Relevant bibliographies by topics / Elastin

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  2. Dissertations / Theses
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Academic literature on the topic 'Elastin'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 August 2024

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Journal articles on the topic "Elastin"

1

TASSLER, P. L., A. L. DELLON, and C. CANOUN. "Identification of Elastic Fibres in the Peripheral Nerve." Journal of Hand Surgery 19, no. 1 (February 1994): 48–54. http://dx.doi.org/10.1016/0266-7681(94)90049-3.

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Traditional histological staining techniques, as well as elastin-specific antibodies and electron microscopy, have been used to assess the distribution of elastin within the peripheral nerve. The location of the elastin identified by the VerHoeff-VanGiesen or Weigert stains has been shown to coincide with the unambiguous identilication of elastin by immunospecific stains and electron microscopy. Elastin is located in all three connective layers of the peripheral nerve. Thick elastic fibres, consisting of amorphous elastiu protein and microfibrils, are located consistently in the perineurium and, to a lesser extent, in the epineurium. The endoneurium contains small collections of elastic fibres widely distributed between the axons. Compared with collagen, the overall content of elastin, however, is small, suggesting that the visco-elastic properties of peripheral nerve may be due primarily to collagen.
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Schwartz, E., and R. Fleischmajer. "Association of elastin with oxytalan fibers of the dermis and with extracellular microfibrils of cultured skin fibroblasts." Journal of Histochemistry & Cytochemistry 34, no. 8 (August 1986): 1063–68. http://dx.doi.org/10.1177/34.8.3525665.

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The formation of a mature elastic fiber is thought to proceed by the deposition of elastin on pre-existing microfibrils (10-12 nm in diameter). Immunohistochemical evidence has suggested that in developing tissues such as aorta and ligamentum nuchae, small amounts of elastin are associated with microfibrils but are not detected at the light microscopic and ultrastructural levels. Dermal tissue contains a complex elastic fiber system consisting of three types of fibers--oxytalan, elaunin, and elastic--which are believed to differ in their relative contents of microfibrils and elastin. According to ultrastructural analysis, oxytalan fibers contain only microfibrils, elaunin fibers contain small quantities of amorphous elastin, and elastic fibers are predominantly elastin. Using indirect immunofluorescence techniques, we demonstrate in this study that nonamorphous elastin is associated with the oxytalan fibers. Frozen sections of normal skin were incubated with antibodies directed against human aortic alpha elastin and against microfibrillar proteins isolated from cultured calf aortic smooth muscle cells. The antibodies to the microfibrillar proteins and elastin reacted strongly with the oxytalan fibers of the upper dermis. Oxytalan fibers therefore are composed of both microfibrils and small amounts of elastin. Elastin was demonstrated extracellularly in human skin fibroblasts in vitro by indirect immunofluorescence. The extracellular association of nonamorphous elastin and microfibrils on similar fibrils was visualized by immunoelectron microscopy. Treatment of these cultures with sodium dodecyl sulfate/mercaptoethanol (SDS/ME) solubilized tropoelastin and other proteins that reacted with the antibodies to the microfibrillar proteins. It was concluded that the association of the microfibrils with nonamorphous elastin in intact dermis and cultured human skin fibroblasts may represent the initial step in elastogenesis.
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Trębacz, Hanna, and Angelika Barzycka. "Mechanical Properties and Functions of Elastin: An Overview." Biomolecules 13, no. 3 (March 22, 2023): 574. http://dx.doi.org/10.3390/biom13030574.

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Human tissues must be elastic, much like other materials that work under continuous loads without losing functionality. The elasticity of tissues is provided by elastin, a unique protein of the extracellular matrix (ECM) of mammals. Its function is to endow soft tissues with low stiffness, high and fully reversible extensibility, and efficient elastic–energy storage. Depending on the mechanical functions, the amount and distribution of elastin-rich elastic fibers vary between and within tissues and organs. The article presents a concise overview of the mechanical properties of elastin and its role in the elasticity of soft tissues. Both the occurrence of elastin and the relationship between its spatial arrangement and mechanical functions in a given tissue or organ are overviewed. As elastin in tissues occurs only in the form of elastic fibers, the current state of knowledge about their mechanical characteristics, as well as certain aspects of degradation of these fibers and their mechanical performance, is presented. The overview also outlines the latest understanding of the molecular basis of unique physical characteristics of elastin and, in particular, the origin of the driving force of elastic recoil after stretching.
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Fonck, E., G. Prod'hom, S. Roy, L. Augsburger, D. A. Rüfenacht, and N. Stergiopulos. "Effect of elastin degradation on carotid wall mechanics as assessed by a constituent-based biomechanical model." American Journal of Physiology-Heart and Circulatory Physiology 292, no. 6 (June 2007): H2754—H2763. http://dx.doi.org/10.1152/ajpheart.01108.2006.

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Arteries display a nonlinear anisotropic behavior dictated by the elastic properties and structural arrangement of its main constituents, elastin, collagen, and vascular smooth muscle. Elastin provides for structural integrity and for the compliance of the vessel at low pressure, whereas collagen gives the tensile resistance required at high pressures. Based on the model of Zulliger et al. (Zulliger MA, Rachev A, Stergiopulos N. Am J Physiol Heart Circ Physiol 287: H1335–H1343, 2004), which considers the contributions of elastin, collagen, and vascular smooth muscle cells (VSM) in an explicit form, we assessed the effects of enzymatic degradation of elastin on biomechanical properties of rabbit carotids. Pressure-diameter curves were obtained for controls and after elastin degradation, from which elastic and structural properties were derived. Data were fitted into the model of Zulliger et al. to assess elastic constants of elastin and collagen as well as the characteristics of the collagen engagement profile. The arterial segments were also prepared for histology to visualize and quantify elastin and collagen. Elastase treatment leads to a diameter enlargement, suggesting the existence of significant compressive prestresses within the wall. The elastic modulus was more ductile in treated arteries at low circumferential stretches and significantly greater at elevated circumferential stretches. Abrupt collagen fiber recruitment in elastase-treated arteries leads to a much stiffer vessel at high extensions. This change in collagen engagement properties results from structural alterations provoked by the degradation of elastin, suggesting a clear interaction between elastin and collagen, often neglected in previous constituent-based models of the arterial wall.
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Boëté, Quentin, Ming Lo, Kiao-Ling Liu, Guillaume Vial, Emeline Lemarié, Maxime Rougelot, Iris Steuckardt, et al. "Physiological Impact of a Synthetic Elastic Protein in Arterial Diseases Related to Alterations of Elastic Fibers: Effect on the Aorta of Elastin-Haploinsufficient Male and Female Mice." International Journal of Molecular Sciences 23, no. 21 (November 3, 2022): 13464. http://dx.doi.org/10.3390/ijms232113464.

