Histamine liberator food.
\r\n\tThe most phenomena of colloids in the surrounding ecosystem appear in the blue color of the sky, which due to the scattering of light by colloidal particles in the air, and this phenomenon is named Tyndall effect. Also, seawater seems blue due to scattering of light by the colloidal particle present in seawater. In our body, blood is a colloidal solution. Some examples in our daily life include milk, cream, gelatin, colored glass, butter, jelly, and river mud. Colloids are useful for human health, commercial, and industrial use. Colloids and colloidal systems are essential and play a significant role in our life. Important applications of colloids are in medicines, sewage disposal, purification of water, cleansing action of soap, the formation of the delta, industry, mining, smoke precipitation, photography, electroplating, artificial rain, agriculture, the rubber industry, and others.
\r\n\r\n\tThis book aims to gather recent researches by outstanding experts in the field of colloids (chemistry, physics, biology, medicine, nanotechnology, pharmacology, and others), which include colloid synthesis, modification, and application.
",isbn:"978-1-83962-979-2",printIsbn:"978-1-83962-969-3",pdfIsbn:"978-1-83962-980-8",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"55025219ea1a8b915ec8aa4b9f497a8d",bookSignature:"Prof. Mohamed Nageeb Rashed",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/10505.jpg",keywords:"Colloids, Biotechnology, Industry, Colloidal Systems, Human Health, Nutrition, Intravenous Therapy, Pharmacology, Drugs, Wastewater Treatment, Nanocolloids, Green Nanocolloids",numberOfDownloads:439,numberOfWosCitations:0,numberOfCrossrefCitations:0,numberOfDimensionsCitations:0,numberOfTotalCitations:0,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"June 30th 2020",dateEndSecondStepPublish:"July 21st 2020",dateEndThirdStepPublish:"September 19th 2020",dateEndFourthStepPublish:"December 8th 2020",dateEndFifthStepPublish:"February 6th 2021",remainingDaysToSecondStep:"6 months",secondStepPassed:!0,currentStepOfPublishingProcess:5,editedByType:null,kuFlag:!1,biosketch:"Professor of analytical and environmental chemistry, member of several national and international societies, and winner of the Egyptian State Award for Environmental Researches.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"63465",title:"Prof.",name:"Mohamed Nageeb",middleName:null,surname:"Rashed",slug:"mohamed-nageeb-rashed",fullName:"Mohamed Nageeb Rashed",profilePictureURL:"https://mts.intechopen.com/storage/users/63465/images/system/63465.gif",biography:"Prof. Mohamed Nageeb Rashed is a professor of analytical and environmental chemistry, a previous vice-dean for environmental affairs, Faculty of Science, Aswan University, Egypt. In 1989 he received his Ph.D. in analytical environmental chemistry from Assiut University, Egypt. His research interest has been analytical and environmental chemistry with special emphasis on soil and water pollution monitoring, control and treatment; bioindicators for water pollution monitoring; wastewater impact; advanced oxidation treatment; photocatalysis, nanocatalyst, nanocomposite and adsorption techniques in water and wastewater treatment. Prof. Rashed supervised several M.Sc. and Ph.D. thesis in the field of pollution, analytical and environmental chemistry. He participated as an invited speaker in 30 international conferences worldwide. Prof.Rashed acts as editor-in-chief and an editorial board member in several international journals (30) in the fields of chemistry and environment. His society membership includes several national and international societies. Prof.Rashed was awarded the Egyptian State Award for Environmental Researches for the year 2001, and enrolled among Top 2% Scientists Around the World from Stanford University, USA, 2020.",institutionString:"Aswan University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"2",totalChapterViews:"0",totalEditedBooks:"3",institution:{name:"Aswan University",institutionURL:null,country:{name:"Egypt"}}}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"8",title:"Chemistry",slug:"chemistry"}],chapters:[{id:"74126",title:"A Simple and “Green” Technique to Synthesize Metal Nanocolloids by Ultrashort Light Pulses",slug:"a-simple-and-green-technique-to-synthesize-metal-nanocolloids-by-ultrashort-light-pulses",totalDownloads:53,totalCrossrefCites:0,authors:[null]},{id:"74914",title:"Hydrocolloids in Dentistry: A Review",slug:"hydrocolloids-in-dentistry-a-review",totalDownloads:2,totalCrossrefCites:0,authors:[null]},{id:"73791",title:"Gemini Imidazolinium Surfactants: A Versatile Class of Molecules",slug:"gemini-imidazolinium-surfactants-a-versatile-class-of-molecules",totalDownloads:25,totalCrossrefCites:0,authors:[null]},{id:"74505",title:"Optimization of Biogenic Synthesis of Colloidal Metal Nanoparticles",slug:"optimization-of-biogenic-synthesis-of-colloidal-metal-nanoparticles",totalDownloads:100,totalCrossrefCites:0,authors:[null]},{id:"74609",title:"Magnetic Iron Oxide Colloids for Environmental Applications",slug:"magnetic-iron-oxide-colloids-for-environmental-applications",totalDownloads:73,totalCrossrefCites:0,authors:[null]},{id:"73859",title:"Colloidal Stability of Cellulose Suspensions",slug:"colloidal-stability-of-cellulose-suspensions",totalDownloads:55,totalCrossrefCites:0,authors:[null]},{id:"73574",title:"Structure and Dynamics of Aqueous Dispersions",slug:"structure-and-dynamics-of-aqueous-dispersions",totalDownloads:101,totalCrossrefCites:0,authors:[null]},{id:"72963",title:"Aerogels Utilization in Electrochemical Capacitors",slug:"aerogels-utilization-in-electrochemical-capacitors",totalDownloads:33,totalCrossrefCites:0,authors:[{id:"271773",title:"Dr.",name:"Ranganatha",surname:"S",slug:"ranganatha-s",fullName:"Ranganatha S"}]}],productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"205697",firstName:"Kristina",lastName:"Kardum Cvitan",middleName:null,title:"Ms.",imageUrl:"https://mts.intechopen.com/storage/users/205697/images/5186_n.jpg",email:"kristina.k@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. 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Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"54493",title:"How Does Chloroplast Protect Chlorophyll Against Excessive Light?",doi:"10.5772/67887",slug:"how-does-chloroplast-protect-chlorophyll-against-excessive-light-",body:'\nPigments in plants, cyanobacteria, algae and photosynthetic anoxygenic bacteria are the most important molecules involved in photosynthesis, the only biological process that tunnels energy on Earth. Pigments play two key roles in photosynthesis: they absorb sunlight and transduce it into chemical energy. The most important pigment is certainly chlorophyll (Chl), an organic compound that typically shows chlorine, a cyclic tetrapyrrole ring, coordinated to a central atom of magnesium (Figure 1). This molecular structure is very similar to that found in the eme group in which the central atom is iron. Diversification of various Chls is due to the different side chains bonded to the chlorine ring (Chl a, b, c, d, e and f).
Structures of the chlorophyll molecules.
The process of light absorption consists of a sequence of photophysical and photochemical reactions that are subdivided into three stages: (i) light absorption, (ii) utilization of this energy to synthesize ATP and reducing power, reduced ferredoxin (Fd) and NADPH and (iii) absorption and reduction of atmospheric CO2 into carbon skeleton. However, the most important and true light reaction is represented by charge separation that occurs at the reaction centres. The process is possible for the presence of organic molecules able to capture sunlight and transduce it in chemical energy namely photosynthetic pigments and that is chlorophylls and, carotenoids. These pigments aggregate with proteins and act as an antenna harvesting the energy of sunlight and tunnelling this energy into the reaction centres located in photosystems. In plants and algae, there are about 200–400 light harvesting molecules. Light harvesting complexes have evolved many adaptive mechanisms that permit photosynthetic organisms to thrive in different environments. The spectral distribution of sunlight that reaches our planet largely covers the absorption spectra of photosynthetic pigments utilized in light harvesting antennas (Figure 2). In a general way, light harvesting antennas have developed the ability to optimize light capture under both low- and high-intensity light conditions [1].
Chlorophyll a, b and carotenoids absorbance spectra.
