List of instruments and materials tested.
\r\n\t
",isbn:"978-1-83968-924-6",printIsbn:"978-1-83968-923-9",pdfIsbn:"978-1-83968-925-3",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"ea4ec0d6ee01b88e264178886e3210ed",bookSignature:"Dr. Hiran Wimal Amarasekera",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/9500.jpg",keywords:"Bone Tumors, Oncology, Childhood Tumors, Cancer, Risk Factors, Modern Management, Benign Lesions, Tumor-Like Conditions, Immunology, Histochemistry, Cell Oncology, Tumor Markers",numberOfDownloads:389,numberOfWosCitations:0,numberOfCrossrefCitations:1,numberOfDimensionsCitations:1,numberOfTotalCitations:2,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"September 28th 2020",dateEndSecondStepPublish:"October 26th 2020",dateEndThirdStepPublish:"December 25th 2020",dateEndFourthStepPublish:"March 15th 2021",dateEndFifthStepPublish:"May 14th 2021",remainingDaysToSecondStep:"4 months",secondStepPassed:!0,currentStepOfPublishingProcess:4,editedByType:null,kuFlag:!1,biosketch:"Consultant Orthopaedic Surgeon from Sri Lanka currently working in University Hospitals of Coventry and Warwickshire, UK, trained at the National Hospital of Sri Lanka, at the Oldchurch Hospital in Essex UK and The Avenue Hospital Melbourne, Australia and University Hospitals of Coventry and Warwickshire, UK, obtained the FRCS from Royal College of Surgeons of Edinburgh, Scotland.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"67634",title:"Dr.",name:"Hiran",middleName:"Wimal",surname:"Amarasekera",slug:"hiran-amarasekera",fullName:"Hiran Amarasekera",profilePictureURL:"https://mts.intechopen.com/storage/users/67634/images/system/67634.jpg",biography:"Hiran Amarasekera is a Consultant Orthopaedic Surgeon from Sri Lanka currently working in University Hospitals of Coventry and Warwickshire, the UK as a hip preservation fellow. \r\nHis special interests include young adult hip and knee problems, sports injuries, Hip and knee arthroplasty, and complex arthroscopic procedures. \r\nHe completed the MBBS from Kasturba medical college Manipal, India and did his postgraduate in Trauma and Orthopaedics at the Post-graduate Institute of the Medicine University of Colombo obtained the MS. \r\nHe was initially trained at the National Hospital of Sri Lanka and then completed the further training at the Oldchurch Hospital in Essex UK and The Avenue Hospital Melbourne, Australia and University Hospitals of Coventry and Warwickshire, UK.\r\nHe obtained the FRCS from Royal College of Surgeons of Edinburgh in 2003 and was elected a fellow of Sri Lanka College of surgeons (FCSSL) 2012. \r\nHe has a keen interest in academia and research. 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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"}},{type:"book",id:"878",title:"Phytochemicals",subtitle:"A Global Perspective of Their Role in Nutrition and Health",isOpenForSubmission:!1,hash:"ec77671f63975ef2d16192897deb6835",slug:"phytochemicals-a-global-perspective-of-their-role-in-nutrition-and-health",bookSignature:"Venketeshwer Rao",coverURL:"https://cdn.intechopen.com/books/images_new/878.jpg",editedByType:"Edited by",editors:[{id:"82663",title:"Dr.",name:"Venketeshwer",surname:"Rao",slug:"venketeshwer-rao",fullName:"Venketeshwer Rao"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"57983",title:"Reactive Oxygen Species at High Altitude (Hypobaric Hypoxia) on the Cardiovascular System",doi:"10.5772/intechopen.72218",slug:"reactive-oxygen-species-at-high-altitude-hypobaric-hypoxia-on-the-cardiovascular-system",body:'\nIn the cardiovascular system, reactive oxygen species (ROSs) and reactive nitrogen species (RNSs) play important physiological roles in the control of endothelial functions, vascular tone, and cardiac functions, as well as a pathophysiological role in inflammation, hypertrophy, fibrosis, angiogenesis, cell proliferation, apoptosis, and migration. The regulation of this biological activity is the result of a balance between oxidants and the buffering action of antioxidants, such that an imbalance between ROS or RNS and antioxidants (called “oxidative stress”), wherein ROS or RNS is increased, contributes to cellular signaling that leads to endothelial dysfunction and cardiovascular remodeling. On the one hand, ROS triggers the activation of different cellular pathways by activating specific proteins (e.g., Akt1/2: serine/threonine protein kinase; PKC: protein kinase C; PDK: 3-phosphoinositide-dependent kinase; Erk1/2: extracellular signal-regulated kinase; JNK: c-Jun N-terminal kinase; PI3K: phosphatidylinositol-3-kinase; and JAK: Janus kinase) in different tissues. On the other hand, ROSs alter the activity of redox-sensitive transcription factors (i.e., AP-1: activator protein 1; NF-κB: nuclear factor-κB; HIF-1α: hypoxia-inducible factor-1α; and STAT: signal transducer and activator of transcription) to induce direct effects on enzymes, receptors, or ion channels and different cellular responses [1]. Oxidative stress is generated by external factors, such as a decrease in the partial pressure of oxygen (PO2) in hypobaric hypoxia due to high-altitude exposure. Over 100 million people live in hypoxic conditions worldwide [2, 3], the number of people exposed to hypoxic conditions is higher if we include people traveling to high altitudes for either leisure or work. Human beings, except Tibetans, are not naturally adapted or genetically equipped to live at high altitudes. Therefore, depending upon its degree and duration or the altitude, hypoxia generates several physiological or pathological effects on the human body [4].
\nThe main effects of exposure to hypobaric hypoxia are excessive erythrocytosis and high-altitude pulmonary hypertension (HAPH). Features of the latter include high pulmonary artery pressure, vascular remodeling of pulmonary arteries, right ventricle hypertrophy (RVH), and cardiac failure. In addition to the mechanical explanation usually considered for this phenomenon, new data suggest other, mechanical-independent mechanisms. We attempt to provide a comprehensive review of the principal factors, sources, and mechanism of action of ROS in the development of cardiovascular diseases under hypobaric hypoxia and/or similar stressors, with a specific focus on the cardiovascular system.
\nROSs are small molecules that derive from O2 and include the superoxide anion (O2•−), hydroxyl ion (OH), peroxyl (RO2), and alkoxy agents (RO•), as well as certain nonradicals that are either oxidizing or easily converted into radicals, such as hypochlorous acid (HOCl), ozone (O3), singlet oxygen (1O2), and hydrogen peroxide (H2O2). There are other types of molecules that are oxidizing agents but contain nitrogen; these radicals are called RNS. One example is peroxynitrite (NOO−), which is derived from nitric oxide (NO) when oxidized by O2•− [5]. These molecules are highly reactive due to the presence of an unpaired valence electron layer [6, 7], and through this electronic condition, ROSs avidly interact with a large number of molecules, including the plasma membrane and organic macromolecules such as proteins, lipids, carbohydrates, and nucleic acids, to achieve electron stability. Through such interactions, ROS can irreversibly alter or destroy the function of specific molecules in the cell; for this reason, ROSs are recognized as important players in many cellular signaling and physiological processes [8].
