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Journal articles on the topic 'Elastin'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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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 (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 an

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2

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 (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

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3

Trębacz, Hanna, and Angelika Barzycka. "Mechanical Properties and Functions of Elastin: An Overview." Biomolecules 13, no. 3 (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

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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 (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

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Boëté, Quentin, Ming Lo, Kiao-Ling Liu, 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 (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 e

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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 (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-syn

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Nishizaki, Tomoyuki. "PKCε Increases Extracellular Elastin and Fibulin-5/DANCE in Dermal Fibroblasts". Cellular Physiology and Biochemistry 46, № 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 pres

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8

Nygaard, Rie Harboe, Scott Maynard, Peter Schjerling, et al. "Acquired Localized Cutis Laxa due to Increased Elastin Turnover." Case Reports in Dermatology 8, no. 1 (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

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9

Sambani, Kyriaki, Stylianos Vasileios Kontomaris, and Dido Yova. "Atomic Force Microscopy Imaging of Elastin Nanofibers Self-Assembly." Materials 16, no. 12 (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 elasti

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10

Cantor, Jerome. "Elastin Peptides as a Potential Disease Vector in the Pathogenesis of Pulmonary Emphysema: An Investigation of This Hypothesis." Life 15, no. 3 (2025): 356. https://doi.org/10.3390/life15030356.

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The degradation of elastic fibers is a fundamental characteristic of pulmonary emphysema, resulting in the release of proinflammatory elastin peptides. The findings discussed in this paper support the hypothesis that these peptides act as carriers of disease, interacting with elastin receptor complexes that promote inflammation, elastic fiber damage, and airspace enlargement. Studies from our laboratory show that the breakdown of these fibers is significantly enhanced by intratracheal instillation of elastin peptides in a lipopolysaccharide-induced model of acute lung injury. This result is co

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11

Powell, J. T. "Evidence against lung galaptin being important to the synthesis or organization of the elastic fibril." Biochemical Journal 252, no. 2 (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 presen

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Saitow, Cassandra B., Steven G. Wise, Anthony S. Weiss, John J. Castellot, and David L. Kaplan. "Elastin biology and tissue engineering with adult cells." BioMolecular Concepts 4, no. 2 (2013): 173–85. http://dx.doi.org/10.1515/bmc-2012-0040.

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AbstractThe inability of adult cells to produce well-organized, robust elastic fibers has long been a barrier to the successful engineering of certain tissues. In this review, we focus primarily on elastin with respect to tissue-engineered vascular substitutes. To understand elastin regulation during normal development, we describe the role of various elastic fiber accessory proteins. Biochemical pathways regulating expression of the elastin gene are addressed, with particular focus on tissue-engineering research using adult-derived cells.

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Cocciolone, Austin J., Jie Z. Hawes, Marius C. Staiculescu, Elizabeth O. Johnson, Monzur Murshed, and Jessica E. Wagenseil. "Elastin, arterial mechanics, and cardiovascular disease." American Journal of Physiology-Heart and Circulatory Physiology 315, no. 2 (2018): H189—H205. http://dx.doi.org/10.1152/ajpheart.00087.2018.

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Large, elastic arteries are composed of cells and a specialized extracellular matrix that provides reversible elasticity and strength. Elastin is the matrix protein responsible for this reversible elasticity that reduces the workload on the heart and dampens pulsatile flow in distal arteries. Here, we summarize the elastin protein biochemistry, self-association behavior, cross-linking process, and multistep elastic fiber assembly that provide large arteries with their unique mechanical properties. We present measures of passive arterial mechanics that depend on elastic fiber amounts and integr

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14

Paulovic, R. P., and R. A. Anwar. "Developmental regulation of the mRNAs for elastins a, b and c in foetal-calf nuchal ligament and aorta." Biochemical Journal 261, no. 1 (1989): 227–32. http://dx.doi.org/10.1042/bj2610227.