The optimal absorption wavelength range for light harvesting antennas is in the red region (680–690 nm), where the energy is utilized by chlorophyll to split water and reduce ferredoxin. The evolution of the most abundant pigments, chlorophyll a, is probably related to its efficient absorption in this region in addition to, perhaps, its chemistry and for its redox potential.
\nAll photosynthetic pigments show a chromophore, which possesses two orbitals whose difference in energy falls within the light spectrum. In consequence, a photon of incident light is able to excite an electron from its ground-state orbital to the excited state. From a chemical point of view, the chromophore exists as conjugated π-electron systems or metal complexes. In a conjugated π system, electron excitation occurs between π orbitals spread across alternating single and double bounds (e.g., carotenoids). The metal complex chromophores share d orbitals between transition metals and ligands (e.g., chlorophylls). Really, in the antenna pigments, chromophores are not individual entities, and they synergically interact with each other and this interaction plays a crucial role in the light harvesting mechanism.
\nLight-harvesting complex (LHC) is the complex of subunit proteins that may be part of a larger supercomplex of a photosystem and is the functional unit in photosynthesis, devoted to the absorption of sunlight. The energy excitation is first tunnelled among other surrounding molecules of the same complex and then from one LHC to another and then funnelled to reaction centres (RCs), where it is converted into charge separation with 90% quantum efficiency.
\nThe presence of proteins in LHC complexes is attributable to the fact that Chl of RCs cannot absorb sunlight at an efficient rate that is enough for efficient photosynthesis to occur. In fact, Chl molecules in RCs absorb only a few photons each second, which are insufficient to drive electron transport into chloroplast membranes (present in 1 RC of about 300 antenna molecules). To overcome this problem, RCs are associated with antenna pigment-protein complexes that absorb sunlight and very efficiently transfer it to RCs. For the importance of the LHCs in gathering sunlight, they differ in the number of pigments and in their composition and structure in a way that they are an optimized energy collector system (Figure 3). The proteins play an important function in the precise position, mutual separation and relative orientation of antenna.
A schematic representation of the light absorption process of chloroplasts. Antenna complexes, composed of carotenoids, Chl a and Chl b molecules, absorb photons from sunlight and transfer them to the RC, which consists of a special couple of molecules of Chl a. Antenna complexes and the RC form a photosystem.
Photosynthetic unit (PSU) represents the basic unit of the light-harvesting apparatus and consists of a large number of antenna chromophores coupled to a RC. Excitation-transfer pathways follow a scheme in which different chromophores build an energy funnel where chromophores, which absorb in the blue side of spectrum, transfer excitation energy to more red-shifted chromophores (Figure 3). Theoretically, the PSUs are considered individual entities but [2] proposed the lake and puddle model. In the second model, the PSUs do not interact with each other and the excitation light absorbed by chromophores is always transferred to the same RC. Differently, in the lake model, the antenna chromophores form a matrix with embedded RCs in which there is an unrestricted energy transfer.
Photosynthesis starts with light absorption by the chromophores, which excites the molecules from the ground state to an electronic excited state. Once sunlight energy is absorbed, pigments in the excited state have a short life and relax to the ground state after about 4 ns [3]. The singlet excited state lifetime of Chl is lower compared with the radiative lifetime, largely owing to intersystem crossing, which yields triplet excited states of Chl (about 10 ns) [4]. This electronic excitation must be usefully harvested before the molecules relax, and this happens when excitons are transferred through space among chromophores until they reach, eventually, a RC where charge separation occurs. In plants, there are two RCs constituted by two Chl molecules, P680 and P700, respectively, for PSII and PSI, and Chl with absorbance maxima corresponding to these wavelengths is proposed as the final slight sink. These chlorophylls drive electron transfer by charge separation, a reaction in which P680 and P700 molecules reduce an acceptor. These driving reactions energetically downhill from the potential that is more negative to ones that are more positive (Figure 4). All these electron transfer steps in photosynthesis share a common feature. The loss of an electron from one component, which remains in an oxidized state, reduces another one. Typically, electron transport carriers are small molecules or atoms of metallic elements that can exist in a number of valence states.
A representation of the linear non-cyclic (solid line) and cyclic electron flow (dashed line) in the chloroplast membranes. OEC tetranuclear Mn cluster; P680, reaction centre of photosystem II (PSII); P680*, excited electronic state of P680; Ph, pheophytin; QA and QB, plastoquinone; protein complex containing cytochrome b6 and cytochrome f; PC, plastocyanin; P700, reaction centre of PSI; P700*, excited electronic state of P700; A0, a special chlorophyll a molecule; A1, phylloquinone; Fe-S, iron sulphur centres; Fd, ferredoxin; NADP, nicotinamide-adenine dinucleotide phosphate and FNR, ferredoxin-NADP+ reductase.
In photosystem RCs, the light-induced loss of an electron (charge separation) leaves P680 and P700 in an oxidized state (P680+ and P700+) and the respective acceptors, pheophytin for P680 and A0 (chlorophyll), in a reduced state. P680+ is reduced from an adjacent tyrosine molecule (TyrZ) in the polypeptide chain of the D1 protein of the PSII complex. In turn, the oxidized is reduced by electrons from the oxygen-evolution complex (OEC) that oxidized water. Two water molecules are oxidized to produce oxygen, four protons and four electrons that are transferred one at a time. These redox reactions are carried out by OEC that consists of four manganese atoms held in a protein matrix with one atom of calcium and chlorine each (Figure 4). This process is known as a S-cycle from [5] that provides protons derived from water oxidation to be released into the lumen of the thylakoid membranes.
\nIn the other set of reactions, reduced pheophytin is oxidized by passing an electron to the first of two plastoquinone (PQ) molecules, tightly bound at the site QA of D2 protein in the PSII. Then, via an iron atom, an electron is transferred to the next PQ at the site QB. Both PQs require two electrons for their complete reduction; at the QA site, PQ undergoes to a single reduction event to the semiquinone state before being re-oxidized by the PQ at QB site. Two successive reductions occur that fully reduce PQ at QB site, which, for its reduction, requires also two protons from the stromal side of the membranes and forms PQH2 that leaves PSII and diffuses in the lipid bilayer, representing a mobile carrier of protons and electrons. A new molecule of PQ (in oxidized form) replaces this plastoquinone in the QB site.
\nPQH2 formed by the PSI activity represents the substrate of the Q cycle on cytochrome b6 f, another integral transmembrane protein complex on thylakoid membranes. PQH2 is oxidized in two steps to PQ. The first step happens at Qp site, located on the luminal side of cytochrome b6 f, and the electron is transferred at the end to plastocyanin (PC), a soluble small protein containing copper. The second electron is transferred until Qn site located on the stromal side of the cytochrome where it reduces further PQ molecule to semiplastoquinone. Another PQH2 molecule originating from PSII is oxidized in the same two steps at the Qp site, generating further a reduced plastocyanin and completing the reduction of semiplastoquinone to PQH2. The oxidation of PQH2 at Qp site determines the release of two protons in the lumen that represents the most important feature of the Q cycle. In fact, this cycle acts as a proton pump, essential to generate the transmembrane electrochemical H+ gradient.
\nAfter light absorption and charge separation in PSI, P700+ is generated, and it is reduced back to P700 by direct interaction with reduced PC diffusing from cytochrome b6 f complex. Plastocyanin, from its copper atom, reduces directly P700+. The electron flow generated by charge separation that occurs in P700 determines the reduction of different carriers, and the final electron acceptor is represented by Fd, a small water-soluble iron-sulphur protein. Reduced Fd is capable of reducing a variety of molecules. Usually, it reduces NADP+, which requires two electrons and two protons to yield NADPH in a reaction catalyzed by ferredoxin-NADP+ reductase (FNR) (Figure 4), thus completing the so-called Z scheme. The electron flow generates even chemical energy, that is ATP, by the enzymatic activity of ATP-ase, a transmembrane complex that utilizes the proton gradient generated by Q cycle and water oxidation, to synthetize ATP.