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Elastic fibers, made of elastin (90%) and fibrillin-rich microfibrils (10%), are the key extracellular components, which endow the arteries with elasticity. The alteration of elastic fibers leads to cardiovascular dysfunctions, as observed in elastin haploinsufficiency in mice (Eln+/-) or humans (supravalvular aortic stenosis or Williams–Beuren syndrome). In Eln+/+ and Eln+/- mice, we evaluated (arteriography, histology, qPCR, Western blots and cell cultures) the beneficial impact of treatment with a synthetic elastic protein (SEP), mimicking several domains of tropoelastin, the precursor of elastin, including hydrophobic elasticity-related domains and binding sites for elastin receptors. In the aorta or cultured aortic smooth muscle cells from these animals, SEP treatment induced a synthesis of elastin and fibrillin-1, a thickening of the aortic elastic lamellae, a decrease in wall stiffness and/or a strong trend toward a reduction in the elastic lamella disruptions in Eln+/- mice. SEP also modified collagen conformation and transcript expressions, enhanced the aorta constrictive response to phenylephrine in several animal groups, and, in female Eln+/- mice, it restored the normal vasodilatory response to acetylcholine. SEP should now be considered as a biomimetic molecule with an interesting potential for future treatments of elastin-deficient patients with altered arterial structure/function.
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Hoareau, Marie, Naïma El Kholti, Romain Debret, and Elise Lambert. "Characterization of the Zebrafish Elastin a (elnasa12235) Mutant: A New Model of Elastinopathy Leading to Heart Valve Defects." Cells 12, no. 10 (May 21, 2023): 1436. http://dx.doi.org/10.3390/cells12101436.

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Elastic fibers are extracellular macromolecules that provide resilience and elastic recoil to elastic tissues and organs in vertebrates. They are composed of an elastin core surrounded by a mantle of fibrillin-rich microfibrils and are essentially produced during a relatively short period around birth in mammals. Thus, elastic fibers have to resist many physical, chemical, and enzymatic constraints occurring throughout their lives, and their high stability can be attributed to the elastin protein. Various pathologies, called elastinopathies, are linked to an elastin deficiency, such as non-syndromic supravalvular aortic stenosis (SVAS), Williams–Beuren syndrome (WBS), and autosomal dominant cutis laxa (ADCL). To understand these diseases, as well as the aging process related to elastic fiber degradation, and to test potential therapeutic molecules in order to compensate for elastin impairments, different animal models have been proposed. Considering the many advantages of using zebrafish, we here characterize a zebrafish mutant for the elastin a paralog (elnasa12235) with a specific focus on the cardiovascular system and highlight premature heart valve defects at the adult stage.
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Nishizaki, Tomoyuki. "PKCε Increases Extracellular Elastin and Fibulin-5/DANCE in Dermal Fibroblasts." Cellular Physiology and Biochemistry 46, no. 1 (2018): 291–302. http://dx.doi.org/10.1159/000488430.

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Background/Aims: In the earlier study, the selective PKCε activator DCP-LA increased elastic fibres in the dermis of HR-1 hairless mice. As a process of elastic fibre formation, tropoelastin, an elastin monomer, is secreted into the extracellular space. Secreted tropoelastin is delivered to the microfibrils by fibulin-5/developmental arteries and neural crest epidermal growth factor-like (DANCE) and undergoes self-association. Then, tropoelastin assembles around the microfibrils, growing into elastin and elastic fibres by lysyl oxidase (LOX)- or LOX-like (LOXL)-mediated cross-linking. The present study was conducted to understand the mechanism underlying DCP-LA-induced increase in elastin/elastic fibre. Methods: Western blotting, immunocytochemistory, and real-time reverse transcription-polymerase chain reaction (RT-PCR) were carried out in cultured human dermal fibroblasts. PKCε, mammalian target of rapamycin complex (mTOR), and p70 S6 kinase (S6K) were knocked-down by transfecting each siRNA. Results: DCP-LA increased elastin and fibulin-5/DANCE in a treatment time (6-24 h)- and a bell-shaped concentration (1 nM-1 µM)-dependent manner in the culture medium of human dermal fibroblasts. DCP-LA markedly increased elastic fibres in the extracellular space of cultured fibroblasts. DCP-LA-induced increase in extracellular elastin and fibulin-5/DANCE was abolished by a PKC inhibitor or knocking-down PKCε. DCP-LA did not affect expression of mRNAs for tropoelastin and fiblin-5/DANCE in cultured fibroblasts. DCP-LA-induced increase in extracellular elastin and fibulin-5/DANCE was not inhibited by the protein synthesis inhibitor cycloheximide or by knocking-down mTOR and S6K. DCP-LA never increased extracellular elastin in the presence of elastase, that breaks down elastin. An inhibitor of matrix metalloproteinase 9, that degrades multiple extracellular matrix components including elastin, had no effect on the basal levels and the DCP-LA-induced increase levels of extracellular elastin. Conclusion: The results of the present study indicate that PKCε, activated by DCP-LA, increases elastin and fibulin-5/DANCE in the extracellular space of cultured fibroblasts by the mechanism independent of transcriptional and translational modulation or inhibition of elastolysis.
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Nygaard, Rie Harboe, Scott Maynard, Peter Schjerling, Michael Kjaer, Klaus Qvortrup, Vilhelm A. Bohr, Lene J. Rasmussen, Gregor B. E. Jemec, and Michael Heidenheim. "Acquired Localized Cutis Laxa due to Increased Elastin Turnover." Case Reports in Dermatology 8, no. 1 (February 13, 2016): 42–51. http://dx.doi.org/10.1159/000443696.