\nBased on the above, ROSs are considered harmful molecules that promote cellular aging in biological organisms. However, to date, at least one beneficial function has been described: ROSs produced by leukocytes, neutrophils, and macrophages were found to play a major role in the defense against host molecules or foreign agents [9]. Additionally, ROSs were recently proposed to participate not only in cellular damage and the destruction of pathogens but also in several reversible regulatory processes in all cells and tissues [9]. In other words, in a healthy organism, the cell normally produces low levels of ROS, which activates specific signaling pathways that contribute to normal responses to various stimuli [10]; however, the inability to adequately compensate for an increase in ROS by the antioxidant system of the tissue or organism (known as “oxidative stress”) can result in the development of several pathologies [11].
\nTherefore, under oxidative stress, high levels of ROS produce changes in the cell through the following mechanisms: (1) activating redox-sensitive protein kinases, such as JAKs, PKC, PI3K, and PDK; (2) activating mitogen-activated protein kinase (MAPK) family members, such as Akt, JNKs, Erk1/2, and p38, which are involved in angiogenesis and cell proliferation, differentiation, migration, growth, motility, survival, and apoptosis; (3) altering the activity of redox-sensitive transcription factors, such as AP-1, NF-κB, HIF-1α, and STAT; (4) inhibiting protein tyrosine phosphatase (PTP), which produces high levels of phosphorylated proteins; (5) producing an increase in the concentration of intracellular calcium [Ca2+]I; (6) producing direct effects on cellular structures, such as enzymes, receptors, and ion channels, or generating indirect effects on these structures through polyunsaturated fatty acids (PUFAs), which are highly susceptible to ROS, such that the oxidative breakdown of n-3 PUFAs may compromise membrane lipid matrix dynamics and, hence, the structure and function of membrane-associated proteins, such as enzymes, receptors, and transporters; and (7) stimulating the activity and expression of pro-inflammatory molecules and pro-oncogenes [1, 7, 8, 12, 13, 14].
\nFor these reasons, regulating ROS production modulates the activity of various intracellular molecules and various cell signaling pathways, thereby inducing specific acute and chronic changes in the phenotype and function of a cell (commonly referred to as “redox signaling”). Thus, with a specific focus on the cardiovascular system, ROSs play an important physiological role in the control of endothelial functions, vascular tone, and cardiac functions, as well as a pathophysiological role in inflammation, hypertrophy, fibrosis, angiogenesis, cell proliferation, apoptosis, and migration, whereby all these processes synergistically contribute to endothelial dysfunction and cardiovascular remodeling [7], as we demonstrate later in this chapter.
\nAs a result of decreased barometric pressure and oxygen partial pressure (PaO2), exposure to high altitudes generates an important effect on the cardiovascular system known as hypobaric hypoxia, where reduced uptake of oxygen leads to a decrease in O2 transported by the blood to all the cells in the organism [15, 16]. The important physiological effects in living beings are derived from acclimatization or adaptability to high altitude, and these effects fundamentally depend on the level of altitude and the duration of exposure [3].
\nAcute hypoxia (AH) occurs when a person (e.g., a tourist or alpinist) is exposed to high altitudes for short periods of time (days or hours), whereas chronic hypoxia (CH) occurs when a person is permanently exposed to hypoxic conditions (i.e., living at high altitude). A new and distinct form of exposure has recently been shown to be different from all types of hypobaric hypoxia described to date and is related to mining exploitation, thus termed “Chilean mining model of chronic intermittent exposure to high altitude” [17]. This type of hypobaric hypoxia involves working over 3000 m above sea level in shifts (days of work at high altitude and days of rest at sea level) and maintaining this condition for years. It has been estimated that over 200,000 people work under these conditions [18]. This biological condition is classified as chronic intermittent hypobaric hypoxia (CIHH).
\nThere are many effects of high altitude that could ultimately lead to pathologies. However, the principal effects are an increase in hematocrit levels by accumulative red cell production or excessive erythrocytosis (chronic mountain sickness) and the development of acute mountain sickness (AMS), which can begin as mild to severe (as cerebral edema or lung edema). Another effect is the development of hypoxic pulmonary vasoconstriction (HPV), which leads to HAPH, with a prevalence of up to 15% in individuals exposed to high altitude [4].
\nThe latter is of utmost interest, since its consequences are the clinical development of pulmonary hypertension and RVH or cor pulmonale [19, 20, 21]. Nevertheless, it must be noted that these effects appear to be less severe in CIHH exposure than in chronic exposure (CH) [16, 22].
\nPreviously, it was suggested that exposure to high altitude limits O2 supplementation in the organism in general and thus reduces the generation of free radicals (ROS), which are derived from this important gas [23]. However, this concept was later disputed with data suggesting that exposure to high altitude (>3000 m) leads to an increase in ROS production in many cell lines, thus generating an O2 supplementation paradox [24, 25, 26]. Finally, the high-altitude-induced increase in ROS products was confirmed by human studies, in which the concentrations of specific biomarkers of oxidative stress (plasmatic lipid peroxidation and iso-8-prostaglandin F-2α level in urine) were found to be increased after acute or chronic exposure to high altitude (4300 m) and without exercise [6]. Therefore, these findings suggest that exposure to hypoxia produces oxidative stress, thus causing all the aforementioned effects on both physiological and pathological cell signaling responses [9, 27].
\nStudies have evaluated the main sources of ROS in several cell lines under hypoxic conditions and concluded that the predominant source of ROS in the cardiovascular system is the enzymatic complex nicotinamide adenine dinucleotide phosphate (NADPH) oxidase (NOX), which prevails over other ROS-generating systems, such as mitochondria and xanthine oxidase [5, 28]. NADPH oxidases comprise a complex multicomponent family of transmembrane and cytosolic proteins that use NADPH as an electron donor to reduce molecular oxygen to the superoxide anion and hydrogen peroxide. The prototype NADPH oxidase was formerly known as gp91phox and was first described in leukocytes [1]. However, it is important to highlight that subsequent studies characterized seven members of the NOX family (NOX1 to 5 and dual oxidases 1 and 2) with diverse distributions among specific tissues and organs [10]; these NOX family members have since been described in nonphagocytic cells, including neurons, skeletal muscle, myocytes, hepatocytes, endothelial cells, hematopoietic cells, stem cells, and cardiomyocytes [28]. For example, previous studies found that stimulating rat cardiomyocytes with angiotensin II (Ang II) directly activated the NADPH oxidase complex, specifically the NOX2 isoform. This NOX2 complex can be activated in healthy organisms by several factors, including a G-protein receptor agonist (Ang II) and endothelin-1 (ET-1), vascular endothelial growth factor (VEGF), and mechanical shear stress from blood flow. However, the pathological activation of NOX2 (e.g., cytokines such as tumor necrosis factor-alpha) can result in the generation of much higher concentrations of ROS that appear to contribute to pathological states, including endothelial dysfunction, myocardial hypertrophy, fibrosis, heart failure, inflammation, atherosclerosis, coronary artery disease, stroke, and renal and pulmonary fibrosis [10].