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The data presented clearly suggest that relative amounts of mRNAs for elastins a, b and c are developmentally regulated in foetal-calf nuchal ligament and aorta and that this regulation is tissue-specific. In nuchal ligament, at earlier stages of foetal development, the relative amounts of mRNAs for elastins a and b are very low. After the foetal age of about 6 months the relative amount of mRNA for elastin b begins to increase. This is followed by an increase in the relative amount of mRNA for elastin a. In aorta, with increasing foetal age, the relative amounts of mRNAs for elastins b and c

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Bressan, G. M., D. Daga-Gordini, A. Colombatti, I. Castellani, V. Marigo, and D. Volpin. "Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface." Journal of Cell Biology 121, no. 1 (1993): 201–12. http://dx.doi.org/10.1083/jcb.121.1.201.

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The fine distribution of the extracellular matrix glycoprotein emilin (previously known as glycoprotein gp115) (Bressan, G. M., I. Castellani, A. Colombatti, and D. Volpin. 1983. J. Biol. Chem. 258: 13262-13267) has been studied at the ultrastructural level with specific antibodies. In newborn chick aorta the protein was exclusively found within elastic fibers. In both post- and pre-embedding immunolabeling emilin was mainly associated with regions where elastin and microfibrils are in close contact, such as the periphery of the fibers. This localization of emilin in aorta has been confirmed b

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16

Akiyama, Mari. "Elastic Fibers and F-Box and WD-40 Domain-Containing Protein 2 in Bovine Periosteum and Blood Vessels." Biomimetics 8, no. 1 (2022): 7. http://dx.doi.org/10.3390/biomimetics8010007.

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Elastic fibers form vessel walls, and elastic fiber calcification causes serious vascular diseases. Elastin is a well-known elastic fiber component; however, the insoluble nature of elastic fibers renders elastic fiber component analysis difficult. A previous study investigated F-box and WD-40 domain-containing protein 2 (FBXW2) in the cambium layer of bovine periosteum and hypothesized that fiber structures of FBXW2 are coated with osteocalcin during explant culture. Here, FBXW2 was expressed around some endothelial cells but not in all microvessels of the bovine periosteum. The author hypoth

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17

Moset Zupan, Andreja Moset, Carolyn Nietupski, and Stacey C. Schutte. "Cyclic Adenosine Monophosphate Eliminates Sex Differences in Estradiol-Induced Elastin Production from Engineered Dermal Substitutes." International Journal of Molecular Sciences 22, no. 12 (2021): 6358. http://dx.doi.org/10.3390/ijms22126358.

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Lack of adult cells’ ability to produce sufficient amounts of elastin and assemble functional elastic fibers is an issue for creating skin substitutes that closely match native skin properties. The effects of female sex hormones, primarily estrogen, have been studied due to the known effects on elastin post-menopause, thus have primarily included older mostly female populations. In this study, we examined the effects of female sex hormones on the synthesis of elastin by female and male human dermal fibroblasts in engineered dermal substitutes. Differences between the sexes were observed with 1

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18

Ohnishi, Y., M. Akiyama, S. Tajima, A. Ishibashi, and Y. Seyama. "Elastic Nevus With Normal Expression of Elastin and Elastin-Related Proteins mRNAs." Dermatology 198, no. 3 (1999): 307–9. http://dx.doi.org/10.1159/000018138.

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19

Joss-Moore, Lisa A., Yan Wang, Xing Yu, et al. "IUGR decreases elastin mRNA expression in the developing rat lung and alters elastin content and lung compliance in the mature rat lung." Physiological Genomics 43, no. 9 (2011): 499–505. http://dx.doi.org/10.1152/physiolgenomics.00183.2010.

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Complications of intrauterine growth restriction (IUGR) include increased pulmonary morbidities and impaired alveolar development. Normal alveolar development depends upon elastin expression and processing, as well as the formation and deposition of elastic fibers. This is true of the human and rat. In this study, we hypothesized that uteroplacental insufficiency (UPI)-induced IUGR decreases mRNA levels of elastin and genes required for elastin fiber synthesis and assembly, at birth (prealveolarization) and postnatal day 7 (midalveolarization) in the rat. We further hypothesized that this woul

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20

Yu, J. "Elastic tissues of the intervertebral disc." Biochemical Society Transactions 30, no. 6 (2002): 848–52. http://dx.doi.org/10.1042/bst0300848.