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Cutis laxa is a rare disease characterized by abnormal skin wrinkling and laxity, due to decreased elastin synthesis or structural extracellular matrix defects. We have explored elastin metabolism in a case of adult onset cutis laxa localized to the upper body of a woman. For this purpose, we obtained skin biopsies from affected and unaffected skin areas of the patient and analyzed these with microscopy, polymerase chain reaction, western blotting and cell culture experiments. Skin from the affected area lacked elastin fibers in electron microscopy but had higher mRNA expression of elastin and total RNA. Levels of an apparent tropoelastin degradation product were higher in the affected area. Fibroblast cultures from the affected area were able to produce elastin and showed higher proliferation and survival after oxidative and UVB stress compared to fibroblasts from the unaffected area. In conclusion, we report a case of acquired localized cutis laxa with a lack of elastic fibers in the skin of the patient's upper body. The lack of elastic fibers in the affected skin was combined with increased mRNA expression and protein levels of elastin. These findings indicate that elastin synthesis was increased but did not lead to deposited elastic fibers in the tissue.
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Sambani, Kyriaki, Stylianos Vasileios Kontomaris, and Dido Yova. "Atomic Force Microscopy Imaging of Elastin Nanofibers Self-Assembly." Materials 16, no. 12 (June 11, 2023): 4313. http://dx.doi.org/10.3390/ma16124313.

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Elastin is an extracellular matrix protein, providing elasticity to the organs, such as skin, blood vessels, lungs and elastic ligaments, presenting self-assembling ability to form elastic fibers. The elastin protein, as a component of elastin fibers, is one of the major proteins found in connective tissue and is responsible for the elasticity of tissues. It provides resilience to the human body, assembled as a continuous mesh of fibers that require to be deformed repetitively and reversibly. Thus, it is of great importance to investigate the development of the nanostructural surface of elastin-based biomaterials. The purpose of this research was to image the self-assembling process of elastin fiber structure under different experimental parameters such as suspension medium, elastin concentration, temperature of stock suspension and time interval after the preparation of the stock suspension. atomic force microscopy (AFM) was applied in order to investigate how different experimental parameters affected fiber development and morphology. The results demonstrated that through altering a number of experimental parameters, it was possible to affect the self-assembly procedure of elastin fibers from nanofibers and the formation of elastin nanostructured mesh consisting of naturally occurring fibers. Further clarification of the contribution of different parameters on fibril formation will enable the design and control of elastin-based nanobiomaterials with predetermined characteristics.
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Powell, J. T. "Evidence against lung galaptin being important to the synthesis or organization of the elastic fibril." Biochemical Journal 252, no. 2 (June 1, 1988): 447–52. http://dx.doi.org/10.1042/bj2520447.

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Previously it has been suggested that galaptin, an endogenous beta-galactoside-binding lectin, may function in the organization of lung elastic fibres. Galaptin was not present in preparations of rat or porcine lung elastic fibrils, neither did it bind to any of the fibril-associated proteins when these were separated by SDS/polyacrylamide-gel electrophoresis. Elastin and galaptin synthesis and secretion were investigated in lung fibroblast cultures and in anatomically preserved slices from developing rat lung. In both systems the synthesis and secretion of elastin was unmodified by the presence of beta-galactosides or antigalaptin in the culture medium. The synthesis of galaptin was unmodified by the presence of anti-elastin or beta-aminoproprionitrile in the culture medium. Cultured fibroblasts secreted elastin but only trivial amounts of galaptin. When cultures were treated with iodoacetamide (10(-5)M) galaptin synthesis was maintained but elastin synthesis ceased. These results argue against galaptin having an important role in the synthesis, secretion or organization of the elastic fibril.
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Dissertations / Theses on the topic "Elastin"

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Getie, Kebtie Melkamu. "Mass spectrometric characterization of elastin peptides and the effect of solar radiation on elastin." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=980155932.

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Bhanji, Tania. "Elastin in zebrafish and mice." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=111938.

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The extracellular matrix is a vital component of the cardiovascular system, in that, it not only provides structural support but also plays a critical role in the maintenance of cellular stability. One of the major components of the vascular matrix is elastin, which confers vessels with the specialized property of stretch and recoil. Elastin deficiency has been implicated in many vascular diseases and determined experimentally to be a negative regulator of smooth muscle cell proliferation. In zebrafish, two elastin genes have been identified, which are actively expressed during development. Based on this finding, protein production and spatial localization for the two elastin proteins was studied by immunohistochemistry with specific antibodies. Results revealed a global distribution for elastin 1 in the ventral aorta and swim bladder, whereas elastin 2 was preferentially localized to the bulbus arteriosus indicating a possible specialized function of elastin 2 in this structure. This observation, and the unique physiological property of this structure, suggests a possible reason for the preservation of both elastin genes during evolution.
In the second part of this study, elastin-null mice were studied to uncover the impact of the loss of elastin on the expression of other elastic fiber-associated proteins. The expression of fibrillin-1, the major component of microfibrils, was not altered in the absence of elastin, implying that elastin is not necessary for the formation of microfibrils. On the other hand, both fibulin-2 and -5 were upregulated in the absence of elastin, suggesting that expression of these genes are controlled by elastin. Overall, this study highlights the importance of elastin in evolution, as well as its potential role in the regulation of expression of other matrix molecules.
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Ferron, Florence Joelle. "The implications of fibulin-5 on elastin assembly and its role in the elastic fiber /." Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=101846.

