co-culture model of RPE cells with neuroretina for evaluating the neuroprotective effects of adipose-MSCs. Cell Tissue Res. 358 - 3, pp. 705 - 716. 2014.\nDOI: 10.1007/s00441-014-1987-5\n\nCarlo De Werra; Salvatore Condurro; Salvatore Tramontano; Mario Perone; Ivana Donzelli; Salvatore Di Lauro; Massimo Di Giuseppe; Rosa Di Micco; Annalisa Pascariello; Antonio Pastore; Giorgio Diamantis; Giuseppe Galloro. Hydatid disease of the liver: thirty years of surgical experience.Chirurgia italiana. 59 - 5, pp. 611 - 636.\n(Italia): 2007. ISSN 0009-4773\n\nChapters in books\n\t\n' Salvador Pastor Idoate; Salvatore Di Lauro; Jose Carlos Pastor Jimeno. PVR: Pathogenesis, Histopathology and Classification. Proliferative Vitreoretinopathy with Small Gauge Vitrectomy. Springer, 2018. ISBN 978-3-319-78445-8\nDOI: 10.1007/978-3-319-78446-5_2. \n\n' Salvatore Di Lauro; Maria Isabel Lopez Galvez. Quistes vítreos en una mujer joven. Problemas diagnósticos en patología retinocoroidea. Sociedad Española de Retina-Vitreo. 2018.\n\n' Salvatore Di Lauro; Salvador Pastor Idoate; Jose Carlos Pastor Jimeno. iOCT in PVR management. OCT Applications in Opthalmology. pp. 1 - 8. INTECH, 2018. DOI: 10.5772/intechopen.78774.\n\n' Rosa Coco Martin; Salvatore Di Lauro; Salvador Pastor Idoate; Jose Carlos Pastor. amponadores, manipuladores y tinciones en la cirugía del traumatismo ocular.Trauma Ocular. Ponencia de la SEO 2018..\n\n' LOPEZ GALVEZ; DI LAURO; CRESPO. OCT angiografia y complicaciones retinianas de la diabetes. PONENCIA SEO 2021, CAPITULO 20. (España): 2021.\n\n' Múltiples desprendimientos neurosensoriales bilaterales en paciente joven. Enfermedades Degenerativas De Retina Y Coroides. SERV 04/2016. \n' González-Buendía L; Di Lauro S; Pastor-Idoate S; Pastor Jimeno JC. Vitreorretinopatía proliferante (VRP) e inflamación: LA INFLAMACIÓN in «INMUNOMODULADORES Y ANTIINFLAMATORIOS: MÁS ALLÁ DE LOS CORTICOIDES. 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It has become a massive part of our daily lives, making predictions based on experience, making this a fascinating area that solves problems that otherwise would not be possible or easy to solve. This topic aims to encompass algorithms that learn from experience (supervised and unsupervised), improve their performance over time and enable machines to make data-driven decisions. 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The area covers many techniques that offer solutions to emerging problems in robotics and enterprise-level software systems. Collaborative intelligence is highly and effectively achieved with multi-agent systems. Areas of application include swarms of robots, flocks of UAVs, collaborative software management. Given the level of technological enhancements, the popularity of machine learning in use has opened a new chapter in multi-agent studies alongside the practical challenges and long-lasting collaboration issues in the field. It has increased the urgency and the need for further studies in this field. We welcome chapters presenting research on the many applications of multi-agent studies including, but not limited to, the following key areas: machine learning for multi-agent systems; modeling swarms robots and flocks of UAVs with multi-agent systems; decision science and multi-agent systems; software engineering for and with multi-agent systems; tools and technologies of multi-agent systems.",annualVolume:11423,isOpenForSubmission:!0,coverUrl:"https://cdn.intechopen.com/series_topics/covers/27.jpg",editor:{id:"148497",title:"Dr.",name:"Mehmet",middleName:"Emin",surname:"Aydin",fullName:"Mehmet Aydin",profilePictureURL:"https://mts.intechopen.com/storage/users/148497/images/system/148497.jpg",institutionString:null,institution:{name:"University of the West of England",institutionURL:null,country:{name:"United Kingdom"}}},editorTwo:null,editorThree:null,editorialBoard:[{id:"275140",title:"Dr.",name:"Dinh Hoa",middleName:null,surname:"Nguyen",fullName:"Dinh Hoa Nguyen",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRbnKQAS/Profile_Picture_1622204093453",institutionString:null,institution:{name:"Kyushu University",institutionURL:null,country:{name:"Japan"}}},{id:"20259",title:"Dr.",name:"Hongbin",middleName:null,surname:"Ma",fullName:"Hongbin Ma",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002bRhDJQA0/Profile_Picture_2022-05-02T08:25:21.jpg",institutionString:null,institution:{name:"Beijing Institute of Technology",institutionURL:null,country:{name:"China"}}},{id:"28640",title:"Prof.",name:"Yasushi",middleName:null,surname:"Kambayashi",fullName:"Yasushi Kambayashi",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0030O00002aYOQxQAO/Profile_Picture_1625660525470",institutionString:null,institution:{name:"Nippon Institute of Technology",institutionURL:null,country:{name:"Japan"}}}]}]}},libraryRecommendation:{success:null,errors:{},institutions:[]},route:{name:"chapter.detail",path:"/chapters/62642",hash:"",query:{},params:{id:"62642"},fullPath:"/chapters/62642",meta:{},from:{name:null,path:"/",hash:"",query:{},params:{},fullPath:"/",meta:{}}}},function(){var e;(e=document.currentScript||document.scripts[document.scripts.length-1]).parentNode.removeChild(e)}()