\nStudies of the vascular system have shown that the predominant isoform of the NADPH complex is NOX4 [27, 29], and previous investigations revealed that NOX4 is involved in oxygen sensing, vasomotor control, angiogenesis, fibrosis, cell proliferation, differentiation, migration, apoptosis, and senescence. Elevated expression of NOX4 has been reported in a number of cardiovascular diseases, including atherosclerosis, pulmonary fibrosis, cardiac failure, and ischemic stroke [30].
\nNotably, previous studies have demonstrated that a single mutation in NOX4 disrupts O2•− production; these studies showed that although O2•− production was undetectable in NOX4-transfected cells, there was robust production of H2O2, in contrast to the mixture of O2•− and H2O2 production following transfection with NOX1-NOX3 and NOX5 [31].
\nThis effect of NOX4 was found due to the mutation of a highly conserved histidine residue in the E-loop of the NOX4 structure that promotes the rapid dismutation of O2•− before it leaves the enzyme [32], highlighting that higher concentrations of NOX4-produced H2O2 also elicit multiple effects. These effects are smooth muscle cell hypertrophy, activation of metalloproteases, and a low concentration of NOX4, which has been proposed as a cardiac protector [33]. Preliminary data from DNA microarray screens indicate that H2O2 causes a more than two-fold induction in the expression of nearly 100 genes, with a more than two-fold reduction in the expression of many more. Further, many transcription factors have been shown to be activated by H2O2. For example, as mentioned above, nuclear factor-κB (NF-κB) usually resides in the cytoplasm in association with an inhibitor protein (IκB) but is dissociated from IκB in the presence of H2O2. This process generates the nuclear translocation of NF-κB, and other transcription factors directly affected by exogenous H2O2, such as activator protein 1 (AP-1) (a complex composed of the jun and fos gene products) [1].
\nAs mentioned previously, HAPH is one of the principal pathologies involved in hypoxic exposure and arises from the narrowing of pulmonary arteries, which elevates pulmonary vascular resistance and, consequently, pulmonary artery pressure. HAPH is characterized by excessive proliferation and hypertrophy of pulmonary arterial medial smooth muscle and adventitial remodeling. ROS may serve as important regulators of pulmonary vascular remodeling, and some evidence supports a prominent role of NOX4 in the pathogenesis of HAPH [27]. For example, NOX4 is the major NADPH oxidase homolog expressed in human pulmonary artery smooth muscle cells, and its expression at both the mRNA and protein levels is significantly increased in lungs from patients with idiopathic pulmonary arterial hypertension (IPAH) compared to that in healthy lungs [34], which may suggest a strong correlation between NOX4 and the onset of HAPH.
\nIn addition, NOX4 expression was found to be increased in a CH-induced pulmonary artery hypertension (PAH) experimental mouse model. Therefore, NOX4 may also mediate hypoxia-induced growth of human pulmonary smooth muscle cells [35]. Indeed, this was corroborated in studies that silenced NOX4 expression by RNA interference; the results demonstrated a decrease in the growth of human pulmonary arterial smooth muscle cells and fibroblast proliferation [30].
\nFurthermore, if we focus on the HPV response to high altitude (hypobaric hypoxia), this effect is explained by smooth muscle cell contraction. Studies have shown that one of the main pathways involves an increase in intracellular calcium [Ca2+]I from the extracellular space and intracellular stores through voltage-activated potassium channels (KV) and nonspecific cation channels (NSCC) [36]. Nevertheless, further studies in lung cells found an increase in hypoxia-induced ROS that produced the activation of a calcium sensor (SMIT1) in the endoplasmic reticulum (ER), where this protein activates CRAC channels that contribute to the increase in intracellular Ca2+ [37].
\nIn the nitric oxide (NO) pathway, studies have reported that intermittent hypobaric hypoxia exposure reduces the bioavailability of NO in lung parenchyma and vasculature [27, 38]. NO is an endogenous vasodilator that activates cyclic GMP, which in turn activates protein kinase G (PKG) and ultimately causes reuptake of Ca2+ and the opening of calcium-activated potassium channels, leading to the relaxation of vascular smooth muscle cells (VSMCs). The decrease in NO bioavailability observed following exposure to intermittent hypobaric hypoxia may be due to the destruction of NO by hypobaric hypoxia-induced ROS, such as superoxide anion (O2−), which is produced by the enzymatic complex NAPH oxidase, specifically the NOX4 subunit [27, 29]. In agreement with these findings, studies silencing NOX4 and p22phox, another subunit involved in the activation of NADPH oxidase-NOX4, showed attenuation of ROS formation and proliferation in human and rat pulmonary artery smooth muscle cells (PASMCs) [39]. Therefore, all these ROS-activated cellular mechanisms may contribute to pulmonary artery remodeling, pulmonary hypertension, and finally, cardiac failure due to RVH.
\nRecently, other studies noted that NOX4 does not contribute to the development of hypoxia-induced pathologies, such as HPV or pulmonary hypertension. However, these studies found increases in superoxide anion (O2•−) levels in SMCs of NOX2- and NOX1-overexpressing mice and that NOX4 overexpression increased H2O2 levels. Therefore, NOX4 may be incapable of destroying NO; this contrasts with NOX1- and NOX2-derived O2•−, which destroys NO and contributes to the formation of ONOO−, thus leading to vascular dysfunction [40].
\nNOX4 has received considerable attention because it differs from NOX1 and NOX2 in several aspects: (1) NOX4 mRNA expression is higher than that of the other NOX homologs (>1000-fold higher copy number than NOX1 and NOX2) and different from NOX1 and NOX2, which are induced by Ang II in VSMCs. This is supported by studies in cultured cells showing the expression of NOX4 mRNA at copy numbers greater than 10- to 100-fold that of NOX2 and greater than 100-fold that of NOX1 [41]. Therefore, NOX4 is the most abundant NOX isoform in the vasculature. However, one must be mindful that mRNA levels may not accurately reflect protein expression levels of the various NOX isoforms [42]. (2) NOX4 expression increases over the course of differentiation and is required for the maintenance of the differentiated phenotype in cultured cells. (3) NOX4, unlike NOX1 and NOX2, is independent of cytosolic activator subunits and thus is potentially constitutively active. This is supported by overexpression studies conducted mostly in HEK293 cells, which have suggested that NOX4-dependent ROS production is controlled by the abundance of the enzyme. This aspect does not exclude the possibility that other interacting proteins, such as Poldip2 or protein disulfide isomerase, alter the activity of NOX4. Conversely, NOX4 predominantly releases H2O2, which cannot alter NO. NOX4 overexpression in the presence of NO does not lead to ONOO− formation, which strongly argues against significant O2•− formation by the enzyme [33].