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Elastic fibres have been generally considered to play no significant role in the mechanical functioning of the intervertebral disc since earlier studies reported that the elastic fibre network was sparse and irregular. However, a recent study has reported that the network is highly organized and that the distribution and orientation of elastic fibres varies from region to region. In the annulus, elastic fibres appear densely distributed in the region between the lamellae and also in ‘bridges’ across the lamellae. They are also organized in the nucleus where long straight fibres are radially or

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Li, Fei, Xuan Li, Yue-tang Wang, et al. "The Etiological Heterogeneity of Bicuspid Aortopathy between Ascending and Root Morphotype." Heart Surgery Forum 23, no. 6 (2020): E913—E919. http://dx.doi.org/10.1532/hsf.3333.

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Background: Valve-related hemodynamics and intrinsically regulated matrix proteases are 2 determined pathogenetic factors associated with medial elastin degeneration in bicuspid aortopathy. This study analyzed the association between elastic fiber deterioration and the 2 pathogenetic factors in ascending and root morphotypes, aiming to elucidate the etiological heterogeneity between the 2 morphotypes. Methods: Four-dimensional flow cardiac magnetic resonance was used to measure the regional wall shear stress (WSS) on the ascending aorta, and matrix metalloproteinase (MMP) expression was assess

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Bland, Richard D., Robert Ertsey, Lucia M. Mokres, et al. "Mechanical ventilation uncouples synthesis and assembly of elastin and increases apoptosis in lungs of newborn mice." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 1 (2008): L3—L14. http://dx.doi.org/10.1152/ajplung.00362.2007.

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Prolonged mechanical ventilation (MV) with O2-rich gas inhibits lung growth and causes excess, disordered accumulation of lung elastin in preterm infants, often resulting in chronic lung disease (CLD). Using newborn mice, in which alveolarization occurs postnatally, we designed studies to determine how MV with either 40% O2or air might lead to dysregulated elastin production and impaired lung septation. MV of newborn mice for 8 h with either 40% O2or air increased lung mRNA for tropoelastin and lysyl oxidase, relative to unventilated controls, without increasing lung expression of genes that r

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BROWN-AUGSBURGER, Patricia, Thomas BROEKELMANN, Joel ROSENBLOOM, and Robert P. MECHAM. "Functional domains on elastin and microfibril-associated glycoprotein involved in elastic fibre assembly." Biochemical Journal 318, no. 1 (1996): 149–55. http://dx.doi.org/10.1042/bj3180149.

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Studies in vitro suggest that the C-terminus of tropoelastin mediates elastin polymerization through an interaction with microfibril-associated proteins. In this study we have used cultured auricular chondrocytes as a model system to examine whether this interaction is critical for elastic fibre formation in vivo. Auricular chondrocytes, which deposit an abundant elastic fibre matrix, were cultured in the presence of Fab fragments of antibodies directed against the C-terminus (CTe) or an N-terminal domain (ATe) of tropoelastin. Immunofluorescent staining of the extracellular matrix deposited b

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Reichheld, Sean E., Lisa D. Muiznieks, Fred W. Keeley, and Simon Sharpe. "Direct observation of structure and dynamics during phase separation of an elastomeric protein." Proceedings of the National Academy of Sciences 114, no. 22 (2017): E4408—E4415. http://dx.doi.org/10.1073/pnas.1701877114.

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Despite its growing importance in biology and in biomaterials development, liquid–liquid phase separation of proteins remains poorly understood. In particular, the molecular mechanisms underlying simple coacervation of proteins, such as the extracellular matrix protein elastin, have not been reported. Coacervation of the elastin monomer, tropoelastin, in response to heat and salt is a critical step in the assembly of elastic fibers in vivo, preceding chemical cross-linking. Elastin-like polypeptides (ELPs) derived from the tropoelastin sequence have been shown to undergo a similar phase separa

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Fhayli, Wassim, Quentin Boëté, Nadjib Kihal, et al. "Dill Extract Induces Elastic Fiber Neosynthesis and Functional Improvement in the Ascending Aorta of Aged Mice with Reversal of Age-Dependent Cardiac Hypertrophy and Involvement of Lysyl Oxidase-Like-1." Biomolecules 10, no. 2 (2020): 173. http://dx.doi.org/10.3390/biom10020173.

