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Artículos de revistas sobre el tema "Extracellular matrix Physiology"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 28 de enero de 2023

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1

Roman, Jesse, Andrew H. Limper y John A. McDonald. "Lung Extracellular Matrix: Physiology and Pathophysiology". Hospital Practice 25, n.º 11 (15 de noviembre de 1990): 125–40. http://dx.doi.org/10.1080/21548331.1990.11704038.

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2

Bloksgaard, Maria, Merry Lindsey y Luis A. Martinez-Lemus. "Extracellular matrix in cardiovascular pathophysiology". American Journal of Physiology-Heart and Circulatory Physiology 315, n.º 6 (1 de diciembre de 2018): H1687—H1690. http://dx.doi.org/10.1152/ajpheart.00631.2018.

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The extracellular matrix (ECM) actively participates in diverse aspects of cardiovascular development and physiology as well as during disease development and progression. ECM roles are determined by its physical and mechanical properties and by its capacity to both release bioactive signals and activate cell signaling pathways. The ECM serves as a storage depot for a wide variety of molecules released in response to injury or with aging. Indeed, there is a plethora of examples describing how cells react to or modify ECM stiffness, how cells initiate intracellular signaling pathways, and how cells respond to the ECM. This Perspectives article reviews the contributions of 21 articles published in the American Journal of Physiology-Heart and Circulatory Physiology in response to a Call for Papers on this topic. Here, we summarize the contributions of these studies focused on the cardiac and vascular ECM. We highlight the translational importance of these studies and conclude that the ECM is a critical component of both the heart and vasculature. Readers are urged to examine and learn from this special Call for Papers.

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3

Wijsman, Pieta C., Lisa H. van Smoorenburg, Daniël M. de Bruin, Jouke T. Annema, Huib AM Kerstjens, Onno M. Mets, Maarten van den Berge, Peter I. Bonta y Janette K. Burgess. "Imaging the pulmonary extracellular matrix". Current Opinion in Physiology 22 (agosto de 2021): 100444. http://dx.doi.org/10.1016/j.cophys.2021.05.007.

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4

Rienks, Marieke, Anna-Pia Papageorgiou, Nikolaos G. Frangogiannis y Stephane Heymans. "Myocardial Extracellular Matrix". Circulation Research 114, n.º 5 (28 de febrero de 2014): 872–88. http://dx.doi.org/10.1161/circresaha.114.302533.

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5

Davis, George E. y Donald R. Senger. "Endothelial Extracellular Matrix". Circulation Research 97, n.º 11 (25 de noviembre de 2005): 1093–107. http://dx.doi.org/10.1161/01.res.0000191547.64391.e3.

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6

Tayebjee, Muzahir H., Robert J. MacFadyen y Gregory YH Lip. "Extracellular matrix biology". Journal of Hypertension 21, n.º 12 (diciembre de 2003): 2211–18. http://dx.doi.org/10.1097/00004872-200312000-00002.

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7

Ramirez, Francesco, Lynn Y. Sakai, Harry C. Dietz y Daniel B. Rifkin. "Fibrillin microfibrils: multipurpose extracellular networks in organismal physiology". Physiological Genomics 19, n.º 2 (4 de octubre de 2004): 151–54. http://dx.doi.org/10.1152/physiolgenomics.00092.2004.

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Organismal physiology depends significantly on the proper assembly of extracellular matrix (ECM) macroaggregates that impart structural integrity to the connective tissue. Recent genetic studies in mice have unraveled unsuspected new functions of architectural matrix components in regulating signaling events that modulate patterning, morphogenesis, and growth of several organ systems. As a result, a new paradigm has emerged whereby tissue-specific organization of the ECM dictates not only the physical properties of the connective tissue, but also the ability of the matrix to direct a broad spectrum of cellular activities through the regulation of growth factor signaling. These observations pave the way to novel therapeutic approaches aimed at counteracting the deleterious consequences of perturbations of connective tissue homeostasis.

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8

Vogel, Viola. "Unraveling the Mechanobiology of Extracellular Matrix". Annual Review of Physiology 80, n.º 1 (10 de febrero de 2018): 353–87. http://dx.doi.org/10.1146/annurev-physiol-021317-121312.