\nTherefore, eNOS uncoupling is an important mechanism that leads to endothelial dysfunction. It is becoming progressively clear that the presence of low concentrations of H2O2 not only acts as a vasodilator by activating kinase G Iα3 but also may activate and induce eNOS by several mechanisms [33]. Thus, NOX4 might have an antagonistic function to NOX1 and NOX2, since it differs from these NADPH oxidases. NOX4 is a special NOX because it is highly constitutively active and is highly expressed in many cardiovascular cells. However, studies using both anti-NOX4 antibodies and in situ hybridization showed that NOX4 is primarily expressed in the middle layer of pulmonary blood vessels in both mice and humans [34].
\nNumerous studies have shown that NOX4 is robustly upregulated in response to transforming growth factor-beta (TGF-β) stimulation in various cell types, including aortic and pulmonary smooth muscle cells, pulmonary and cardiac fibroblasts, and endothelial and embryonic kidney cells [43]. However, tumor necrosis factor-alpha is less specific and can increase NOX1, NOX2, and NOX4 activity and/or the expression of these oxidases in various vascular cells. Other stimuli that induce NOX4 expression are ER stress, shear stress, hypoxia, and ischemia, as well as the activation of PKCα, NF-κB, HIF-1α, and Nrf2. These pathways are also likely dependent on the stimulus and cell type [44], and as mentioned above, Ang II has been shown to potently activate NOX1 and NOX2, but its effect on NOX4 expression is much less pronounced [30].
\nHIF-1α is a heterodimeric subunit of the transcription factor HIF-1, which regulates the transcription of genes involved in adaptive responses to hypoxia. Therefore, HIF-1 induces and promotes the expression of several genes containing hypoxia-responsive elements (HREs) in their regulatory region, such as proangiogenic factors (VEGF) or stromal-cell derived factor-1α (SDF-1α, CXCL12), vasoconstrictors (endothelin-1), and inflammation-associated genes (iNOS—inducible nitric oxide synthase and COX2—cyclooxygenase). Many of these factors promote angiogenesis and wound healing and are thus critical for the response to local hypoxia and injury. This HIF-1 system is also used to measure the systemic oxygen supply and to control the formation of red blood cells [12] through the glycoprotein erythropoietin (EPO). EPO has strong organ-protective effects in the heart, brain, and kidney, promotes re-endothelialization, and induces the mobilization of endothelial progenitor cells (EPCs), where ROS-NOX2 production is fundamental for EPO-induced mobilization of EPCs and vascular repair in hypoxic conditions [12].
\nHowever, the role of HIF-1α in the development of cardiac hypertrophy has been sparsely documented [45]. More interestingly, carvedilol, a β-receptor blocker, has emerged as a beneficial treatment for cardiac hypertrophy, as it inhibits the overexpression of HIF-1α during pressure overload in the rat heart [46]. Subsequent studies in cardiomyocytes under mild hypoxic conditions showed that HIF-1α controls the process of cardiac hypertrophy through the activation of transient receptor potential canonical 3 (TRPC3) and 6 (TRPC6), producing an increase in the levels of [Ca2+]i and calcineurin [47].
\nTRPC channels are nonselective cation channels that mediate Ca2+ influx into several cell types, including cardiac myocytes [48]. TRPC expression in cardiac hypertrophy has been studied by several laboratories, with somewhat variable results. For example, previous studies have shown that TRPC3 promotes cardiomyocyte hypertrophy in several animal models, including abdominal aortic banding (AAB) rats and spontaneous hypertensive heart failure rats [47]. Other studies have demonstrated that TRPC6 sequentially initiates a calcineurin signaling circuit during pathological cardiac hypertrophy. However, Ohba et al. [49] demonstrated that TRPC1, TRPC3, TRPC5, and TRPC6 are constitutively expressed, but only TRPC1 expression is significantly increased in hypertrophic hearts from AAB rats. However, these studies regarding the role of HIF-1α in cardiac hypertrophy were based on pathological situations, and their conclusions were controversial. Therefore, the potential role of HIF-1α in adaptive cardiac hypertrophy needs to be clarified.
\nFurther, previous studies showed that the HIF-1 pathway is involved in hypoxia-induced autophagy in cardiomyocytes and that HIF-1-induced autophagy may, therefore, help cardiomyocytes to overcome hypoxic injury and increase survival [50]. In other words, HIF-1α upregulation can increase autophagy and ameliorate the hypoxia-induced reduction in cell viability. Regarding survival and cardiac viability in hypoxic conditions, cardiac muscle cell survival plays a critical role in maintaining the correct function of the heart and, possibly, in cardiac embryogenic development. In contrast, adult cardiomyocytes are thought to be terminally differentiated and therefore have lost their proliferative capacity. One of the mechanisms that cardiomyocytes employ to protect themselves from deleterious stimuli is the release of survival cytokines capable of promoting cytoprotection in an autocrine/paracrine manner [51, 52]. One of these cytokines is cardiotrophin-1 (CT-1). CT-1 is a member of the interleukin-6 family with hypertrophic properties in neonatal and adult cardiomyocytes [53]. In adult cardiomyocytes, CT-1 exerts a protective function in response to death stimuli (apoptosis and necrosis), such as Ang II, H2O2, and ischemia-reperfusion. The cardioprotective properties of CT-1 under stress conditions suggest that it may be upregulated during cardiac diseases that are characterized by an environment of reduced oxygen availability, inflammation, and oxidative stress. Indeed, circulatory levels of CT-1 are elevated in pathological conditions associated with ischemia, including unstable angina pectoris, acute myocardial infarction, hypertensive heart disease, and heart failure. Importantly, studies have shown that hypoxia increased CT-1 in cardiac cells (in vitro and in vivo) through direct regulation of the CTF1 promoter by HIF-1α, and this CT-1 activation may protect cells from apoptosis, thus supporting a protective role of CT-1 as a survival factor for cardiomyocytes [52].
\nHAPH-induced RVH or end-stage cor pulmonale [19, 20, 21] is primarily explained as a compensatory effect of right ventricular afterload. However, numerous investigations have established new avenues for the development of cardiac hypertrophy that highlight oxidative stress as the main mediator [5, 54].