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The extracellular matrix (ECM) is the material found surrounding the cells in a tissue. One component of the ECM is the elastic fiber, which confers the property of elasticity to its environment. Organs such as the lung, skin and major blood vessels have an abundance of elastic fibers so that they are able to expand and recoil. Elastic fibers are composed of two main components; elastin and microfibrils. Microfibrils are composed primarily of fibrillin-1 and provide a scaffold unto which tropoelastin monomers assemble. Elastic fibers interact with many other proteins in the ECM, one of which is fibulin-5. Based on the severe elastic fiber defects observed in the fibulin-5 null mouse, it was established that fibulin-5 plays an essential role in elastic fiber development. This role may be in the deposition of tropoelastin onto microfibrils and/or in stabilizing the elastic fibers in the extracellular matrix. In the present study, the relationship between fibulin-5 and the elastic fiber was investigated through a number of in vivo and in vitro experiments. To test the hypothesis that fibulin-5 requires the presence of elastin to assemble in the ECM, full-length recombinant fibulin-5 (rF5) was purified from transfected cells and used to make a fibulin-5 antibody. Solid-phase binding assays using rF5 showed that fibulin-5 binds tropoelastin at two sites; the initial portion of the C-terminus and the first calcium-binding epidermal growth factor-like domain at the N-terminus. Immunofluorescence staining of elastin null mouse embryonic fibroblast cultures revealed that fibulin-5 does not require elastin to be present in the ECM in order to assemble. Subsequently, solid-phase binding assays showed that fibulin-5 can bind to the N-terminus of fibrillin-1. To determine if fibulin-5 could exist independent of elastin and/or fibrillin-1 in vivo, an immunohistochemical analysis was conducted on heart, liver, lung, colon, spleen, testis and kidney. All three proteins were co-localized in all organs except in the kidney, where fibrillin-1 was found to independently stain the capillary tufts of the renal corpuscles and renal tubules. Thus, fibulin-5 may be co-regulated with elastin and is not present on elastin-independent microfibrils. Additionally, novel locations of elastic fibers were uncovered in the heart, liver, colon, spleen and testis. Overall, this study provides important insights as to the role of fibulin-5 in elastic fiber structure and assembly and also reveals the complexity in understanding the pathogenesis of diseases involving elastic fiber proteins.
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Moore, Glynis Wilson. "Human aortic elastin : an examination of elastic lamellae fragmentation associated with ageing and atherosclerosis." Thesis, Queen's University Belfast, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356892.

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Dillon, Tara J. "Elastin metabolisim in human lung disease /." Title page, contents and abstract only, 1994. http://web4.library.adelaide.edu.au/theses/09PH/09phd5793.pdf.

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Smith, Kinley. "The distribution and function of elastin and elastic fibres in the canine cruciate ligament complex." Thesis, University of Liverpool, 2010. http://livrepository.liverpool.ac.uk/1437/.

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Anterior cruciate ligament rupture (ACL) is a major source of morbidity in the dog, leading to severe osteoarthritis of the knee joint and marked lameness. Following rupture, the ACL will not heal and in the dog, ACL rupture is thought to be the end stage of degenerative ligament disease (non-contact ACL injury). The extracellular matrix (ECM) of CLs has been extensively studied but little is known of the role of elastic fibres in the physiology of the ECM, the mechanics of CL function and in CL degeneration. Elastic fibres include polymers of fibrillins (microfibrils), bundles of microfibrils (oxytalan fibres) and elastin fibres (bundles of microfibrils with an elastin core). The hypothesis of this thesis is that elastin has a mechanical and a biological role in the canine cruciate ligament complex. It is further hypothesised that the distribution and function of elastic fibres will vary between three breeds of dog with differing risk of ACL rupture are: the greyhound with a low risk, the beagle with a low-to-moderate risk and the Labrador retriever with a high risk. The distribution of elastic fibres, fibrillins and cells was investigated throughout the CL complex using a combination of histochemical staining and immunofluorescence. CL microanatomy was studied using Nomarski differential interference microscopy. Elastin was measured biochemically and compared to histologic assessment of tissue architecture, elastic fibre staining and other biochemical parameters. The biological effect of elastin degradation products (EDPs) was assessed in an in vitro ACL cell culture model. A low risk dog breed to ACL rupture (greyhound) was used in all investigations and comparisons were made with other breeds with regard to cellular and elastic fibre anatomy. Differences in cell morphology between breeds with differing risk of ACL rupture may reflect fundamental differences in CL physiology possibly through altered cell-to-cell communication. Cellular and matrix changes, considered degenerative, were seen throughout the CL complex and may reflect adaptation rather than degeneration in certain dog breeds such as the greyhound. Elastin content ranged from 5.9 to 19.4% of ligament dry weight. This was a far greater proportion of canine CLs than previously. Elastin fibres may have a mechanical role in bundle reorganization following ligament deformation. The distribution of fibrillins 1 and 2 was different from the pattern previously reported in tendon and may represent a fundamental difference between ligament and tendon. In the greyhound CL there was a significant proportional increase in oxytalan fibre staining with advancing CL degeneration. This response was seen also in the Labrador retriever and the beagle but the increase in oxytalan fibre staining was less marked with advancing degeneration. Therefore production of oxytalan fibres may reflect a healing response in damaged CL tissue in breeds at a low risk of ligament rupture. Fragments of elastin containing the VGVAPG motif affect canine ACL cells in vitro resulting in increased transcription of fibrillin 2 mRNA. Additionally, there was synergism with TGF-β1 resulting in upregulation of the elastin laminin receptor 1, through which EDPs are transduced. EDPs may thus have a role in response to injury in the CL.
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Chevallier, Stéphane. "Elastokines et Lactosylcéramide : cardioprotection et vieillissement." Thesis, Reims, 2011. http://www.theses.fr/2011REIMM203/document.