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Elastic fibers (90% elastin, 10% fibrillin-rich microfibrils) are synthesized only in early life and adolescence mainly by the vascular smooth muscle cells through the cross-linking of its soluble precursor, tropoelastin. Elastic fibers endow the large elastic arteries with resilience and elasticity. Normal vascular aging is associated with arterial remodeling and stiffening, especially due to the end of production and degradation of elastic fibers, leading to altered cardiovascular function. Several pharmacological treatments stimulate the production of elastin and elastic fibers. In particul

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Muiznieks, Lisa D., Anthony S. Weiss, and Fred W. Keeley. "Structural disorder and dynamics of elastinThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 2 (2010): 239–50. http://dx.doi.org/10.1139/o09-161.

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Elastin is a self-assembling, extracellular-matrix protein that is the major provider of tissue elasticity. Here we review structural studies of elastin from over four decades, and draw together evidence for solution flexibility and conformational disorder that is inherent in all levels of structural organization. The characterization of disorder is consistent with an entropy-driven mechanism of elastic recoil. We conclude that conformational disorder is a constitutive feature of elastin structure and function.

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Zheng, Qian, Elaine C. Davis, James A. Richardson, et al. "Molecular Analysis of Fibulin-5 Function during De Novo Synthesis of Elastic Fibers." Molecular and Cellular Biology 27, no. 3 (2007): 1083–95. http://dx.doi.org/10.1128/mcb.01330-06.

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ABSTRACT Elastic fibers contribute to the structural support of tissues and to the regulation of cellular behavior. Mice deficient for the fibulin-5 gene (fbln5 − / −) were used to further elucidate the molecular mechanism of elastic fiber assembly. Major elastic fiber components were present in the skin of fbln5 − / − mice despite a dramatic reduction of mature elastic fibers. We found that fibulin-5 preferentially bound the monomeric form of elastin through N-terminal and C-terminal elastin-binding regions and to a preexisting matrix scaffold through calcium-binding epidermal growth factor (

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Lei, Ting, Lin Ye, Yunlin Pei, Huaiqing Sun, and Chaowan Guo. "Applications of Elastin in Cosmetics: Prospects and Challenges." Cosmetics 12, no. 1 (2025): 18. https://doi.org/10.3390/cosmetics12010018.

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Elastin is a crucial component of the extracellular matrix that plays a significant role in maintaining skin elasticity and firmness. Within the dermis, elastin works in collaboration with collagen to form supportive structures that contribute to the overall health and appearance of the skin. As individuals age, the rate of elastin synthesis gradually declines, resulting in the degradation of skin elastic fibers, which subsequently leads to skin laxity and the formation of wrinkles. Furthermore, environmental factors, particularly ultraviolet radiation, can exacerbate the degradation of elasti

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Oberson, D., L. Desfontaines, H. Pezerat, W. Hornebeck, P. Sebastien, and C. Lafuma. "Inhibition of human leukocyte elastase by mineral dust particles." American Journal of Physiology-Lung Cellular and Molecular Physiology 270, no. 5 (1996): L761—L771. http://dx.doi.org/10.1152/ajplung.1996.270.5.l761.

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After isolation, purification, and radiolabeling of elastin from baboon aorta and lung, the rates of hydrolysis of both 3H-labeled elastins by porcine pancreatic elastase (PPE or by human leukocyte elastase (HLE) were compared. PPE (30 nM) degraded aorta and lung elastins at rates of 40 and 75 micrograms/h, respectively, leading to their complete solubilization. In contrast, the low rate of hydrolysis of lung elastin (10 micrograms/h) by HLE was paradoxically accompanied with a fivefold decrease in the Michaelis constant value and became negligible after 1 h of incubation. Moreover, HLE adsorp

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XIONG, Jiang, Wei GUO, Ren WEI, Shang-wei ZUO, Xiao-ping LIU, and Tao ZHANG. "Elastic fiber regeneration in vitro and in vivo for treatment of experimental abdominal aortic aneurysm." Chinese Medical Journal 126, no. 3 (2013): 437–41. http://dx.doi.org/10.3760/cma.j.issn.0366-6999.20122151.