\nTo support the involvement of oxidative stress, a study evaluating both smooth muscle cells and endothelial cells in the development of pulmonary artery remodeling in CH was conducted. This study found that such arterial remodeling occurs via a mitochondrial factor, which requires the Rieske iron-sulfur protein (RISP), a mitochondrial complex III protein required for ROS generation. RISP depletion in endothelial cells and smooth muscle cells prevented CH-induced pulmonary hypertension, but it did not prevent RVH, suggesting that right ventricle remodeling in CH occurs through a mechanism independent of the increase in pulmonary artery pressure [55]. Thus, RVH could be directly produced by hypoxia-induced ROS, such that some in vitro experiments showed increased ROS levels in chicken cardiomyocytes and Hep3B cells cultured under AH [56].
\nTherefore, acute and chronic hypoxic exposure could generate oxidative stress [6] and may activate a large variety of protein kinases, such as MAPK, tyrosine kinases, and Rho kinases, and transcription factors (NF-κB, AP-1, and HIF-1α) that are derived from cellular hypertrophy [57] may also inactivate PTP. Both combined and separate effects induce an increase in the phosphorylation cascade or produce an increase in the concentration of intracellular calcium [Ca2+]I and stimulate the activity and expression of pro-inflammatory genes and proto-oncogenes [7].
\nRegarding cardiomyocytes, NOX2-mediated O2•− formation has been found to activate the protein kinase B or serine/threonine kinase (Akt) signaling pathways through PI3K, JNK, ERK1/2, and p38-MAPK. Thus, activation of these signaling pathways may play a central role in Ang II-stimulated cardiomyocyte hypertrophy [5, 58, 59]. Consequently, oxidative stress could play a fundamental role in cardiac hypertrophy, specifically RVH (possibly independent of the mechanical explanation) as a result of exposure to hypoxia. This is congruent with other studies demonstrated that NOX2 knockout attenuated Ang II and myocardial infarct-induced myocardial fibrosis and cardiomyocyte hypertrophy in mice. Hence, it could be surmised that NOX2 may play an important role in the development of cardiac hypertrophy in either hypoxic or other conditions, and this role may be independent of changes in blood pressure [60].
\nIn addition to NOX2, several studies have reported a relative abundance of NOX4 expression in human and mouse cardiac myocytes [61, 62] and in pulmonary arteries under hypoxia [27]. NOX4 is induced in experimental models of heart failure and in humans [61]. Recent studies using cardiac-specific NOX4 knockout mice revealed decreased levels of ROS and improved performance along with reduced hypertrophy, fibrosis, and apoptosis. Conversely, an experiment using a transgenic cardiac-specific NOX4-overexpressing mouse showed deleterious effects, such as promoting dysfunction, fibrosis, and apoptosis, in response to pressure overload [62]. While these results suggest that NOX4 is a major source of oxidative stress involved in the failing heart, there are reports showing opposite effects using a global NOX4 knockout and cardiac-specific NOX4 transgenic model [63]. These contradictory findings could be explained by differences in the methodology used to induce heart failure.
\nSupporting a more active role of NOX4, studies have revealed that NOX4 induces positive endothelial effects by producing H2O2, which in turn activates protein kinase G Iα by thiol oxidation and subsequent dimerization. Moreover, H2O2 also activates endothelial NOS (eNOS). Therefore, it is necessary to determine how NOX4 may mediate such contradictory roles [30].
\nAnother important source of ROS in cardiomyocytes is the mitochondrial complex (electron transport chain). Previous studies have found that mitochondria in cardiomyocytes increase their generation of ROS during hypoxia (1–5% O2), with the increased ROS generation originating from the proximal region of the electron transport chain, most likely complex III. These observations suggest that ROS generated by mitochondria may trigger p38 phosphorylation (activation) during hypoxia and thus highlight that the role of p38 phosphorylation in cardiomyocytes is highly dependent on PO2. Moreover, this ROS-induced p38 activation has been shown through another source independent of the electron transport chain, cobalt chloride [64]. However, hemoglobin (Hb), which is increased in hypobaric hypoxia exposure, depending on the type and duration of exposure, has intrinsic heme-oxidase activity that leads to the production of superoxide and thus contributes to oxidative stress. Therefore, the release of superoxide by Hb is favored in the T structure. Thus, sustained or excessive desaturation of Hb (T structure) may increase ROS production [65], and the phosphorylation of p38 MAPK during hypoxia may involve several ROS sources.
\nAlthough ROS generation is a normal physiological process, its counterbalance seems to be impaired under hypobaric hypoxia. The resulting imbalance leads to changes with potential pathological consequences for the cardiovascular system.
\nUnder hypobaric hypoxia, ROS levels are elevated, resulting in a subsequent unbalanced oxidative status. The principal sources of hypobaric hypoxia are NOX4 in the vascular system and NOX2 in cardiac tissue. The main effects of this oxidative increase include cellular damage, impaired NO pathway signaling, and the activation of calcium channels, transcription factors, pro-inflammatory molecules, and kinase proteins, all of which have deleterious effects on the cardiovascular system.
\nTherefore, this exaggerated or unbalanced ROS activity is closely related to the development of specific changes in the cardiovascular system under hypoxia, such as HPV, altitude pulmonary hypertension, pulmonary artery remodeling, and RVH. Notably, although most of the sources in this review described results from nonhypobaric hypoxia conditions, the information gathered reveals a broad view of the relationship between ROS and hypoxia. However, it is still necessary to further elucidate the undefined aspects of this association and the controversies concerning the poor characterization of hypobaric hypoxia.
\nThis work was funded by a grant from GORE-TARAPACA FIC BIP 30434827-0.
\nIn recent years, nanotechnology has been used to develop novel materials including nano and submicron scaled materials such as nanorods, nanofoams, nanotubes, nanofilms, and nanofibers. These materials find use in various industrial applications and are the topics of many contemporary academic research efforts. Of these materials, the polymer electrospun fibers have found broad uses for catalysis, drug delivery, semiconductors and filtration [1, 2, 3].
\nMany polymers have been electrospun into nonwoven fiber mats. The polymer materials can have intrinsic piezo, thermal, and mechanical properties. When the polymers are formed into fiber structures such as thin mats, the high porosities and high specific surface areas of the mats can enhance the mat structural properties compared to similar mats of microfibers. The material and structural properties of these mats are ideally suited for filter media for air filtration and face masks.
\nLess common in the literature are discussions of the fabrication of yarns from electrospun fibers. The fabrication of yarns requires a mechanical method to entangle and interlock the intrinsic fibers, often by twisting, to form a self-supporting assembly of the fibers of an overall cylindrical shaped structure that can be characterized by a structure diameter.