In the past, the higher order structure of PSII was thought to be important only to increase the efficiency of light harvesting; nowadays, it has been suggested that it provides the essential dynamic properties involved in its regulation [6]. When light is low, in a way, extremely efficient antenna systems absorb light and tunnel it through RC, but when light is in excess, a large extent of this energy is dissipated, overall as heat, to prevent photo-damage to PSUs. When plants are exposed to shade or sunlight conditions, different mechanisms occur. Shade leaves are typically larger in area but thinner than sun leaves because they develop shorter palisade cells. In shade leaves, the chloroplasts move within the cells to take up a position where they will absorb the maximum light without shading other chloroplasts below. In addition, shade leaves show a large number of antenna, and usually, the peripheral antenna are rich in Chl b molecules (Chl a/b = 1.33). All these mechanisms enhance and optimize the light absorption. However, even shade leaves have adapted mechanisms aimed to regulate the light absorption, as the state II-I transition (also called spillover process). The aim of this process is the reduction of light tunnelled to P680 altering the ratio of light energy absorbed between PSII and PSI. In fact, RCs of the two photosystems have different absorption spectra (high energy is absorbed by P680 as compared with P700), and this determines that when the energy flow through each is not balanced to the requirement of the Z scheme, an excess of energy could accumulate in the system. In this way, LHCII trimers represent a feedback loop that adjusts the amount of antenna Chls, providing energy to each photosystem (state transition). The excess of light energy flowing through PSII RCs is higher than that flowing through PSI RCs, conditions in which an excess of reduced PQ occurs. This activates a kinase that phosphorylates some LHCII trimers, and this extra charge allows them to dissociate from the PSII (state II) and migrate towards the stroma lamellae (state I transition) where they bind to the PSI complex, increasing in this way the flow through the system. The increase of PSI activity leads to the oxidation of reduced PQ, which activates a phosphatase that removes the phosphate group to the LHCII trimers that return to PSII (state II transition).
\nIn contrast, sun leaves live in very high radiation levels overall at the top of the canopy. The light response curve in relation to the light intensity shows that the amount of energy utilized is lower than that absorbed because the light energy utilized in carbon reduction is mostly due to the limitation on the rate of CO2 diffusing into the leaf (Figure 5). In these conditions, the antenna Chls become saturated and tunnel a high flow of the excitation energy to the RC that cannot be dissipated along the electron flow. The excess of energy must be efficiently dissipated through different mechanisms in order to avoid photo-damage to PSII.
Absorbed and utilized energy in response to increasing light intensities. When light absorbed exceed photosystems requirement, the ‘excess energy’ can potentially cause photo-oxidative damage if it is not efficiently dissipated.
Photosystem II is particularly sensitive to photoinhibition because the high redox potential of the oxidized P680 (P680+), on the other hand, necessary for water oxidation. Accumulation of P680+ leads to different types of photoinhibition:
\nAcceptor-side photoinhibition: when reduced PQ is not re-oxidized, the P680* charge recombination is inhibited and P680 is expected to lead to the triplet state of P680, TP680*. This chemical species may react with oxygen and produce harmful singlet oxygen.
Donor-side photoinhibition: if the OEC is chemically inactivated, the donation of electrons from water does not keep up with the electron transfer from P680 to the acceptor side. In this case, an accumulation of P680+ occurs. The high redox potential of this chemical species induces the oxidation of various organic components such as proteins or pigments until damage is done to D1 protein of PSII.
Different mechanisms are present in PSII aimed to dissipate the excess of photons absorbed by antenna, and different defence lines occur into the chloroplast.
First line of chloroplast defence includes suppression mechanisms aimed to reduce or dissipate the excitation light tunnelled in P680. At leaf level, the change in the leaf angle with respect to the incident light and/or the chloroplast movement into the leaf to self-shading positions along the sidewalls of cells represent mechanisms by which a decrease in absorbed light can occur.
\nIn the chloroplast, there are essentially three mechanisms to contrast the high light conditions: adjustment in synthesis and amount of antenna protein, movement of LHCII (state II-I transition) and non-photochemical quenching [7]. The first of these mechanisms is related to the expression of Lhcb genes, whose expression is downregulated by high light conditions and/or low CO2 concentration. The sensor mechanism is not known even though one possible candidate is the redox potential (i.e., the level of reduced PQ) [8], but also ROS represent possible signal molecules [9, 10]. Clearly, these slow mechanisms cannot entirely prevent the accumulation of excess of energy in the antenna system. However, photosynthesis in green plants depends on protective mechanisms that adapt within minutes or seconds to changing light conditions. Excited Chls return to the ground state either by emitting photons (fluorescence) or by dissipating it as heat. All these mechanisms aimed to remove this trapped energy before it passed on down the electron transport chain are named non-photochemical quenching (NPQ). NPQ is heterogeneous and composed by at least three components: the major and rapid component is the pH- or energy-dependent component qE, a second component qT, related to the phenomenon of state transition but negligible in most of plants under excess light and the third and slow component, qI, related to the photoinhibition of photosynthesis [11].
\nIt has been reported that two distinct qE mechanisms occur, one involving zeaxanthin (Zea) (quenching type 1) and the other carotenoid lutein (Lut) (quenching type 2) [12]. In qE type I, three xanthophylls, violaxanthin (Vio), anteraxanthin (Ant) and Zea, are involved in the well-known xanthophyll cycle in which the epoxidation of Vio to Zea via Ant determines an efficient dissipation of excess light into heat [13]. Electron flow pumping and generating protons in the lumen decrease its pH from about 7 to less than 5; this represents a strong signal that starts a series of quenching processes. The low pH-induced protonation of PsbS peptide, for its proximity to antenna complexes (CP24, CP26 and CP29), induces in turn in these complexes conformational changes. In the chemical state, antenna complexes bind one molecule of Zea and one of Chl (Zea-Chl complex = quenching complex) that accept energy transfer from excited Chls. Zeaxanthins are able to return to their ground state dissipating energy as heat :
\nIt has been reported that in the crystal structure of LHCII is present Vio, and its peripheral localization suggests that it could be de-epoxidized to Zea by Vio de-epoxidase (VDE), an enzyme that is activated by low lumen pH occurring in high light conditions. The back reaction by Zea epoxidase is slow and causes a sustained quenching that relaxes within 1–3 hours following light stress and depends on the release of Zea from antenna pigments. In conclusion, Zea is certainly considered a regulator of light harvesting for its role in the xanthophyll cycle and carries out three fundamental roles during high light conditions: (i) protection against photo-oxidation due to radical oxygen’s attack (because it quenches oxygen singlet energy), (ii) absorption of Chl triplet energy and (iii) absorption of incoming photons and transferring them to neighbouring Chl molecules increasing in this way the overall absorption spectrum of the PSs [14]. In addition, it has been reported that this xanthophyll exhibits an antioxidant function in the thylakoid membrane [15].
\nIn addition, trimeric LHCII binds other types of xanthophylls: two all-trans-luteins and a 9-cis-noexanthin [16]. The minor monomeric complexes CP24, CP26 and CP29 all bind Lut, and in addition, CP29 binds two xanthophyll cycle carotenoids and one-half to one neoxanthin (Neo), CP24 binds two xanthophyll cycle carotenoids and CP26 binds one xanthophyll cycle carotenoids and one Neo [17, 18]. In the quenching type 2, qE is an intrinsic LCHII property: protein conformational changes alter configurations of bound pigment (normally Lut), which become an efficient quencher of Chl-excited state [12]. A change in the conformational state of another LHCII-bound xanthophyll, Neo, correlates with the extent of quenching. In the model for type 2 quenching proposed by [19], Zea acts not as a quencher but as an allosteric modulator of the ΔpH sensitivity of this intrinsic LHCII quenching process. The two types of quenching involved different xanthophylls that operate at different sites, but there are some similarities in the reasons that both involve ΔpH and PsbS-mediated conformational changes [12].