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Background The pathological characteristics of abdominal aortic aneurysm (AAA) involved the regression of extracellular matrix (ECM) in aortic walls, especially elastic structure in medial layer. As the major structural protein of aorta, elastin contributes to the extensibility and elastic recoil of the vessels. We hypothesized that overexpression of elastin in vessel walls might regenerate the elastic structure of ECM, restore the elastic structure of the aneurysmal wall, and eventually lead to a reduction of aortic diameters (ADs) in an experimental model of AAA. Methods Tropoelastin (TE) of

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Keeley, F. W., C. M. Bellingham, and K. A. Woodhouse. "Elastin as a self–organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self–assembly of elastin." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1418 (2002): 185–89. http://dx.doi.org/10.1098/rstb.2001.1027.

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Elastin is the major extracellular matrix protein of large arteries such as the aorta, imparting characteristics of extensibility and elastic recoil. Once laid down in tissues, polymeric elastin is not subject to turnover, but is able to sustain its mechanical resilience through thousands of millions of cycles of extension and recoil. Elastin consists of ca . 36 domains with alternating hydrophobic and cross–linking characteristics. It has been suggested that these hydrophobic domains, predominantly containing glycine, proline, leucine and valine, often occurring in tandemly repeated sequences

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Hurle, J. M., G. Corson, K. Daniels, R. S. Reiter, L. Y. Sakai, and M. Solursh. "Elastin exhibits a distinctive temporal and spatial pattern of distribution in the developing chick limb in association with the establishment of the cartilaginous skeleton." Journal of Cell Science 107, no. 9 (1994): 2623–34. http://dx.doi.org/10.1242/jcs.107.9.2623.

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In this work we have analyzed the presence of elastic components in the extracellular matrices of the developing chick leg bud. The distributions of elastin and fibrillin were studied immunohistochemically in whole-mount preparations using confocal laser microscopy. The association of these constituents of the elastic matrix with other components of the extracellular matrix was also studied, using several additional antibodies. Our results reveal the transient presence of an elastin-rich scaffold of extracellular matrix fibrillar material in association with the establishment of the cartilagin

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Roark, E. F., D. R. Keene, C. C. Haudenschild, S. Godyna, C. D. Little, and W. S. Argraves. "The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study." Journal of Histochemistry & Cytochemistry 43, no. 4 (1995): 401–11. http://dx.doi.org/10.1177/43.4.7534784.

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We examined the pattern of fibulin-1 mRNA and protein expression in human tissues and cell lines. Fibulin-1 transcripts were found in RNA isolated from most tissues and a variety of cultured cells, including fibroblasts, smooth muscle cells, and several epithelial cell lines, but not endothelial cells, lymphomyloid cells, or a number of carcinoma and melanoma lines. Immunohistochemical analysis showed that fibulin-1 is an intercellular component of connective tissues, predominantly associated with matrix fibers in tissues such as the cervix, dermis, intimal and medial layers of blood vessels,

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Lammers, Steven R., Phil H. Kao, H. Jerry Qi, et al. "Changes in the structure-function relationship of elastin and its impact on the proximal pulmonary arterial mechanics of hypertensive calves." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 4 (2008): H1451—H1459. http://dx.doi.org/10.1152/ajpheart.00127.2008.

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Extracellular matrix remodeling has been proposed as one mechanism by which proximal pulmonary arteries stiffen during pulmonary arterial hypertension (PAH). Although some attention has been paid to the role of collagen and metallomatrix proteins in affecting vascular stiffness, much less work has been performed on changes in elastin structure-function relationships in PAH. Such work is warranted, given the importance of elastin as the structural protein primarily responsible for the passive elastic behavior of these conduit arteries. Here, we study structure-function relationships of fresh ar

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Mizuno, Tomohiro, Donald A. G. Mickle, Chris G. Kiani, and Ren-Ke Li. "Overexpression of elastin fragments in infarcted myocardium attenuates scar expansion and heart dysfunction." American Journal of Physiology-Heart and Circulatory Physiology 288, no. 6 (2005): H2819—H2827. http://dx.doi.org/10.1152/ajpheart.00862.2004.