\nPrior to electrospinning, the submicron fibers were often synthesized by techniques such as drawing, templating, solution casting, and phase separating. Most of these techniques had shortcomings including deformation failures, inability to produce continuous fibers, inability to scale-up, low production rates, or significant by-product wastes. The electrospinning method overcomes some of these shortcomings, and because of its simplicity, is a highly popular synthesis method. Electrospinning is well-documented, established, and cost-effective, and is applied commercially. Figure 1 shows numbers of publications, by publication year, as determined from the Scifinder ™ data base for the past 25 years. The plot shows a steady rise in numbers of papers since about 2000 when Reneker [4] published a seminal paper on electrospinning. The data search was conducted in August 2020 hence the final year was incomplete.
\nNumber of publications on “electrospinning” versus year of publication.
Electrospinning has been used to spin fibers for a wide range of polymers. One of these polymers, polyvinylidene fluoride (PVDF), is well known for its electrical properties. PVDF exhibits five known crystalline phases- α, β, γ, δ and ε. Amongst them, the β-phase has the highest permanent dipole moment due to its trans, TTT, planar zig-zag configuration. The β-phase is considered most responsible for the piezoelectric response obtained from the PVDF materials. A goal of enhancing the beta-phase contents in PVDF materials is an ongoing research pursuit [5, 6].
\nElectrospun fibers have been used as electrets in several applications. Electrets have a surface charge which can be exploited in capturing charged particles. Nanofibers can be converted into electrets by various methods such as corona discharging, surface fluorination and nafion functionalization. Several research groups developed custom made bench-scale procedures to produce polarized fibers which involved simultaneous stretching, heating and electrical poling. Similarly, Lolla et al. [6, 7] produced polarized PVDF fiber mats and tested them for aerosol filtration. The polarized fibers were observed to have higher surface charges, better capture efficiencies and lower pressure drops compared to as-spun fibers. The study was limited by measurement of localized surface potential via a hand-held electrostatic field meter [6]. Table 1 lists several instruments reported in literature used to measure surface potential and charge. All of these instruments make localized measurements (do not measure properties over a large area of a mat) and may be impractical to use for production scale processes due to complexity and cost of operations. Measurements of the surface potential or electrical field are related to electrical charges but methods to calculate charges from the measurements are not always apparent.
\nResearcher | \nInstrument | \nMaterials tested | \nReference | \n
---|---|---|---|
Collins et al.\n | \nScanning Probe microscopy | \nVarious dielectric surfaces | \n[8] | \n
Du et al. | \nKelvin Probe force microscopy (open and closed loop techniques) | \nSingle and multi-layer graphene structures | \n[9] | \n
Takahashi and Yoshita | \nInversion algorithmic methods | \nDC basin-type insulator | \n[10] | \n
Fatihou et al. | \nElectrostatic voltmeter | \nElectrospun PVDF nanofibers | \n[11] | \n
Lolla et al. | \nElectrostatic field meter | \nPolarized electrospun nanofibers | \n[6] | \n
List of instruments and materials tested.
Gade et al. [12] fabricated a custom-made Faraday bucket and a procedure to calculate the charges of fiber mat samples. The Faraday bucket overcomes some limitations or challenges of using the methods listed in Table 1, namely: it is non-destructive, measures large sample sizes, is easy to scale-up, and has a tractable mathematical model to convert voltage to charge value. In this chapter, the Faraday bucket is used to measure and compare charges between electrospun fiber mats and electrospun (continuous twisted fiber) yarns. Layers of fibers mats and yarns were stacked together to explore whether the Faraday bucket was more sensitive to bulk (mass) charge or more sensitive to surface charge. The charges on polarized fibers and yarns are also compared.
\nMany publications discuss methods to charge fibers or to modify fibers surfaces (with coatings or additives such as carbon nanotubes) to enhance performances of fiber filter media. The subject matter is broad, and the numbers of publications are too numerous for a complete list. Table 2 lists a sample of some of the publications.
\nResearcher(s) | \nDescription | \nReference(s) | \n
---|---|---|
Fredrick Brown | \nFundamental physics of electrical and charge effects on filter performance | \n[13, 14] | \n
Choi et al. | \nAluminum coatings applied to micro and nanoscale fibers, modified surface charge to control filter performance | \n[15] | \n
Romay et al.\n Walsh et al.\n Wang et al.\n | \nQuasi-permanent charges on dielectric polymer fibers | \n[16, 17, 18, 19] | \n
Liu et al.\n Khalid et al.\n Jing et al.\n | \nFilters made of highly polar polymer fibers showing high binding affinity to fine particulate matter in aerosols | \n[20, 21, 22] | \n
Li et al.\n | \nFibrous filters hybridized with carbon nanotubes (CNT) exhibiting slip flow effects at the CNT surfaces | \n[23, 24] | \n
A sampling of literature on topics of fiber surface charge, fiber coatings, and additives.
The electrospinning processes typically produce nonwoven, randomly oriented, fiber mats. These fiber mats typically have low mechanical strength (compared to microfiber mats). The electrospinning processes have a low mass production rates per nozzle that limits commercial applications from an economic standpoint. Researchers have studied various approaches to increase the mass production by increasing the number of electrospinning jets in the process [25, 26]. To overcome some of the limitations, researchers have studied electrospun yarns to improve the alignment of fibers and to increase the mechanical strength. Production of highly twisted PVDF – HFP electrospun fiber yarns using a novel ring collector was reported by Shuakat et al. [27]. Afifi et al. [28] and Teo et al. [29] studied methods to continuously produce electrospun yarns. In this chapter the yarns were produced by twisting and drawing the fibers in flight and the twisted yarn were wound onto a spool, which differs from typical electrospinning equipment that collect the fiber mats on a solid grounded surface. The resulting yarns had lengths up to tens of meters long and exhibited mechanical properties different from the electrospun mats.
\nElectrospinning solutions were prepared by dissolving PVDF powder (Arkema Inc., Exton, PA, USA, Kynar® 761 grade resin with molecular weight of 500,000 g/gmol and density of 1.78 g/m3) in co-solvents N-N-Dimethylformamide (DMF) and acetone (Sigma Aldrich, St. Louis, MO, USA). These materials were used in making the solutions without further purification.
\nObservations while electrospinning the fiber mats and yarns showed different fiber diameters were obtained for the two processes likely due to variations in setup geometries and electric field strengths. By trial and error in varying solution concentrations, appropriate solution concentrations for the two processes were determined to produce fibers with diameters of 1200 nm for both processes. The comparisons of charges and properties discussed in the experiments below were obtained for fibers with these diameters.. Electrospinning solutions for producing fiber mats were prepared with 18%wt PVDF polymer by mixing the polymer with 50:50 wt.% blended DMF and Acetone solvents. The PVDF powder was added to mixture of solvents and heat-stirred for half an hour at 70 °C to attain a clear homogenous mixture. For production of fiber yarns, a 13 wt% PVDF polymer solution was prepared by mixing Acetone and N, N-Dimethylformamide (DMF) solvents at 1:1 ratio. This mixture was heated on a hot plate at 70 °C for 20 min to attain a clear homogenous mixture.