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La maladie cardiovasculaire la plus courante dans les pays industrialisés est la maladie coronarienne responsable d’une ischémie du tissu cardiaque pouvant conduire à l’infarctus du myocarde. Bien que les améliorations de la prise en charge aient considérablement réduit les délais de la reperfusion (seul remède à l’ischémie), l’ischémie/reperfusion (I/R) entraîne des dommages cellulaires et tissulaires ainsi qu’une diminution des capacités fonctionnelles du coeur. Il existe néanmoins des systèmes de cardioprotection endogènes (comme le préconditionnement (préC) ou le postconditionnement (postC)) que l’on peut activer via l’administration de substances pharmacologiques. L’élastine, une protéine fibreuse de la matrice extracellulaire, est responsable de l’élasticité de certains de nos tissus (poumons, peau, <). Des peptides issus de la dégradation de l’élastine (PE) exercent un effet cardioprotecteur envers l’I/R en activant la voie de survie cellulaire RISK. Dans des fibroblastes dermiques, la transduction du signal induit par les peptides d’élastine est médiée de façon précoce par un second messager : le lactosylcéramide (LacCer). Cette étude constitue une première approche des effets du LacCer dans la cardioprotection envers l’I/R. Nous avons montré que le LacCer est un médiateur précoce du signal cardioprotecteur induit par les PE et qu’il protège le coeur des dommages liés à l’I/R dans un modèle de coeur isolé et perfusé en postC. Lors du vieillissement, de nombreuses modifications physiologiques sont à l’origine d’une perte d’efficacité des mécanismes de cardioprotection. Dans ce travail, nous avons également étudié les effets cardioprotecteurs des PE, du LacCer et de l’inhibition de p38MAPK (une protéine probablement impliquée dans la perte des mécanismes cardioprotecteurs liée au vieillissement) envers les dommages liés à l’I/R chez les rats âgés. Nous avons montré que les PE exercent un effet cardioprotecteur en pré+postC contre l’I/R au niveau de la survie cellulaire et au niveau de la récupération des capacités contractiles cardiaques. Le LacCer n’exerce un effet protecteur qu’au niveau de la survie cellulaire et l’inhibition de p38MAPK entraine une meilleure récupération des capacités contractiles sans améliorer la survie cellulaire
In developed countries the most common cardiovascular disease is coronary heart disease that is responsible for myocardial ischemia and can lead to myocardial infarction. Reperfusion is the only cure for ischemia. Care improvement has dramatically reduced reperfusion delay but ischemia/reperfusion (I/R) causes a lot of cellular and tissular damages and a reduction of cardiac contractile abilities. Nevertheless cardioprotective pathways (like preconditionning (preC) and postconditionning (postC) can be pharmacologically triggered to reduce I/R injury. Elastin is a fibrous protein from extracellular matrix and is responsible for tissues elasticity in lungs, skin, < Peptides derived from elastin fragmentation (EP) exhibit cardioprotective function against I/R by triggering the RISK pathway, a cell survival pathway. In dermic fibroblasts, elastin peptides pathway is mediated by an early messenger : lactosylcéramide (LacCer). In this work we have studied cardioprotective function of LacCer against I/R injury. We show that LacCer is an early messenger of EP cardioprotective pathway and that it also exhibits a cardioprotective function against I/R in an postconditionning isolated rat heart model. During ageing dramatic physiological modifications are responsible for a loss of efficiency of cardioprotection pathways. In this work we have also studied the potential cardioprotective function of EP, LacCer and p38MAPK inhibition (a protein presumably involved in loss of efficiency of cardioprotection pathways during ageing) against I/R injury in aged rats. We have shown that EP exhibit a cardioprotective function against I/R injury in aged rats as well as young rats in a pre+postconditionning protocol. EP enhance contractile abilities recovering and cell survival. LacCer improves only cell survival and p38MAPK inhibition improves only contractile abilities recovering
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Chalmers, Gavin William Geddes. "A comparative study of the swelling and mechanical properties of vertebrate elastins." Thesis, University of British Columbia, 1988. http://hdl.handle.net/2429/27856.

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The swelling-temperature compensation hypothesis as proposed by Gosline and French (1979) is examined by investigating the physical and mechanical properties of an evolutionary series of vertebrate elastins. Temperature-dependent swelling, low water contents and thermodynamics typical of hydrophobic systems were observed for all elastins except salmon. Salmon elastin, on the other hand, showed temperature-independent swelling and a high water content. Thermodynamic analysis showed that salmon elastin still contained a hydrophobic component. The swelling-temperature compensation hypothesis suggests that the extreme hydrophobic nature of elastin evolved in order to provide the proteins with temperature-dependent swelling and thus, maintaining elastic efficiency over a wide temperature range. All elastins should then be very hydrophobic systems which is inconsistent with the physical chemical results. All vertebrate elastins are not necessarily hydrophobic systems since salmon elastin shows no temperature-dependence to its swelling. The efficiency of a series of vertebrate elastins was measured over 0 to 60°C temperature range using a forced vibration technique. Over a wide frequency range, both lower and higher vertebrate elastins were capable of efficient spring-like behaviour. Both a higher vertebrate, with temperature-dependent swelling, and a lower vertebrate, with no temperaturate-dependence to its swelling, showed elastic efficiency. The swelling-temperature compensation hypothesis must be rejected.
Science, Faculty of
Zoology, Department of
Graduate
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9

Georgilis, Evangelos. "Engineering of Thermoresponsive Diblock Elastin-like Polypeptides." Thesis, Bordeaux, 2019. http://www.theses.fr/2019BORD0444.

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La thèse présentée porte sur l’ingénierie de diblocs de polypeptides à base de motifs élastine (ELPs) susceptibles de s’auto-assembler sous forme de nanoparticules après modification chimique de certains résidus. La stratégie inclue le développement de diblocs d’ELPs composés d’un bloc hydrophobe comportant l’isoleucine en position hôte, fusionné à l’extrémité N-terminale avec un bloc contenant des résidus méthionine chimiosélectivement modifiables. Des modifications du groupement thioéther permettent en effet l’hydrophilisation du segment ELP correspondant ainsi que l’introduction de groupements réactifs. Une première génération d’ELPs diblocs a été développée par génie génétique, production recombinante chez Escherichia coli et caractérisée. Le résidu cystéine à l’extrémité C-terminale a été modifié pour contrôler la monodispersité et introduire des fluorochromes, tandis que les résidus méthionine ont été modifiés pour changer l’équilibre hydrophile/hydrophobe et introduire des groupements réactifs. L’auto-assemblage des diblocs non-modifiés et post-modifiés a été étudiée par des mesures de turbidité et diffusion dynamique de la lumière. Ces méthodes ont mis en évidence une transition thermale de chaînes solubles en agrégats de taille micronique. Pour permettre la formation particules de taille nanométrique, une deuxième génération d’ELPs diblocs a été conçue grâce à l’application d’un modèle empirique. La deuxième génération d’ELPs diblocs forme effectivement des nanoparticules après modification chimiosélective des résidus méthionines. Ces structures pourront potentiellement contribuer au développement de nanoformulations à base d’ELPs
The present work focuses on the engineering of diblock elastin-like polypeptides (ELPs) that thermally assemble into nanostructures after the application of chemical modifications. The strategy involved the development of diblock ELPs composed of a hydrophobic isoleucine-containing block fused at its N-terminal end to a block containing residues amenable to chemoselective modifications, namely methionine. This particular residue was employed because the orthogonal modification of its thioether group allows for the change of the hydrophilic/lipophilic balance of the diblock ELP and the possible simultaneous grafting of functional ligands. A first generation of diblock ELPs was therefore designed by means of molecular clonings, produced in E. coli, and characterized by chemical methods to further monitor post-modifications. The chemical modifications were applied at the C-terminal cysteine to control the system monodispersity and introduce fluorescent probes, and also at methionine in order to change the hydrophilic/lipophilic balance and introduce reactive groups. The self-assembly of the non-modified and post-modified ELPs was monitored by means of turbidimetry, nanoparticle tracking analysis and dynamic light scattering, which showed that these sequences possessed a transition from monomers to aggregates. To access nanoparticle formation, a second generation of diblock ELPs was developed, the design of which was based on theoretical modeling. The second generation diblocks self-assembled into nanoparticles by means of methionine post-modifications. It is expected that these sequences will contribute to the development of diblock ELP-based nano-formulations
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Alanazi, Hamdan Noman. "Characterization of Elastin-Like Polypeptides Using Viscometry." Cleveland State University / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=csu1311026986.