\nGiven that the xanthophyll cycle quenches only 95% of the triplet Chl [20], the unquenched triplet Chl is the reason for the need of singlet oxygen not only scavenging by carotenoids bound to LHCII but also by carotenoids free in lipid matrix [21]. Lut has the specific property of quenching harmful 3Chl* by binding at site L1 of the major LHCII complex and of other Lhc proteins of plants, thus preventing ROS formation [20]. Neo contributes PSII photoprotection in a dual way: determins conformational change in trimeric LHCII, which reduces light absorption and controls the accessibility of the O2 to the inner core of the complex [20, 22]. The trimeric organization of LHCII is, definitively, effective in screening the internal protein domain from molecular oxygen [23].
As reported above, the excess of excitation energy induces an excess of singlet-excited Chl a that is de-excited via thermal dissipation. However, the remaining singlet-excited Chl a can convert to triplet-excited Chl that readily reduces molecular oxygen. This determines the synthesis of ROS that is potentially dangerous to organic molecules in the chloroplast. In the second line of defence, antioxidant molecules and enzymes that together scavenge ROS play a key role.
\nThe primary products of molecular oxygen reduction are disproportionate to H2O2 and O2 in a reaction catalyzed by superoxide dismutase (SOD). H2O2 produced is then reduced to water with the reducing power of ascorbate (ASA) in a reaction catalyzed by ASA peroxidase (APX), and ASA is oxidized to monodehydroascorbate (MDHA) that is directly reduced to ASA by reduced ferredoxin or NADPH by MDHA reductase. Alternatively, MDHA is spontaneously disproportionated to dehydroascorbate (DHA) and ASA. DHA is then reduced by reduced glutathione (GSH), by the enzyme DHA reductase that produces oxidized glutathione (GSSG) and ASA. Finally, GSSG is reduced again in GSH by the action of GSH reductase, and the reducing power is represented by reduced Fd or NADPH, that, in turn, are reduced by PSI activity. This indicates that any pathway aimed to regenerate ASA utilizes electrons derived from water. For this reason, the previous process is referred as water-water cycle [10].
\nIn addition to the primary antioxidant systems, carotenoids have a protective role against ROS since they are very efficient physical and chemical quenchers of singlet oxygen and potent scavengers of other free radicals [24]. For example, β-carotene, located in the core complex of both PSII and PSI, plays a role as a quencher of Chl triplet and singlet oxygen [25], and the products generated from the oxidation of β-carotene by singlet oxygen represent primary sensor signalling under oxidative stress [26]. Other carotenoids play an important role as antioxidants in the chloroplast. Lut is the most abundant carotenoid in the chloroplast and is required as a quencher [7], while Neo can scavenge superoxide anion [27]. The antioxidant activity of carotenoids is carried out in combination with other lipophilic antioxidants. In this way, it has been reported that Zea, in cooperation with tocopherol, prevented photo-oxidation induced by high light [28], or a strong increase in carotenoids pigment (including those involved in xanthophyll cycle) is reported together with the activity of SOD enzyme following oxidative stress [29]. Again, carotenoids can influence the structure and fluidity of thylakoid membranes [30], that is essential for photosynthetic functions, influence barrier status to ions and oxygen, increase thermostability and protect against lipid peroxidation. In fact, as reported by [30], β-carotene can fluidize the membrane because it can move in the inner hydrophobic part of the membrane, and xanthophyll (and in particular Zea) shows the polar group that orientates these carotenoids perpendicular to the membrane surface.
In the last 30–40 years, the susceptibility of D1 protein to photo-damage has been well known, and the concept of the replacement of the damaged D1 protein during the repair cycle of PSII is extensively investigated [13, 31–33]. Moreover, D1 damage has been shown to be directly proportional to light intensity [34].
\nThe repair process of photo-damaged D1 proteins consists of different steps: (i) prompt, partial disassembly of the PSII holocomplex, (ii) exposure of the photo-damaged PSII core to the stroma of the chloroplast, (iii) degradation of photo-damaged D1, (iv) de novo D1 biosynthesis and insertion in the thylakoid membrane and (v) re-assembly of the PSII holocomplex, followed by activation of the electron-transport process through the reconstituted D1/D2 heterodimer [35]. The sequence leading to the recovery of photo-damaged PSII is consistent with the frequent D1 turnover in the chloroplast and with the heterogeneity in the configuration and function of PSII.
\nIn the past, the sensibility of PSII was linked to an inherent defect of photosynthetic apparatus but now it is clear how this mechanism of damage-repair of PSII is extremely regulated [33] and protects even PSI from irreversible damage. In fact, the repair mechanisms in PSI are time and high energy consuming, and it has been suggested that the inhibition of PSII is likely to protect PSI [33].
\nReduced Fd plays an important role in preventing the over-reduction of electron flow, and a wide range of electron sinks are available in chloroplasts. Electrons are preferentially utilized by the FNR enzyme that produces NADPH for CO2 photoassimilation or ferredoxin:thioredoxin reductase that synthesizes thioredoxin responsible for the regulation of some enzymes of Calvin-Benson cycle [36]. On the other hand, reduced Fd can release electrons also to ferredoxin:nitrite reductase and sulphite reductase for the reductive assimilation of nitrite [37] and sulphur [38]. Finally, reduced Fd represents an electron donor for fatty acid desaturases [39] and glutamine:oxoglutarate amino transferase [40]. However, when NADP+ is not available, reduced Fd releases its electron to different acceptors whose function is to avoid an over-reduction of PSI [41]. It has been discovered that there is an electron transport driven solely by PSI and scientists called it cyclic electron flow. In this cycle, electrons can be recycled from reduced Fd to PQ and subsequently, to the cytochrome b6 f complex via the Q cycle [42]. Such cyclic flow generates ΔpH and thus ATP without the accumulation of reduced species. In addition, the generated ΔpH may regulate photosynthesis via NPQ (see Section 4). Another electron acceptor of reduced Fd is molecular oxygen inducing the pseudo-cyclic electron flow. The reduction of molecular oxygen with one electron generates superoxide anions in the so-called Mehler reaction, which restores the redox poise when linear electron flow is over-reduced [43]. The radical oxygen species is efficiently removed by water-water cycle. Chlororespiration is another effective electron sink in which reduced Fd is directly involved. In this process, two enzymes play the key role: NADH dehydrogenase complex and nucleus-encoded plastid-localized terminal oxidase (PTOX). The enzyme PTOX catalyzes the reaction in which electrons are transferred from PQH2 to molecular oxygen forming water [44].
\nFinally, in addition to the above-reported electron flow, photorespiration is another efficient pathway by which plants adjust the ATP/NADPH ratio and consume the excess of excitation energy.
Certainly, Chls represent the key molecules involved in light energy absorption and transduction into chemical energy. Chls absorb the light energy that reaches leaves in a very efficient manner but sometimes, light exceeds photochemistry requirement, and the complexity of photosystems is essential to modulate and dissipate excess of excitation energy. A wide range of responses to environmental stimuli thus characterizes the photoprotection of chloroplasts. The increasing level of complexity from the molecular (pigments and protein) to supramolecular (photosystems) level mirrors the necessity of different time-scale responses (from seconds to months) to modulate light that is (inevitably) absorbed. In the range of seconds to minutes, modulation of the redox state of photosynthetic electron transport activates the non-photochemical quenching of excess of excitation energy not only through xanthophyll cycles [13] but also by II-I state transition [45]. On a larger scale (minutes to hours), modulation of redox state of electron transport induces changes in gene expression (organellar and nucleus) through retrograde regulation that changes the structure of the photosynthetic apparatus [46, 47]. On the time scale from weeks to months, the redox state of electron transport determines changes in plant growth and morphology [48].
The interest in making this chapter was to explain the pathology of chronic urticaria as prevalent and its high morbidity.
We often see this problem in our primary care consultations and emergency services, so we consider its important to make a chapter about urticaria.
The current version of the EAACI/GA2LEN/EDF/WAO urticaria guideline from 2018 contains new aspects about diagnosis and treatment.
At the end of the chapter, we show a series of cases treated in our practice (observed in a Juan Ramon Jimenez’s dermatology room in Huelva, Spain), exposing results obtained with the different forms of treatment (Figure 1).
Chronic urticaria.