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Ventricular dilation after myocardial infarction can cause heart failure. Increasing strength and elasticity in the infarct region might prevent ventricular dilation. Because elastin provides strength, extensibility, and resilience to tissues and maintains tissue architecture, we studied the effect of elastin expression in the infarct on scar expansion and heart function. COS-7 cells transfected with a plasmid with an elastin gene fragment or a vector were seeded into a Gelfoam mesh and cultured. Mechanical stretch test ( n = 5/group) showed that the elastin mesh was more elastic ( P < 0.05

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Arribas, Silvia M., Ana M. Briones, Catherine Bellingham, et al. "Heightened aberrant deposition of hard-wearing elastin in conduit arteries of prehypertensive SHR is associated with increased stiffness and inward remodeling." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 6 (2008): H2299—H2307. http://dx.doi.org/10.1152/ajpheart.00155.2008.

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Elastin is a major component of conduit arteries and a key determinant of vascular viscoelastic properties. Aberrant organization of elastic lamellae has been reported in resistance vessels from spontaneously hypertensive rats (SHR) before the development of hypertension. Hence, we have characterized the content and organization of elastic lamellae in conduit vessels of neonatal SHR in detail, comparing the carotid arteries from 1-wk-old SHR with those from Wistar-Kyoto (WKY) and Sprague Dawley (SD) rats. The general structure and mechanics were studied by pressure myography, and the internal

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Shifren, Adrian, Anthony G. Durmowicz, Russell H. Knutsen, Gilles Faury, and Robert P. Mecham. "Elastin insufficiency predisposes to elevated pulmonary circulatory pressures through changes in elastic artery structure." Journal of Applied Physiology 105, no. 5 (2008): 1610–19. http://dx.doi.org/10.1152/japplphysiol.90563.2008.

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Elastin is a major structural component of large elastic arteries and a principal determinant of arterial biomechanical properties. Elastin loss-of-function mutations in humans have been linked to the autosomal-dominant disease supravalvular aortic stenosis, which is characterized by stenotic lesions in both the systemic and pulmonary circulations. To better understand how elastin insufficiency influences the pulmonary circulation, we evaluated pulmonary cardiovascular physiology in a unique set of transgenic and knockout mice with graded vascular elastin dosage (range 45–120% of wild type). T

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Pepe, Antonietta, and Brigida Bochicchio. "An Elastin-Derived Self-Assembling Polypeptide." Journal of Soft Matter 2013 (June 13, 2013): 1–7. http://dx.doi.org/10.1155/2013/732157.

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Elastin is an extracellular matrix protein responsible for the elastic properties of organs and tissues, the elastic properties being conferred to the protein by the presence of elastic fibers. In the perspective of producing tailor-made biomaterials of potential interest in nanotechnology and biotechnology fields, we report a study on an elastin-derived polypeptide. The choice of the polypeptide sequence encoded by exon 6 of Human Tropoelastin Gene is dictated by the peculiar sequence of the polypeptide. As a matter of fact, analogously to elastin, it is constituted of a hydrophobic region (G

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Manohar, Advaitanand, Wen Shi, and Rashid A. Anwar. "Partial characterization of bovine elastin gene; comparison with the gene for human elastin." Biochemistry and Cell Biology 69, no. 2-3 (1991): 185–92. http://dx.doi.org/10.1139/o91-027.

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A 14 kilobase (kb) genomic clone of the gene for bovine elastin, containing exons 1 and 2, has been characterized. This clone extends about 6.5 kb in the 5′ direction from the initiation codon and 978 nucleotides in the 3′ direction from exon 2. The size of the first intron is about 6.4 kb. The sequence immediately 5′ to the initiation codon is highly conserved between the genes for bovine and human elastins and contains a TATA box consensus sequence (ATAAA), CAAT, and Sp1 binding sites. Several putative AP-2 binding sites are also present. Comparative analysis of the sequences flanking the fi

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Subramaniam, K., H. Kumar, and M. H. Tawhai. "Evidence for age-dependent air-space enlargement contributing to loss of lung tissue elastic recoil pressure and increased shear modulus in older age." Journal of Applied Physiology 123, no. 1 (2017): 79–87. http://dx.doi.org/10.1152/japplphysiol.00208.2016.