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Books on the topic "Elastin"

1

Ladislas, Robert, and Hornebeck William 1946-, eds. Elastin and elastases. Boca Raton, Fla: CRC Press, 1989.

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Lawson-Smith, Rebecca K. Development of elastin-based biomaterials by PEG conjugation to an elastin polypeptide. Ottawa: National Library of Canada, 2003.

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M, Tamburro A., Davidson James M, and Università degli studi della Basilicata (Potenza, Italy), eds. Elastin: Chemical and biological aspects : proceedings of the International Congress, Maratea (Italy), October 10-13, 1988. Galatina [Italy]: Congedo editore, 1990.

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Derek, Chadwick, Goode Jamie, Ciba Foundation, and Symposium on the Molecular Biology and Pathology of Elastic Tissues (1994 : Nairobi, Kenya), eds. The molecular biology and pathology of elastic tissues. Chichester: J. Wiley, 1995.

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Raybould, Mark Christopher. Molecular variation in the human elastin gene. Birmingham: University of Birmingham, 1995.

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Chen, Vivian Wenjun. Human elastin peptide-coated synthetic materials in blood-contacting applications. Ottawa: National Library of Canada, 1999.

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Morley, Shari. Role of protein kinases in stretch-induced regulation of elastin synthesis through increasd translational efficiency. Ottawa: National Library of Canada, 1998.

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Smith, Adam Campbell. Functional deficiency in the 67-kD elastin binding protein is a crucial component of the pathomechanism of costello syndrome. Ottawa: National Library of Canada, 2000.

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Manohar, Advaitanand. Isolation and characterization of a 5' bovine genomic clone for elastin and the identification of putative CIS-acting element. Ottawa: National Library of Canada, 1990.

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Yang, Jianying. Biochemical studies of elastin and collagen accumulation in arteries and ventricles of normal developing rats and young spontaneously hypertensive rats. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1992.

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Book chapters on the topic "Elastin"

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Kozel, Beth A., Robert P. Mecham, and Joel Rosenbloom. "Elastin." In The Extracellular Matrix: an Overview, 267–301. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-16555-9_8.

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Steiner, G., and C. Zimmerer. "Elastin." In Polymer Solids and Polymer Melts – Definitions and Physical Properties I, 338–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-32072-9_24.

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Haubeck, H. D. "Elastin." In Springer Reference Medizin, 760. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_978.

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Haubeck, H. D. "Elastin." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_978-1.

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Davidson, Jeffrey M. "Elastin." In Connective Tissue Disease, 29–54. Boca Raton: CRC Press, 2021. http://dx.doi.org/10.1201/9781003210016-3.

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Bährle-Rapp, Marina. "Elastin." In Springer Lexikon Kosmetik und Körperpflege, 180. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_3524.

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Ehrlich, Hermann. "Marine Elastin." In Biological Materials of Marine Origin, 361–75. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-007-5730-1_10.

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Bährle-Rapp, Marina. "Hydrolyzed Elastin." In Springer Lexikon Kosmetik und Körperpflege, 268. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_4969.

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Bährle-Rapp, Marina. "Lauroyl Hydrolyzed Elastin." In Springer Lexikon Kosmetik und Körperpflege, 314. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-71095-0_5871.

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Pasquali-Ronchetti, Ivonne, Claudio Fornieri, Miranda Baccarani-Contri, and Daniela Quaglino. "Ulfrastructure of Elastin." In Novartis Foundation Symposia, 31–58. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514771.ch3.

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Conference papers on the topic "Elastin"

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Chow, Ming-Jay, Raphaël Turcotte, and Katherine Yanhang Zhang. "Elastin in the Arterial ECM: Interactions With Collagen and the Mechanical Properties After Elastin Degradation." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14257.

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Elastin and collagen are the main structural components in the extracellular matrix (ECM) that contribute to the anisotropic and hyperelastic passive mechanical behavior of elastic arteries. It is commonly accepted that the elastin fibers support most of the load at the onset of stretching while collagen fiber recruitment and the transition to collagen bearing the load occurs at higher pressures [1]. Various diseases lead to changes in the ECM, for example in aortic aneurysm there is reduced elastin, excess aged collagen, and fragmentation of the elastic lamellae [2]. Likewise hypertension has been shown to increase arterial collagen and wall thickness with increased stiffness [3]. Improving our knowledge of how the ECM structure affects the mechanical behavior of arteries can provide insights to disease progression and better treatment methods.
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Espinosa, Gabriela, Lisa Bennett, William Gardner, and Jessica Wagenseil. "The Effects of Extracellular Matrix Protein Insufficiency and Treatment on the Stiffness of Arterial Smooth Muscle Cells." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14131.