Urticaria is a common process. Although the true incidence is not known, it is believed that between 15 and 25% of the population may suffer at some point in his life. Acute urticaria has a prevalence of 20% and the chronic form 0.5–1% [1]. Age, race, sex, occupation, geographical region, and the season of the year may be implicated in urticaria and angioedema. The majority of acute episodes are due to adverse reactions to medications or food or, in children, to viral diseases.
Spontaneous chronic urticaria represents about 70% of all chronic hives and may persist for several years. Patients with chronic urticaria often describe a decrease in the quality of life because of itching and may have alterations of sleep, fatigue, social isolation, or emotional disorders (Figures 2–4).
Epidemiology of chronic urticaria in United States.
Epidemiology of chronic urticaria in Australia.
Prevalence of chronic urticaria.
Urticaria is a disease that affects the skin and mucosa, characterized by the presence of hives. It is a localized intracutaneous edema that circled an area of redness (erythema), which is typically itchy. Individual hives can persist from 30 minutes to 36 hours and can measure from only 1 millimeter up to 15–20 cm in diameter, named giant hives [2]. Increased dilation and permeability of blood vessels that characterize the hives are present in the superficial dermis and undertake the venous plexus located there (Figure 5). It is rare and it may occur with concomitant angioedema.
Urticaria. Picture with histological findings.
Another similar entity is angioedema, with a similar mechanism as urticaria [3], but the pathology is located in the deep dermis and subcutaneous tissue, and swelling is the main manifestation. The skin may be normal or erythematous. There is less itching, but it can cause pain or burning sensation. The mouth, lips, eyes, throat, feet, and hands are most commonly affected (Figures 6 and 7). When angioedema affects the throat, it can be life-threatening, because there is interference in breathing. It is caused by an allergic reaction, sometimes by a hereditary condition (hereditary angioedema), but normally we do not know the cause [3].
Angioedema.
Angioedema.
Foods that require a ripening process to achieve a better taste are presumed to have a high histamine content. In the same way as foods that are made during fermentation. These include de following [4] (Table 1).
Yogurt | Soured cream |
---|---|
Buttermilk | Quark |
Cottage cheese | Alcohol |
Hard cheeses, cheddar | Vinegar |
Aged cheeses, brie | Sauerkraut |
Histamine liberator food.
The Spanish society of diamine oxidase (DAO) states on their website that the following food histamine liberators:
Alcohol, citrus fruits, strawberries, pineapple, kiwi, tomato sauce, seafood, chocolate, fish, mushrooms, pig, cereals, and egg white.
Some food additives such as glutamate, benzoate, several colorants (yellow E-102 and E-110, E-124, amaranth E-123), sulfites, and nitrites can release endogenous histamine.
The department for dermatology in Bonn’s paper lists the following foods as being capable of releasing endogenous histamine (Table 2).
Citrus fruit | Chocolate |
---|---|
Papaya | Fish |
Strawberries | Crustaceans |
Pineapple | Pork |
Nuts | Egg white |
Peanuts | Additives |
Tomatoes | Liquorice |
Spinach | Spices |
Foods as being capable of releasing endogenous histamine.
The mast cell is the main effector cell in urticaria and angioedema. Cutaneous mast cells attach to fibronectin and laminin through the integrin beta1 of Very Late Antigen (VLA), VLA-3, VLA-4, and VLA-5 activation and vitronectin through alfa1 and beta3 integrin [5].
Once activated, the mast cell releases granules containing histamine and other mediators of inflammation such as platelet activating factor (PAF) from, TNF alpha, IL-3, IL-4, IL-5, IL-6, IL-8, IL-13, GM-CSF, PGD-2, and leukotrienes (LTC4, LTD4, LTEA). Histamine, TNF alpha, and IL-8 also stimulate endothelial adhesion molecules that favors the migration of eosinophils, monocytes, and neutrophils from the bloodstream to the skin.
Histamine is an amine vasoactive located in granules of mast cells [5], basophils, and platelets. Its effects on the skin are mediated through histamine H1 and H2 receptors. H1 receptors mediate urticaria vasodilation, increased vascular permeability, and sensory nerve stimulation. Sensory nerve stimulation determines the release of neuropeptides such as substance P, peptide vasoactive intestinal (VIP), and somatostatin, which in turn induce the mast cell activation and increase in histamine.
The vascular endothelium expressed a significant number of H2 receptors, so the vascular response in the UC is an immunomodulatory effect, to increase the synthesis of pro-inflammatory cytokines such as IL-1 and IL-6 of monocytes and IL-6 and IL-8 cell endothelial. In addition to histamine, other soluble factors synthesized by mast cells contribute to the increase of vascular dilation and permeability; favor chemotaxis, cell activation of leukocyte, and endothelial cells; and induce stimulation sensory. These are the cytokines, chemokines, and neuropeptides and arachidonic acid metabolites.
The degranulation is attributed to immunological causes (autoimmune, IgE-dependent, immune complexes, complement-dependent), not immune (pseudoallergies, agents release by mast cells) and idiopathic. The path of the synthesis of prostaglandins and leukotrienes, hours later the mast cell activation, occurs in the synthesis of leukotrienes and prostaglandins from arachidonic acid via two-way enzymatic metabolism: the cyclooxygenase path and the lipoxygenase pathways.
Studies have shown that LTB4 has a potent chemotactic activity, which is produced by mast cells in the early and selective recruitment of leukocytes. At chronic urticaria (CU), these mediators appear to be the most important in the chronicity of the disease. There are no immune reactions (pseudoallergics); the mechanisms are not clear but may compromise the metabolism of arachidonic acid, prostaglandins, and leukotrienes [2] (Figure 8).
Physiopathology of urticaria. Note like that the mast cells are the principal cells implicated.
According to the time evolution, urticaria can be divided into:
Acute urticaria: less than 6 weeks.
Chronic urticaria*: lesions appear for more than 6 weeks [6].
Recurrent urticaria: outbreaks recur over time, but its duration is limited. Episodes of hives last less than asymptomatic intervals.
* Chronic urticaria is divided into two:
Spontaneous chronic urticaria: spontaneous emergence of hives, angioedema, or both for longer than 6 weeks, due to a known or unknown cause.
Inducible urticaria: physical urticarial (This hives occur at the site of the stimulation)l, cholinergic, aquagenic and contact urticarias (Figure 9).
Acute and chronic urticaria.
Urticaria typically presents well circumscribed wheals (polimorphyc, serpenginous or round), with intensely pruritic for less than 24 hours of evolution. Wheals can be generalized, including arms, legs, face. Urticaria +/− angioedema (primarily in the face), can be acute (with an evolution of less than 6 weeks), or chronic (greater than 6 weeks [7] (Figures 10–15).
Generalities of urticaria.
Dermatological manifestations of urticaria. Note the typical hives.
Dermatological manifestations of urticaria. Note the erythema.
Linear hives made by compression.
Coalescing urticarial papules.
Urticaria and angioedema.
For diagnosis we have several tools, among which the most useful, simple, and cost-effective is the clinical history, but we can ask for additional tests in the case of diagnostic doubt or suspicion of systemic disease [8].
A detailed clinical history and a good physical examination of the patient are necessary to make the diagnosis.
Thanks to its history, we can classify chronic urticaria as spontaneous or inducible. For this, we must focus on the following aspects:
A family history of atopy or urticaria.
Commonly used drugs and relation with the hives.
A history of allergies, infections, or any other cause that has been able to trigger hives.
Work performed and hobbies.
Induction of urticaria due to exercise or exposure to physical agents.
How the body reacts to insect bites.
If the patient has been on holidays or trip recently.
If it has relationship with the menstrual cycle or stress.
If the quality of life is affected.
Duration of the disease.
Frequency and duration of the hives, size, shape, and distribution.
If associated symptoms are subjective such as pain, burning, etc.
If the patient has nocturnal or diurnal variation.
How the response was to the treatments used.
Complementary tests serve as support to the diagnosis, to detect associated systemic diseases or for differential diagnosis.
Basic laboratory tests, as blood count and biochemical reaction (determination of C-reactive protein, glomerular sedimentation rate), can help us rule out there is a systemic disease. The baseline of tryptase, antithyroid antibodies, and thyroid profile and study of complement and specific IgE where allergy is suspected, could also be useful. If an infection cause is suspected, hepatitis B and C virus or Helicobacter Pylori could be detected.