\nThe fiber mats were synthesized by using a typical single-needle electrospinning setup as shown in Figure 2. The polymer solutions were loaded into 5 ml plastic syringes and fed by syringe pump (NE-1000, New Era Pump Systems, Inc., Farmingdale, NY). The metallic needles were charged by high voltage power supplies (ES30P-5 W, Gamma High Voltage Research, Ormond Beach, FL) to generate potential differences between the collector and the needle. The fiber mats were collected on rotating cylindrical drum collectors covered with 30 cm × 30 cm sheets of grounded aluminum foil. The fiber mats were electrospun for varying times to create mats of basis weights of 10, 20, 30, 40 and 50 g/m2. In the experiments involving stacked layers of mats, all of the layers were formed of mats of 20 g/m2 basis weights. The electrospinning conditions are listed in Table 3.
\nSchematic of electrospinning set-up.
PVDF (wt.%) | \nDMF – Acetone mass ratio | \nTip to Collector Distance (cm) | \nApplied Potential (kV) | \nFlow Rate (ml/hr) | \nAvg. Fiber Diameter (nm) | \nStandard Deviation (nm) | \nDrum Rotation Rate (rpm) | \n
---|---|---|---|---|---|---|---|
18 | \n1:1 | \n20 | \n27 | \n5 | \n1139 | \n654 | \n30 | \n
Electrospinning conditions and fiber diameter data.
\nFigure 3 shows the experimental setup used to generate the electrospun yarn and is similar to setups reported in literature [28, 30]. The setup consisted of fiber spinning and yarn winding sections. In the fiber spinning section, a metallic conical-shaped funnel collector was connected to the motor and controller. The syringe pump and power supply were used to electrospin the polymer solution at a flowrate of 4 - 5 ml/hr. A potential difference of 10 – 20KV was applied between the metal needles and the collector with an 8 cm distance between the needles and the edge of the collector.
\nIllustration of fiber yarn setup.
Charged polymer jets launched from drops of polymer solution at the tips of the needles and followed the electric field gradient towards the wide neck of the conical-shaped collector. Once a substantial mat of fibers collected over the open end of the collector, the center of mat was hooked onto a wire and pulled to stretch the mat into the shape of an inverted cone.
\nThe metal collector was rotated by the motor to twist the fiber structure into a twisted continuous yarn. The yarn gradually increased in length and was stretched and attached to the take-up reel for collection onto a spool. The rotation speeds of the metal collector and the take-up reel were adjusted by trial and error to produced yarns of uniform twist and uniform outer diameter.
\nIn the case of electrospun mats, replicate samples were obtained at consistent basis weights by adjusting the time of fiber accumulation on the mats, so that the resulting fiber mat had uniform thickness and mass over the area of the sample. But in the case of fiber yarns a suitable length of sample was considered from each replicate run and compared for consistency by comparing the mass to length ratio of each sample. Results showed ±3% variation in mass/length for each of sample used in these experiments.
\nMats and yarns were polarized by the treatments described below. The treatments were not applied to stacked layers of mats in the layered mat experiments described later. Figure 4 (a) shows a photograph of the sample holder made of PTFE (Teflon®) for the main frame, brass bars for the clamps, and thin aluminum plates for the electrodes. The PTFE was chosen over other materials as it was easy to machine and had many desired properties such as low electrical conductivity, low dielectric constant, and relatively high melt temperature. Figure 4 (b) shows the sample holder inside of a Fischer Scientific iso-temp oven. The aluminum plates were 19 cm × 11 cm and 1 mm in thickness. One aluminum plate was grounded and the other was electrically charged to produce an electric field between the plates of 2.5 kV/cm. The distance between the electrodes was 6 cm. The fiber mat samples and yarn samples were placed in the holder to perform all polarization treatments including simultaneous heating, stretching and electrical poling.
\n(a) End view of fabricated sample holder showing the two planar electrodes used to apply the electric field for poling the sample. (b) Photo of sample holder inside of oven and high voltage power supply for charging the electrode above the oven.
Heat treatments were applied to change the sample temperature from room temperature to 150 °C with a temperature ramp-up rate of about 10C per min up to the soak temperature (150 C). The sample was held at the soak temperature for 5 minutes and then allowed to cool at a temperature ramp-down at rate of about 10C/min. The oven did not have ramp-rate control, so the ramp rates are estimates based on observed temperature readings.
\nThe electric field poling was applied at field strength of 2.5 kV/cm during the heating of the oven. The poling started at the same time as the oven and stopped when the oven was turned off at the end of the soak time.
\nUniaxial stretched mats and yarns were obtained by clamping the mats and yarns into the holder positioned parallel to and between the aluminum electrodes. The moveable clamp was moved to create a 10% stretch of the samples. The stretch time of the sample started when the sample was placed in the holder and stretched. The stretch time included time to place the holder into the oven, temperature ramp-up, temperature soak, temperature ramp-down, time to remove the holder, and ended when the sample was removed from the stretching mechanism in the holder, for a total of about 52 min. The as-spun and polarized samples were stored in the static shielding bags immediately after fabrication to avoid any dissipation of ions or charge.
\nThe morphology characteristics of the electrospun fiber mats and yarns were observed using a scanning electron microscopy (SEM, TM3000 and TM3030 Plus, and Hitachi, Japan). SEM images were analyzed by FibraQuant 1.3 software (nano Scaffold Technologies, LLC, Chapel Hill, NC) to measure the fiber diameter distributions. Figure 5 shows SEM images and fiber size distributions for PVDF fibers and yarns. Electric charges on the fiber mat were measured using a Faraday Bucket. A detailed description of the Faraday Bucket is given in reference [12]. The fiber mats were cut to the size needed for the measurement (4 cm by 4 cm) otherwise the measurements were non-destructive. Based on the electrostatic principles, as a sample lowered into the interior of the Faraday Bucket, the inner metallic “bucket” acquired an electric potential that was detected as a change in voltage relative to the surroundings (ground). By an appropriate circuit model of the Faraday bucket the measured potential was converted to charge.
\nSEM images of (a) fiber yarn and (b) fibers as seen on the surface of the fiber yarn with average fiber diameter of 1139 nm ± 654 nm, and average fiber yarn diameter of 900 μm ± 300 μm and c) fiber size distribution curve.
Fiber yarns produced using setup in Figure 3 were characterized as-spun and after polarization discussed in Section 2.4. The as-spun and polarized yarn samples were wrapped on a ‘U’ shaped copper wire and lowered into the Faraday bucket for measurement. The calculated charges were normalized with respect to mass of sample as discussed by Gade et al. [12]. The influence of U-shaped wire holding the yarn on the measured charge was found to be negligible when the wire without yarn was lowered into the Faraday bucket and produced zero measured voltage.