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Increased arterial stiffness is directly correlated with hypertension and cardiovascular disease. Stiffness of the conducting arteries is largely determined by the extracellular matrix (ECM) proteins in the wall, such as collagen and elastin, produced by the smooth muscle cells (SMCs) found in the medial layer. Elastin is deposited as soluble tropoelastin and is later crosslinked into elastin fibers. Newborn mice lacking the elastin protein ( Eln−/−) have increased arterial wall stiffness and SMCs with altered proliferation, migration and morphology [1]. Vessel elasticity is also mediated by other ECM proteins, such as fibulin-4. Elastic tissue, such as lung, skin, and arteries, from fibulin-4 deficient ( Fbln4−/−) mice show no decrease in elastin content, but have reduced elasticity due to disrupted elastin fibers [2]. Arteries from both elastin and fibulin-4 deficient mice have been previously studied, but the mechanical properties of their SMCs have not been investigated. Recent experiments comparing arterial SMCs from old and young animals suggest that mechanical properties of the SMCs themselves may contribute to changes in wall stiffness [3]. Hence, we investigated the stiffness of isolated arterial SMCs from elastin and fibulin-4 deficient mice using atomic force microscopy (AFM). In addition, we studied the effects of two elastin treatments on the mechanical properties of SMCs from Eln+/+ and Eln−/− mice. Differences between the treatments may elucidate the importance of soluble versus crosslinked elastin on single cell stiffness.
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Cheng, Jeffrey K., Robert P. Mecham, and Jessica E. Wagenseil. "Postnatal Time Course of Arterial Mechanics in a Mouse Model of Pathological Remodeling due to Decreased Elastin Amounts." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14346.

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Properly developed large elastic arteries serve as reservoirs that store stroke volume during systole and damp downstream blood pressure fluctuations. This function is enabled by the extracellular matrix (ECM) protein elastin. Mouse gene expression data reveals that elastin expression begins during embryonic development and peaks around postnatal day (P) 14. Expression then decreases to low levels for the remainder of adult life, indicating that elastin production during development is critical for a properly functioning vessel [1]. Reduced elastin in humans due to genetic mutations is associated with a congenital narrowing of the ascending aorta, known as supravalvular aortic stenosis, and chronic hypertension [2].
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Gruber, Matthew J., Varun Krishnamurthy, D. A. Narmoneva, and Robert B. Hinton. "Elastin Haploinsufficiency Is Associated With Altered Interstitial Phenotype and Progressive Aortopathy." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192891.

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Supravalvular aortic stenosis (SVAS) [1] is a disease of the cardiovascular system that leads to narrowing of the large arteries in humans. Studies have shown [2] that SVAS is caused by mutations or deletions in the elastin gene resulting in elastin haploinsufficiency. Elastin haploinsufficiency results in systemic hypertension [3], thinner and more numerous elastic lamellae [4], and altered arterial mechanics [5]. Genetically modified elastin deficient mice (ELN+/-) recapitulates the human phenotype including obstructive arterial disease and decreased arterial compliance [1,3]. Elastin deficiency in these mice is associated with changes in the mechanical microenvironment in the vascular wall [6], including enhanced wall thickness, increased smooth muscle cell (SMC) proliferation [7] and stiffening of arteries [8]. However, the molecular mechanisms for these changes are not fully understood. Also from a developmental perspective, no information is available regarding initiation and progression of aortic pathology in ELN+/− mice with time. The objectives of this study were to determine the temporal effects of elastin haploinsufficiency on the functional properties of aortic tissue and the aortic cell phenotype, using the elastin deficient mouse model (ELN+/-). We hypothesized that elastin haploinsufficiency will result in progressive abnormalities in aortic stiffness and dynamic alterations in aortic smooth muscle cell phenotype.
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McClure, Michael J., Scott A. Sell, and Gary L. Bowlin. "Multi Layered Polycaprolactone-Elastin-Collagen Small Diameter Conduits for Vascular Tissue Engineering." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192895.

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The architecture of the vascular wall is highly intricate and requires unique biomechanical properties in order to function properly. Native artery is composed of a mix of collagens, elastin, endothelial cells (ECs), smooth muscle cells (SMC), fibroblasts, and proteoglycans arranged into three distinct layers: the intima, media, and adventitia. Throughout artery, collagen and elastin play an important role, providing a mechanical backbone, preventing vessel rupture, and promoting recovery while undergoing pulsatile deformations [1]. The low-strain mechanical response of artery to blood flow is dominated by the elastic behavior, of elastin, which prevents pulsatile energy from being dissipated as heat [2]. A higher amount of energy loss indicates a decrease in recoverability, which could lead to eventual disruption of blood flow. An effective way to quantify recoverability is through hysteresis and compliance measurement. The hypothesis of this study was that the fabrication of a multi-layered electrospun tissue engineering scaffold composed of polycaprolactone (PCL), elastin, and collagen would demonstrate dynamic mechanical properties indicative of a highly elastic material, similar to the three distinct layers of native arterial tissue, while remaining conducive to tissue regeneration. PCL was chosen, in this case, to provide mechanical integrity and elasticity, while elastin and collagen would provide further elasticity and bioactivity [3,4].
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McClure, Michael J., Scott A. Sell, David G. Simpson, Beat H. Walpoth, and Gary L. Bowlin. "A Three Layered Electrospun Matrix to Mimic Native Arterial Architecture Using Polycaprolactone, Elastin, and Collagen: A Preliminary Study." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19172.

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The architecture of the vascular wall is highly intricate and requires unique biomechanical properties in order to function properly. Native artery is composed of a mix of collagens, elastin, endothelial cells (ECs), smooth muscle cells (SMC), fibroblasts, and proteoglycans arranged into three distinct layers: the intima, media, and adventitia. Throughout artery, collagen and elastin play an important role, providing a mechanical backbone, preventing vessel rupture, and promoting recovery while undergoing pulsatile deformations [1]. The low-strain mechanical response of artery to blood flow is dominated by the elastic behavior, of elastin, which prevents pulsatile energy from being dissipated as heat [2]. A higher amount of energy loss indicates a decrease in recoverability, which could lead to eventual disruption of blood flow. An effective way to quantify recoverability is through hysteresis and compliance measurement. The hypothesis of this study was that the fabrication of a multi-layered electrospun tissue engineering scaffold composed of polycaprolactone (PCL), elastin (ELAS), and collagen (COL) would demonstrate dynamic mechanical properties indicative of a highly elastic material, similar to the three distinct layers of native arterial tissue, while remaining conducive to tissue regeneration. PCL was chosen, in this case, to provide mechanical integrity and elasticity, while elastin and collagen would provide further elasticity and bioactivity [3,4].
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Olgar, Handan Arkin, and Mustafa Bilsel. "Simulations of elastin like proteins." In 2010 15th National Biomedical Engineering Meeting. IEEE, 2010. http://dx.doi.org/10.1109/biyomut.2010.5479831.