New guidelines recommend not to perform additional exploration in a systematic way in acute urticaria and just a complete blood count with ESR and a suspension of nonsteroidal anti-inflammatory drugs (NSAIDs) in the CU (Figure 16).
Diagnosis algorithm.
Different ways are approached for the treatment of urticaria: eliminating histaminergic food such as seafoods, canned goods, tomatoes, strawberries, bananas, pineapple, or apples and avoiding nonsteroidal anti-inflammatory drugs (NSAIDs) [9], nonsedative H1-antihistamines, and in severe cases systemic corticosteroids [10].
The treatment of choice are antihistamines, from a daily tablet up to four tablets as maximum dose.
Corticosteroids are excluded for exacerbations and must be prescribed in short guideline (maximum 10 days) without progressive decrease.
Avoid taking NSAIDs.
Nonsedative H1-antihistamines to full dose (four tablets in a day) [11].
Systemic corticoids, preferably in short treatment (10-day short guideline).
Forms resistant to treatment: biological agents (omalizumab*).
Avoid taking NSAIDs (Figure 17).
Nonsedative antihistamines.
*Omalizumab is a recombinant humanized monoclonal antibody, which blocks the high-affinity Fc receptor of IgE (Figure 18). It has been approved for treatment in cases of moderate-to-severe asthma, but it has promising results in the management also of chronic urticaria [12]. The dose is 150 or 300 mg by subcutaneous injection every 4 weeks. Dosing is not dependent on body weight or serum IgE level. The appropriate duration for CIU has not been evaluated yet. It’s necessary to periodically reassess the need for continued therapy with omalizumab [13].
Monoclonal antibody that binds to the Cε3 domain of circulating IgE, which prevents IgE from binding to and activating receptors in mast cells (Figure 19).
Recommended treatment algorithm for chronic urticaria.
The European Academy of Allergy and Clinical Immunology (EAACI)/Global Allergy and Asthma European Network (GA2LEN)/European Dermatology Forum (EDF)/World Allergy Organization (WAO) and the American Academy of Allergy, Asthma, and Immunology (AAAAI) have some differences in their recommendations for urticaria treatment, but the core recommendations remain similar.
A brief summary of AAAAI guidelines are as follows [14]:
As first-line treatment, second-generation nonsedating H1 antihistamines.
Remain in the treatment algorithm first-generation H 1 antihistamines (differs from EAACI/GA 2LEN/EDF/WAO guidelines).
Second-line options to consider: adding other second-generation H 1 antihistamines, up-dosing second-generation H 1 antihistamines, leukotriene receptor antagonists, adding H 2 antagonists or first-generation H 1 antihistamines at bedtime.
Omalizumab as third-line treatment.
Corticosteroids considered only for short treatment.
Cyclosporine A* is used in refractory chronic urticaria not responsive to other treatments.
A brief summary of EAACI/GA2LEN/EDF/WAO guidelines are as follows:
First-line treatment, second-generation H 1 antihistamines.
Up-dosing second-generation H1 antihistamines are the second-line therapy.
Omalizumab is the third-line treatment, which is recommended because it is less toxic than cyclosporine A.
Not included in algorithm H2 antihistamines (used only on an individual case).
Avoid first-generation H1 antihistamines based on benefit to risk ratio.
Corticosteroids may be considered only for the short-term intervention.
Cyclosporine A for refractory chronic urticaria not responsive to other treatments.
*Cyclosporin A is an immunosuppressive agent, widely used in organ transplantation to prevent rejection.
The current version of the EAACI/GA2LEN/EDF/WAO urticaria guideline recommends:
When chronic inducible urticaria is suspected, differential diagnoses should be ruled out. The diagnosis should be confirmed by provocation test disease. The activity should be measured by determining the trigger threshold disease burden and control should be measured.
Second-generation H1 antihistamines remain the treatment of first choice.
If continuous treatment for 2–4 weeks does not lead to adequate control of symptoms, the guidelines recommend up-dosing (up to four times the standard dose).
If there is no improvement with high-dose antihistamines, it is recommended to add omalizumab to the regimen in patients with chronic spontaneous urticaria.
If there is no success after 6 months of omalizumab therapy, off-label treatment with cyclosporine is recommended.
Assessment scales serve to evaluate the treatment, as well as this pathological entity affects the quality of life of the patient. We have the urticarial activity score (UAS) [15] or angioedema activity score (AAS) [16], chronic urticaria quality-of-life questionnaire, and urticaria control test (UCT).
The current guideline endorses the urticaria activity score and/or the angioedema activity score to assess the disease activity in CSU patients [17] (Figure 20).
UAS.
The urticaria control test should be used in all CSU patients. The UCT is a retrospective tool used to rapidly and reliably assess disease control with four simple questions (Figure 21). Patients answer each of the four UCT questions, and the corresponding points (0–4 per answer) are added up to yield a total score of 0–16. The cutoff for controlled urticaria is 12 points. A score of 11 or less indicates insufficient disease control, whereas a score of 12 or more suggests adequate disease control [18].
Urticaria control test.
None.
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\\n\\n4.1 The Corresponding Author represents and warrants that the Chapter does not and will not breach any applicable law or the rights of any third party and, specifically, that the Chapter contains no matter that is defamatory or that infringes any literary or proprietary rights, intellectual property rights, or any rights of privacy. The Corresponding Author warrants and represents that: (i) the Chapter is the original work of themselves and any Co-Author and is not copied wholly or substantially from any other work or material or any other source; (ii) the Chapter has not been formally published in any other peer-reviewed journal or in a book or edited collection, and is not under consideration for any such publication; (iii) they themselves and any Co-Author are qualifying persons under section 154 of the Copyright, Designs and Patents Act 1988; (iv) they themselves and any Co-Author have not assigned and will not during the term of this Publication Agreement purport to assign any of the rights granted to IntechOpen under this Publication Agreement; and (v) the rights granted by this Publication Agreement are free from any security interest, option, mortgage, charge or lien.
\\n\\nThe Corresponding Author also warrants and represents that: (i) they have the full power to enter into this Publication Agreement on their own behalf and on behalf of each Co-Author; and (ii) they have the necessary rights and/or title in and to the Chapter to grant IntechOpen, on behalf of themselves and any Co-Author, the rights and licenses expressed to be granted in this Publication Agreement. If the Chapter was prepared jointly by the Corresponding Author and any Co-Author, the Corresponding Author warrants and represents that: (i) each Co-Author agrees to the submission, license and publication of the Chapter on the terms of this Publication Agreement; and (ii) they have the authority to enter into this Publication Agreement on behalf of and bind each Co-Author. The Corresponding Author shall: (i) ensure each Co-Author complies with all relevant provisions of this Publication Agreement, including those relating to confidentiality, performance and standards, as if a party to this Publication Agreement; and (ii) remain primarily liable for all acts and/or omissions of each such Co-Author.
\\n\\nThe Corresponding Author agrees to indemnify and hold IntechOpen harmless against all liabilities, costs, expenses, damages and losses and all reasonable legal costs and expenses suffered or incurred by IntechOpen arising out of or in connection with any breach of the aforementioned representations and warranties. This indemnity shall not cover IntechOpen to the extent that a claim under it results from IntechOpen's negligence or willful misconduct.
\\n\\n4.2 Nothing in this Publication Agreement shall have the effect of excluding or limiting any liability for death or personal injury caused by negligence or any other liability that cannot be excluded or limited by applicable law.
\\n\\n5. TERMINATION
\\n\\n5.1 IntechOpen has a right to terminate this Publication Agreement for quality, program, technical or other reasons with immediate effect, including without limitation (i) if the Corresponding Author or any Co-Author commits a material breach of this Publication Agreement; (ii) if the Corresponding Author or any Co-Author (being an individual) is the subject of a bankruptcy petition, application or order; or (iii) if the Corresponding Author or any Co-Author (being a company) commences negotiations with all or any class of its creditors with a view to rescheduling any of its debts, or makes a proposal for or enters into any compromise or arrangement with any of its creditors.