\nEvaluation of the effects on charge measurments of stacked of mats was conducted only with as-spun mats (not with polarized mats). The purpose of this was to assess whether the Faraday bucket measurements were more sensitive to surface area or to mass of the samples.
\n\nFigure 6a shows a photograph of a single 4 × 4 cm fiber mat. Figure 6b shows five as-spun mats stacked on top of each other. All mats were cut to size 4 cm × 4 cm and had a 1 × 1 cm tab at one edge. Figure 6c shows a bar chart of calculated charges per unit mass of individual and stacked layer samples. The measurements of the five individual samples are labeled as 1 to 5. The stacked samples are labeled A to D where A was formed by stacking the mats 1 + 2 (i.e., individual mats 1 and 2 stacked), B was three mats 1 + 2 + 3, C was four mats 1 + 2 + 3 + 4, and D was five mats 1 + 2 + 3 + 4 + 5.
\n(a) Photograph of example of a single fiber mat of size 4 × 4 cm with a 1 × 1 cm tab on one edge, (b) photograph of five mats stacked on top of each other. (c) Bar chart of charge/mass of various samples (1–5 = measured charge/mass of five individual samples) (a = charge of stacked mats 1 + 2, B = stacked mats 1 + 2 + 3, C = stacked mats 1 + 2 + 3 + 4, D = stacked mats 1 + 2 + 3 + 4 + 5). The error bars in (c) represent average of three charge measurements of same mats and error is one standard deviation.
All the single mats in Figure 6c had approximately the same measured charges of about 130 nC/g. All the mats had the same basis weight (20 g/m2), hence had the same masses.
\nIf the Faraday bucket detected charge in bulk (i.e. per mass) then stacking the mats should not show a difference in charge/mass. If the Faraday bucket detected charge based on charge on the external mat surface area, and the charges of the mats do not transfer between the mats, then we would expect the measured charge/mass to decrease as mass increased and the surface area remained the same.
\nThe results in Figure 6c shows the charge/mass linearly increased proportional to the number of mats in the stack. The charge/mass of stacked sample D (with five individual mats) was approximately double that of a single mat. Numerically this indicates that the measured charge per total mass increased over the single mat charge by about 25% for each additional mat in the stack. The increase in charge per mass indicates the bulk charge mechanism alone is unlikely. The increase in charge also strongly indicates that the measurement is not that of the charges on the external surfaces of the stacked mats assuming the charges do not migrate to the surface. Hence the mechanism is more complex. It is interesting to note that each subsequent mat added to the stack to linearly increased the measured charge by 25%. This gives the relationship
\nor
\nwhere \n
The plot in Figure 7 compares the charges of the (a) as-spun mats and yarns, and (b) polarized mats and yarns. For comparison purposes the samples of polarized and nonpolarized mats and yarns are compared on equal mass basis. The labels A, B, C, D and E indicate the masses of fibers in the yarns and mats corresponding to 0.0058, 0.0124, 0.0196, 0.0278 and 0.0376 g respectively. The data reported in Figure 7 are for electrospun mats of varying basis weights (not stacked layers of mats). For the given areas and masses of the mats the A, B, C, D and E mat samples correspond to 10, 20, 30, 40 and 50 g/m2 basis weights.
\nCharge/mass plot for mats and yarns (a) as-spun, (b) polarized. The respective masses of the samples were a = 0.0058 g, B = 0.0124 g, C = 0.0196 g, D = 0.0278 g, and E = 0.0376 g.
In Figure 7 the charges per mass of the mats were about 2 to 5 times the value for the yarns. The charge per mass of the as-spun and polarized mats increased as the mat mass increased with approximate slope of 17% (comparable to the 25% slope observed in the layered mats of Figure 6). Charges on the yarn samples did not vary as much with mass. Both the as-spun and polarized yarns tended to have a modest decrease in charge per mass as yarn mass increased. The difference in performance between the yarns and the mats is probably due to the way the yarn was folded to fit into the Faraday bucket. Increasing the mass of the yarn was obtained by increasing the length of the yarn hence the overall surface area per mass of the yarn was constant. But to fit the yarn into the Faraday bucket, the yarn was wound onto the U shaped metal wire which resulted in the first layers of the windings being covered by subsequent layers. Unlike the stacked fiber mats, the resulting charge/mass decreased with mass. This suggests that the measured charges per mass of the yarns were mostly proportional to the external area/mass ratio and may also give insight to the performance of the mats. This topic should be further explored in future work.
\n\nFigure 8 shows plots comparing the as-spun to polarized mats and yarns. The comparison of the mats in Figure 8a shows the polarized treatments only marginally increased the charges on the mats. This contrasts with the increases in charges reported in literature [6]. There were some differences between the treatments in this work compared to reference [6] such as the heat cycle in [6] was at a controlled ramp rate and the electrical polarization was maintained until the mat had completely cooled, while in this work the ramp rate was not controlled and the electrical polarization was for a shorter time period. It is possible, though not verified here, that the beta phase content of the electrospun fibers was near its maximum in the as-spun fibers and hence the polarization treatment did not have much room to increase the beta phase content. This is left for future investigation.
\nCharge/mass plot for as-spun and polarized samples (a) Mats, (b) yarns the respective masses of the samples were a = 0.0058 g, B = 0.0124 g, C = 0.0196 g, D = 0.0278 g, and E = 0.0376 g.
The comparison of yarns in Figure 8b similarly show a small increase in the charge in most of the cases. Overall, the charges on the yarns did not change significantly with mass. The polarized samples A, B, and E showed greater charge compared to the as-spun samples while C and D showed less charge. These variations may be within experimental error possibly due to the hand winding of the yarns onto the U-shaped wire holder.
\nPolymer PVDF was electrospun to form fiber mats and continuous twisted yarns. Samples of the mats and yarns were polarized by stretching, heating and poling. The as-spun and polarized mats and fibers were measured for their charge via a Faraday bucket. The results showed the mats had significantly higher charge per mass than the yarns at the same mass. The measured charge per unit mass of the mats increased as the mass of the mat increased. The measured charge per mass of the yarns slightly decreased as mass increased. The polarization treatments used in this work did not significantly increase the charge of the mats and yarns. Charge measurements of stacked layers of mats suggest that the charge measured by the Faraday bucket is a complicated combination of surface area and bulk mass. Changing the basis weights of fiber mats (instead of stacking layers) gave similar trends suggesting the same mechanisms may apply to both stacked and directly spun mats. The nearly constant measured charges of the yarns suggest that the charge per mass may be related to the surface area per mass of the yarns.
\nThis work was funded by Coalescence Filtration Fibers Consortium (CFNC): Parker Hannifin, Hollingsworth and Vose, and Donaldson. We acknowledge the assistance of technicians Steve Roberts and William Imes for fabrication and operation of the Faraday bucket.
\n.
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