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Nagel, D., and R. M. Kottmann. "Dysregulated Elastin Promotes Pulmonary Fibrosis." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4219.

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Wang, Jingli, and Lisa Pruitt. "The Contribution of Elastin, Collagen, and Smooth Muscle Cells to Residual Strains in Large Elastic Arteries." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-59886.

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The contribution of elastin, collagen, and smooth muscle cells to residual strain in porcine aortas were evaluated by assessing several parameters: opening angle, neutral axis, and residual strain. Elastase or collagenase was used to remove elastin or collagen. Smooth muscle cells were activated using Ca2+/KCl solutions or deactivated using KCN solutions. Several statistically significant trends (P&lt;0.05) were obtained. As elastin was removed, the opening angle increased. As collagen was removed, the opening angle decreased. In addition, the activation of smooth muscle cells reduced the opening angle. Smooth muscle cell activation and collagenase digestion resulted in: 1) a decrease in residual strain and strain gradient, 2) the neutral axis shifting toward the adventitia side of the vessel wall.
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Haslach, Henry W., Jonathan Chung, and Aviva Molotsky. "Fracture Mechanisms in Bovine Aorta." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19366.

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Rupture of vascular tissue in the circulatory system under non-impact loading is involved in potentially life threatening events such as Marfan’s syndrome or rupture of small renal veins during shock wave lithotripsy. The rupture mechanisms are not well-understood. The complexity of the artery wall precludes the use of rupture theories invented for metals or for fibered composites with a homogeneous matrix. Artery tissue is composed of ground material, smooth muscle cells, elastin and collagen. The collagen fibers, which are generally circumferentially oriented, are the load carrying material after large deformations. Clark and Glagov [1] propose that the media of an elastic artery is built of musculo-elastic fascicles made up of a layer of circumferentially oriented SMC that lie parallel and between two elastin lamellae. Between the elastin sheets of adjacent elements are interspersed collagen fiber bundles.
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Reports on the topic "Elastin"

1

Chilkoti, Ashutosh. Elastin Bioelastomers for Microactuation. Fort Belvoir, VA: Defense Technical Information Center, December 2002. http://dx.doi.org/10.21236/ada415591.

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Gontar, I. P., O. I. Emelyanova, O. A. Rusanova, N. I. Emelyanov, and O. P. Slusar. LAMININ AND ELASTIN AS INITIAL AND SUBSEQUENT POINTS OF AUTOIMMUNE INFLAMMATION IN SCLERODERMA. "PLANET", 2019. http://dx.doi.org/10.18411/978-5-907192-54-6-2019-xxxvi-57-63.

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Gontar, I. P., O. I. Emelyanova, O. A. Rusanova, and N. I. Emelyanov. DISORDER OF IMMUNOPATHOGENESIS OF MAIN COLLAGEN TYPES AND ELASTIN ELASTASE SYSTEM IN SYSTEMIC SCLERODERMA. Планета, 2018. http://dx.doi.org/10.18411/978-5-907109-24-7-2018-xxxv-82-88.

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Bidwell, III, and Gene L. Thermally Targeted Delivery of a c-Myc Inhibitory Peptide In Vivo Using Elastin-like Polypeptide. Fort Belvoir, VA: Defense Technical Information Center, October 2009. http://dx.doi.org/10.21236/ada525489.

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Broadley, Caroline, Debra A. Gonzalez, Rhada Nair, and Jeffrey M. Davidson. Canine Vocal Fold Fibroblasts in Culture: Expression of alpha-Smooth Muscle Actin and Modulation of Elastin Synthesis. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada302739.

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Gontar, I. P., O. A. Rusanova, A. S. Trofimenko, O. I. Emelyanova, L. A. Maslakova, and N. Emelyanov. CARDIOVASCULAR CONDITIONS IN PATIENTS WITH SYSTEMIC SCLERODERMA THAT ARE ASSOCIATED WITH HUMORAL IMMUNITY IMPAIRMENT TO ELASTIN AND ELSTASE. Планета, 2018. http://dx.doi.org/10.18411/978-5-907109-24-7-2018-xxxiv-54-55.

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Loewenthal, M., K. Loseke, T. A. Dow, and R. O. Scattergood. Elastic emission polishing. Office of Scientific and Technical Information (OSTI), December 1988. http://dx.doi.org/10.2172/476648.

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Morgan and Gardiner. L51980 Monitoring Pipeline Coatings With the Elastic Wave In-Line Inspection Vehicle. Chantilly, Virginia: Pipeline Research Council International, Inc. (PRCI), March 2000. http://dx.doi.org/10.55274/r0011180.

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This report describes a program with the aim of improving discrimination of stress corrosion cracking (SCC) from non-SCC in data from the Elastic Wave (EW) in-line inspection tool. A major component of the work reported here was to create a database of features reported from Elastic Wave inspections. This allows consistent information to be collated for excavated features, as a basis for characterization of the EW tool's response to particular features. Following completion of the work reported here the database was transferred to Pipeline Integrity International, vendors of the Elastic Wave service.
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Yates, Steven, Sally Hicks, Jeffrey Vanhoy, and Marcus McEllistrem. Elastic/Inelastic Measurement Project. Office of Scientific and Technical Information (OSTI), March 2016. http://dx.doi.org/10.2172/1242960.

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Kramer, Mitchell. Elastic Path Commerce 6.2. Boston, MA: Patricia Seybold Group, January 2010. http://dx.doi.org/10.1571/pr01-14-10cc.

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