\\n\\nIn case of termination, IntechOpen will notify the Corresponding Author, in writing, of the decision.
\\n\\n6. INTECHOPEN’S DUTIES AND RIGHTS
\\n\\n6.1 Unless prevented from doing so by events outside its reasonable control, IntechOpen, in its discretion, agrees to publish the Chapter attributing it to the Corresponding Author and any Co-Author.
\\n\\n6.2 IntechOpen has the right to use the Corresponding Author’s and any Co-Author’s names and likeness in connection with scientific dissemination, retrieval, archiving, web hosting and promotion and marketing of the Chapter and has the right to contact the Corresponding Author and any Co-Author until the Chapter is publicly available on any platform owned and/or operated by IntechOpen.
\\n\\n6.3 IntechOpen is granted the authority to enforce the rights from this Publication Agreement, on behalf of the Corresponding Author and any Co-Author, against third parties (for example in cases of plagiarism or copyright infringements). In respect of any such infringement or suspected infringement of the copyright in the Chapter, IntechOpen shall have absolute discretion in addressing any such infringement which is likely to affect IntechOpen's rights under this Publication Agreement, including issuing and conducting proceedings against the suspected infringer.
\\n\\n7. MISCELLANEOUS
\\n\\n7.1 Further Assurance: The Corresponding Author shall and will ensure that any relevant third party (including any Co-Author) shall, execute and deliver whatever further documents or deeds and perform such acts as IntechOpen reasonably requires from time to time for the purpose of giving IntechOpen the full benefit of the provisions of this Publication Agreement.
\\n\\n7.2 Third Party Rights: A person who is not a party to this Publication Agreement may not enforce any of its provisions under the Contracts (Rights of Third Parties) Act 1999.
\\n\\n7.3 Entire Agreement: This Publication Agreement constitutes the entire agreement between the parties in relation to its subject matter. It replaces and extinguishes all prior agreements, draft agreements, arrangements, collateral warranties, collateral contracts, statements, assurances, representations and undertakings of any nature made by or on behalf of the parties, whether oral or written, in relation to that subject matter. Each party acknowledges that in entering into this Publication Agreement it has not relied upon any oral or written statements, collateral or other warranties, assurances, representations or undertakings which were made by or on behalf of the other party in relation to the subject matter of this Publication Agreement at any time before its signature (together "Pre-Contractual Statements"), other than those which are set out in this Publication Agreement. Each party hereby waives all rights and remedies which might otherwise be available to it in relation to such Pre-Contractual Statements. Nothing in this clause shall exclude or restrict the liability of either party arising out of its pre-contract fraudulent misrepresentation or fraudulent concealment.
\\n\\n7.4 Waiver: No failure or delay by a party to exercise any right or remedy provided under this Publication Agreement or by law shall constitute a waiver of that or any other right or remedy, nor shall it preclude or restrict the further exercise of that or any other right or remedy. No single or partial exercise of such right or remedy shall preclude or restrict the further exercise of that or any other right or remedy.
\\n\\n7.5 Variation: No variation of this Publication Agreement shall be effective unless it is in writing and signed by the parties (or their duly authorized representatives).
\\n\\n7.6 Severance: If any provision or part-provision of this Publication Agreement is or becomes invalid, illegal or unenforceable, it shall be deemed modified to the minimum extent necessary to make it valid, legal and enforceable. If such modification is not possible, the relevant provision or part-provision shall be deemed deleted.
\\n\\nAny modification to or deletion of a provision or part-provision under this clause shall not affect the validity and enforceability of the rest of this Publication Agreement.
\\n\\n7.7 No partnership: Nothing in this Publication Agreement is intended to, or shall be deemed to, establish or create any partnership or joint venture or the relationship of principal and agent or employer and employee between IntechOpen and the Corresponding Author or any Co-Author, nor authorize any party to make or enter into any commitments for or on behalf of any other party.
\\n\\n7.8 Governing law: This Publication Agreement and any dispute or claim (including non-contractual disputes or claims) arising out of or in connection with it or its subject matter or formation shall be governed by and construed in accordance with the law of England and Wales. The parties submit to the exclusive jurisdiction of the English courts to settle any dispute or claim arising out of or in connection with this Publication Agreement (including any non-contractual disputes or claims).
\\n\\nLast updated: 2020-11-27
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The Corresponding Author (acting on behalf of all Authors) and INTECHOPEN LIMITED, incorporated and registered in England and Wales with company number 11086078 and a registered office at 5 Princes Gate Court, London, United Kingdom, SW7 2QJ conclude the following Agreement regarding the publication of a Book Chapter:
\n\n1. DEFINITIONS
\n\nCorresponding Author: The Author of the Chapter who serves as a Signatory to this Agreement. The Corresponding Author acts on behalf of any other Co-Author.
\n\nCo-Author: All other Authors of the Chapter besides the Corresponding Author.
\n\nIntechOpen: IntechOpen Ltd., the Publisher of the Book.
\n\nBook: The publication as a collection of chapters compiled by IntechOpen including the Chapter. Chapter: The original literary work created by Corresponding Author and any Co-Author that is the subject of this Agreement.
\n\n2. CORRESPONDING AUTHOR'S GRANT OF RIGHTS
\n\n2.1 Subject to the following Article, the Corresponding Author grants and shall ensure that each Co-Author grants, to IntechOpen, during the full term of copyright and any extensions or renewals of that term the following:
\n\nThe aforementioned licenses shall survive the expiry or termination of this Agreement for any reason.
\n\n2.2 The Corresponding Author (on their own behalf and on behalf of any Co-Author) reserves the following rights to the Chapter but agrees not to exercise them in such a way as to adversely affect IntechOpen's ability to utilize the full benefit of this Publication Agreement: (i) reprographic rights worldwide, other than those which subsist in the typographical arrangement of the Chapter as published by IntechOpen; and (ii) public lending rights arising under the Public Lending Right Act 1979, as amended from time to time, and any similar rights arising in any part of the world.
\n\nThe Corresponding Author confirms that they (and any Co-Author) are and will remain a member of any applicable licensing and collecting society and any successor to that body responsible for administering royalties for the reprographic reproduction of copyright works.
\n\nSubject to the license granted above, copyright in the Chapter and all versions of it created during IntechOpen's editing process (including the published version) is retained by the Corresponding Author and any Co-Author.
\n\nSubject to the license granted above, the Corresponding Author and any Co-Author retains patent, trademark and other intellectual property rights to the Chapter.
\n\n2.3 All rights granted to IntechOpen in this Article are assignable, sublicensable or otherwise transferrable to third parties without the Corresponding Author's or any Co-Author’s specific approval.
\n\n2.4 The Corresponding Author (on their own behalf and on behalf of each Co-Author) will not assert any rights under the Copyright, Designs and Patents Act 1988 to object to derogatory treatment of the Chapter as a consequence of IntechOpen's changes to the Chapter arising from translation of it, corrections and edits for house style, removal of problematic material and other reasonable edits.
\n\n3. CORRESPONDING AUTHOR'S DUTIES
\n\n3.1 When distributing or re-publishing the Chapter, the Corresponding Author agrees to credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen. The Corresponding Author warrants that each Co-Author will also credit the Book in which the Chapter has been published as the source of first publication, as well as IntechOpen, when they are distributing or re-publishing the Chapter.
\n\n3.2 When submitting the Chapter, the Corresponding Author agrees to:
\n\nThe Corresponding Author will be held responsible for the payment of the Open Access Publishing Fees.
\n\nAll payments shall be due 30 days from the date of the issued invoice. The Corresponding Author or the payer on the Corresponding Author's and Co-Authors' behalf will bear all banking and similar charges incurred.
\n\n3.3 The Corresponding Author shall obtain in writing all consents necessary for the reproduction of any material in which a third-party right exists, including quotations, photographs and illustrations, in all editions of the Chapter worldwide for the full term of the above licenses, and shall provide to IntechOpen upon request the original copies of such consents for inspection (at IntechOpen's option) or photocopies of such consents.