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As a normal part of mature aging, lung tissue undergoes microstructural changes such as alveolar air-space enlargement and redistribution of collagen and elastin away from the alveolar duct. The older lung also experiences an associated decrease in elastic recoil pressure and an increase in specific tissue elastic moduli, but how this relates mechanistically to microstructural remodeling is not well-understood. In this study, we use a structure-based mechanics analysis to elucidate the contributions of age-related air-space enlargement and redistribution of elastin and collagen to loss of lung

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Green, Ellen M., Jessica C. Mansfield, James S. Bell, and C. Peter Winlove. "The structure and micromechanics of elastic tissue." Interface Focus 4, no. 2 (2014): 20130058. http://dx.doi.org/10.1098/rsfs.2013.0058.

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Elastin is a major component of tissues such as lung and blood vessels, and endows them with the long-range elasticity necessary for their physiological functions. Recent research has revealed the complexity of these elastin structures and drawn attention to the existence of extensive networks of fine elastin fibres in tissues such as articular cartilage and the intervertebral disc. Nonlinear microscopy, allowing the visualization of these structures in living tissues, is informing analysis of their mechanical properties. Elastic fibres are complex in composition and structure containing, in a

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White, J. F., J. L. Hughes, J. S. Kumaratilake, et al. "Post-embedding methods for immunolocalization of elastin and related components in tissues." Journal of Histochemistry & Cytochemistry 36, no. 12 (1988): 1543–51. http://dx.doi.org/10.1177/36.12.3142951.

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Elastic tissue is composed of amorphous-appearing elastin and 12-nm diameter microfibrils, one component of which has recently been isolated and characterized as the 31 KD microfibril-associated glycoprotein MAGP. Monospecific antibodies to each of these components have been developed in this laboratory. The parameters that determine optimal localization of colloidal gold probes for post-embedding immunolabeling of elastic tissue components have been systematically studied in a variety of normal and developing tissues in mammals and birds. Protein A-gold probes stabilized with dextran have bee

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SEYAMA, Yoshiyuki, Saburo YAMASHITA, and Shogo TOKUDOME. "Study of Elastin." Journal of Japan Atherosclerosis Society 15, no. 3 (1987): 797–802. http://dx.doi.org/10.5551/jat1973.15.3_797.

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Armentano, R. L., J. Levenson, J. G. Barra, et al. "Assessment of elastin and collagen contribution to aortic elasticity in conscious dogs." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 6 (1991): H1870—H1877. http://dx.doi.org/10.1152/ajpheart.1991.260.6.h1870.

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The elastic behavior of total elastin (EE) and collagen (EC) and the recruitment of collagen fibers (FC) supporting wall stress at a given transmural pressure level were assessed in seven conscious dogs using descending thoracic aortic pressure (microtransducer) and diameter (sonomicrometer) measurements. Stress-strain relationships values calculated at control and during bolus administration of angiotensin and nitroglycerin enabled quantification of angiotensin and nitroglycerin enabled quantification of elastic moduli of elastin (EE = 4.868 +/- 1.753 x 10(6) dyn/cm2; means +/- SD) and collag

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Carvalho, Olga Maria de Silvério. "Sexual Dimorphism of Elastic Fibers in Prenatal Lung Mice." European Journal of Biology and Biotechnology 5, no. 3 (2024): 8–15. http://dx.doi.org/10.24018/ejbio.2024.5.3.507.

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Scientific data has revealed the existence of lung gender differences and therefore sparked a renewed interest in understanding the underlying mechanisms and their effect in the healthy lung development and/or in pathological conditions. Elastic fibers have an important role in lung development during pre and post-natal stages, because a well-developed pulmonary elastic fibers favour pre-natal lung maturation and enhance alveolarization. Sexual differences studies on lung elastic fibers content are focused essentially on the post-natal stage, with scarce data on pre-natal lung development. Usi

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Goldman, Jeremy, Shu Q. Liu, and Brandon J. Tefft. "Anti-Inflammatory and Anti-Thrombogenic Properties of Arterial Elastic Laminae." Bioengineering 10, no. 4 (2023): 424. http://dx.doi.org/10.3390/bioengineering10040424.