\n\nThe Corresponding Author shall obtain written informed consent for publication from people who might recognize themselves or be identified by others (e.g. from case reports or photographs).
\n\n3.4 The Corresponding Author and any Co-Author shall respect confidentiality rights during and after the termination of this Agreement. The information contained in all correspondence and documents as part of the publishing activity between IntechOpen and the Corresponding Author and any Co-Author are confidential and are intended only for the recipient. The contents may not be disclosed publicly and are not intended for unauthorized use or distribution. Any use, disclosure, copying, or distribution is prohibited and may be unlawful.
\n\n4. CORRESPONDING AUTHOR'S WARRANTY
\n\n4.1 The Corresponding Author represents and warrants that the Chapter does not and will not breach any applicable law or the rights of any third party and, specifically, that the Chapter contains no matter that is defamatory or that infringes any literary or proprietary rights, intellectual property rights, or any rights of privacy. The Corresponding Author warrants and represents that: (i) the Chapter is the original work of themselves and any Co-Author and is not copied wholly or substantially from any other work or material or any other source; (ii) the Chapter has not been formally published in any other peer-reviewed journal or in a book or edited collection, and is not under consideration for any such publication; (iii) they themselves and any Co-Author are qualifying persons under section 154 of the Copyright, Designs and Patents Act 1988; (iv) they themselves and any Co-Author have not assigned and will not during the term of this Publication Agreement purport to assign any of the rights granted to IntechOpen under this Publication Agreement; and (v) the rights granted by this Publication Agreement are free from any security interest, option, mortgage, charge or lien.
\n\nThe Corresponding Author also warrants and represents that: (i) they have the full power to enter into this Publication Agreement on their own behalf and on behalf of each Co-Author; and (ii) they have the necessary rights and/or title in and to the Chapter to grant IntechOpen, on behalf of themselves and any Co-Author, the rights and licenses expressed to be granted in this Publication Agreement. If the Chapter was prepared jointly by the Corresponding Author and any Co-Author, the Corresponding Author warrants and represents that: (i) each Co-Author agrees to the submission, license and publication of the Chapter on the terms of this Publication Agreement; and (ii) they have the authority to enter into this Publication Agreement on behalf of and bind each Co-Author. The Corresponding Author shall: (i) ensure each Co-Author complies with all relevant provisions of this Publication Agreement, including those relating to confidentiality, performance and standards, as if a party to this Publication Agreement; and (ii) remain primarily liable for all acts and/or omissions of each such Co-Author.
\n\nThe Corresponding Author agrees to indemnify and hold IntechOpen harmless against all liabilities, costs, expenses, damages and losses and all reasonable legal costs and expenses suffered or incurred by IntechOpen arising out of or in connection with any breach of the aforementioned representations and warranties. This indemnity shall not cover IntechOpen to the extent that a claim under it results from IntechOpen's negligence or willful misconduct.
\n\n4.2 Nothing in this Publication Agreement shall have the effect of excluding or limiting any liability for death or personal injury caused by negligence or any other liability that cannot be excluded or limited by applicable law.
\n\n5. TERMINATION
\n\n5.1 IntechOpen has a right to terminate this Publication Agreement for quality, program, technical or other reasons with immediate effect, including without limitation (i) if the Corresponding Author or any Co-Author commits a material breach of this Publication Agreement; (ii) if the Corresponding Author or any Co-Author (being an individual) is the subject of a bankruptcy petition, application or order; or (iii) if the Corresponding Author or any Co-Author (being a company) commences negotiations with all or any class of its creditors with a view to rescheduling any of its debts, or makes a proposal for or enters into any compromise or arrangement with any of its creditors.
\n\nIn case of termination, IntechOpen will notify the Corresponding Author, in writing, of the decision.
\n\n6. INTECHOPEN’S DUTIES AND RIGHTS
\n\n6.1 Unless prevented from doing so by events outside its reasonable control, IntechOpen, in its discretion, agrees to publish the Chapter attributing it to the Corresponding Author and any Co-Author.
\n\n6.2 IntechOpen has the right to use the Corresponding Author’s and any Co-Author’s names and likeness in connection with scientific dissemination, retrieval, archiving, web hosting and promotion and marketing of the Chapter and has the right to contact the Corresponding Author and any Co-Author until the Chapter is publicly available on any platform owned and/or operated by IntechOpen.
\n\n6.3 IntechOpen is granted the authority to enforce the rights from this Publication Agreement, on behalf of the Corresponding Author and any Co-Author, against third parties (for example in cases of plagiarism or copyright infringements). In respect of any such infringement or suspected infringement of the copyright in the Chapter, IntechOpen shall have absolute discretion in addressing any such infringement which is likely to affect IntechOpen's rights under this Publication Agreement, including issuing and conducting proceedings against the suspected infringer.
\n\n7. MISCELLANEOUS
\n\n7.1 Further Assurance: The Corresponding Author shall and will ensure that any relevant third party (including any Co-Author) shall, execute and deliver whatever further documents or deeds and perform such acts as IntechOpen reasonably requires from time to time for the purpose of giving IntechOpen the full benefit of the provisions of this Publication Agreement.
\n\n7.2 Third Party Rights: A person who is not a party to this Publication Agreement may not enforce any of its provisions under the Contracts (Rights of Third Parties) Act 1999.
\n\n7.3 Entire Agreement: This Publication Agreement constitutes the entire agreement between the parties in relation to its subject matter. It replaces and extinguishes all prior agreements, draft agreements, arrangements, collateral warranties, collateral contracts, statements, assurances, representations and undertakings of any nature made by or on behalf of the parties, whether oral or written, in relation to that subject matter. Each party acknowledges that in entering into this Publication Agreement it has not relied upon any oral or written statements, collateral or other warranties, assurances, representations or undertakings which were made by or on behalf of the other party in relation to the subject matter of this Publication Agreement at any time before its signature (together "Pre-Contractual Statements"), other than those which are set out in this Publication Agreement. Each party hereby waives all rights and remedies which might otherwise be available to it in relation to such Pre-Contractual Statements. Nothing in this clause shall exclude or restrict the liability of either party arising out of its pre-contract fraudulent misrepresentation or fraudulent concealment.
\n\n7.4 Waiver: No failure or delay by a party to exercise any right or remedy provided under this Publication Agreement or by law shall constitute a waiver of that or any other right or remedy, nor shall it preclude or restrict the further exercise of that or any other right or remedy. No single or partial exercise of such right or remedy shall preclude or restrict the further exercise of that or any other right or remedy.
\n\n7.5 Variation: No variation of this Publication Agreement shall be effective unless it is in writing and signed by the parties (or their duly authorized representatives).
\n\n7.6 Severance: If any provision or part-provision of this Publication Agreement is or becomes invalid, illegal or unenforceable, it shall be deemed modified to the minimum extent necessary to make it valid, legal and enforceable. If such modification is not possible, the relevant provision or part-provision shall be deemed deleted.
\n\nAny modification to or deletion of a provision or part-provision under this clause shall not affect the validity and enforceability of the rest of this Publication Agreement.
\n\n7.7 No partnership: Nothing in this Publication Agreement is intended to, or shall be deemed to, establish or create any partnership or joint venture or the relationship of principal and agent or employer and employee between IntechOpen and the Corresponding Author or any Co-Author, nor authorize any party to make or enter into any commitments for or on behalf of any other party.
\n\n7.8 Governing law: This Publication Agreement and any dispute or claim (including non-contractual disputes or claims) arising out of or in connection with it or its subject matter or formation shall be governed by and construed in accordance with the law of England and Wales. The parties submit to the exclusive jurisdiction of the English courts to settle any dispute or claim arising out of or in connection with this Publication Agreement (including any non-contractual disputes or claims).
\n\nLast updated: 2020-11-27
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I am also a member of the team in charge for the supervision of Ph.D. students in the fields of development of silicon based planar waveguide sensor devices, study of inelastic electron tunnelling in planar tunnelling nanostructures for sensing applications and development of organotellurium(IV) compounds for semiconductor applications. I am a specialist in data analysis techniques and nanosurface structure. 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