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Elastic laminae, an elastin-based, layered extracellular matrix structure in the media of arteries, can inhibit leukocyte adhesion and vascular smooth muscle cell proliferation and migration, exhibiting anti-inflammatory and anti-thrombogenic properties. These properties prevent inflammatory and thrombogenic activities in the arterial media, constituting a mechanism for the maintenance of the structural integrity of the arterial wall in vascular disorders. The biological basis for these properties is the elastin-induced activation of inhibitory signaling pathways, involving the inhibitory cell

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Kuang, Ping-Ping, and Ronald H. Goldstein. "Regulation of elastin gene transcription by proteasome dysfunction." American Journal of Physiology-Cell Physiology 289, no. 3 (2005): C766—C773. http://dx.doi.org/10.1152/ajpcell.00525.2004.

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Elastin, a major extracellular matrix protein and the core component of elastic fiber, is essential to maintain lung structural integrity and normal physiological function. We previously found that the downregulation of elastin gene transcription by IL-1β is mediated via activation of NF-κB and CCAAT/enhancer binding protein (C/EBP)β, both targets of the ubiquitin-proteasome pathway. To further investigate the molecular mechanisms that underlie the control of elastin gene expression, we disrupted the ubiquitin-proteasome pathway with specific proteasome inhibitors. We found that specific prote

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Su, Hengjie, Tomoko Fujiwara, and Joel D. Bumgardner. "A Study of Combining Elastin in the Chitosan Electrospinning to Increase the Mechanical Strength and Bioactivity." Marine Drugs 19, no. 3 (2021): 169. http://dx.doi.org/10.3390/md19030169.

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While electrospun chitosan membranes modified to retain nanofibrous morphology have shown promise for use in guided bone regeneration applications in in vitro and in vivo studies, their mechanical tear strengths are lower than commercial collagen membranes. Elastin, a natural component of the extracellular matrix, is a protein with extensive elastic property. This work examined the incorporation of elastin into electrospun chitosan membranes to improve their mechanical tear strengths and to further mimic the native extracellular composition for guided bone regeneration (GBR) applications. In t

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Sanaei, Kaveh, Sydney Plotner, Anson Oommen Jacob, Jaime Ramirez-Vick, Narendra Vyavahare, and Nasim Nosoudi. "Effect of all-trans retinoic acid and pentagalloyl glucose on smooth muscle cell elastogenesis." Bio-Medical Materials and Engineering 32, no. 3 (2021): 145–57. http://dx.doi.org/10.3233/bme-201152.

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BACKGROUND: The main objective of tissue engineering is to fabricate a tissue construct that mimics native tissue both biologically and mechanically. A recurring problem for tissue-engineered blood vessels (TEBV) is deficient elastogenesis from seeded smooth muscle cells. Elastin is an integral mechanical component in blood vessels, allowing elastic deformation and retraction in response to the shear and pulsatile forces of the cardiac system. OBJECTIVE: The goal of this research is to assess the effect of the vitamin A derivative all-trans retinoic acid (RA) and polyphenol pentagalloyl glucos

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Joyce, Belinda J., Megan J. Wallace, Richard A. Pierce, Richard Harding, and Stuart B. Hooper. "Sustained changes in lung expansion alter tropoelastin mRNA levels and elastin content in fetal sheep lungs." American Journal of Physiology-Lung Cellular and Molecular Physiology 284, no. 4 (2003): L643—L649. http://dx.doi.org/10.1152/ajplung.00090.2002.

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Our objective was to determine the effects of sustained alterations in fetal lung expansion on pulmonary elastin synthesis. In fetal sheep, lung expansion was either decreased between 111 and 131 days' gestation (term ∼147 days) by tracheal drainage or increased for 2, 4, 7, or 10 days by tracheal obstruction, ending at 128 days' gestation. Lung tropoelastin mRNA levels were assessed by Northern blot analysis, total elastin content was measured biochemically, and staining of lung sections was used to assess the localization and form of elastic fibers. Tracheal obstruction significantly elevate

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