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9

Brown, Lindsay. "Cardiac extracellular matrix: a dynamic entity". American Journal of Physiology-Heart and Circulatory Physiology 289, n.º 3 (septiembre de 2005): H973—H974. http://dx.doi.org/10.1152/ajpheart.00443.2005.

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10

Ma, Zihan, Chenfeng Mao, Yiting Jia, Yi Fu y Wei Kong. "Extracellular matrix dynamics in vascular remodeling". American Journal of Physiology-Cell Physiology 319, n.º 3 (1 de septiembre de 2020): C481—C499. http://dx.doi.org/10.1152/ajpcell.00147.2020.

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Vascular remodeling is the adaptive response to various physiological and pathophysiological alterations that are closely related to aging and vascular diseases. Understanding the mechanistic regulation of vascular remodeling may be favorable for discovering potential therapeutic targets and strategies. The extracellular matrix (ECM), including matrix proteins and their degradative metalloproteases, serves as the main component of the microenvironment and exhibits dynamic changes during vascular remodeling. This process involves mainly the altered composition of matrix proteins, metalloprotease-mediated degradation, posttranslational modification of ECM proteins, and altered topographical features of the ECM. To date, adequate studies have demonstrated that ECM dynamics also play a critical role in vascular remodeling in various diseases. Here, we review these related studies, summarize how ECM dynamics control vascular remodeling, and further indicate potential diagnostic biomarkers and therapeutic targets in the ECM for corresponding vascular diseases.

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11

Gerecht, Sharon. "ANGIOGENESIS BIOMIMETIC: EXTRACELLULAR MATRIX AND OXYGEN". Free Radical Biology and Medicine 65 (noviembre de 2013): S13. http://dx.doi.org/10.1016/j.freeradbiomed.2013.10.412.

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12

Tyagi, Suresh C. "Physiology and homeostasis of extracellular matrix: cardiovascular adaptation and remodeling". Pathophysiology 7, n.º 3 (septiembre de 2000): 177–82. http://dx.doi.org/10.1016/s0928-4680(00)00046-8.

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13

Dunsmore, S. E. y D. E. Rannels. "Extracellular matrix biology in the lung". American Journal of Physiology-Lung Cellular and Molecular Physiology 270, n.º 1 (1 de enero de 1996): L3—L27. http://dx.doi.org/10.1152/ajplung.1996.270.1.l3.

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The lung and other organs are comprised of both cellular and extracellular compartments. Interaction of these components modulates physiological function at the organ, cellular, and subcellular levels. Extracellular components in the gas-exchange region of the lung include both noncellular interstitium and basement membranes. Connective tissue elements of the interstitium in part determine ventilatory function by contributions to tissue compliance and to resistance of the diffusion barrier. The basement membrane underlies cells of both the alveolar epithelium and the capillary endothelium; basement membrane components exert biological effects on adjacent cells through receptor-mediated interactions. This review emphasizes current knowledge concerning the composition and biological activity of extracellular matrix in the alveolar region of the lung. Matrix synthesis and turnover are also considered. Directions for future research are suggested in the context of current knowledge of the lung and other model systems.

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14

Luo, Xia, Lingyan Deng, Laxmi Pangeni Lamsal, Wenjuan Xu, Cheng Xiang y Liming Cheng. "AMP-Activated Protein Kinase Alleviates Extracellular Matrix Accumulation in High Glucose-Induced Renal Fibroblasts through mTOR Signaling Pathway". Cellular Physiology and Biochemistry 35, n.º 1 (2015): 191–200. http://dx.doi.org/10.1159/000369687.

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Background/Aims: Extracellular matrix accumulation contributes significantly to the pathogenesis of diabetic nephropathy. Although AMP-activated protein kinase (AMPK) has been found to inhibit extracellular matrix synthesis by experiments in vivo and vitro, its role in alleviating the deposition of extracellular matrix in renal interstitial fibroblasts has not been well defined. Methods: Currently, we conducted this study to investigate the effects of AMPK on high glucose-induced extracellular matrix synthesis and involved intracellular signaling pathway by using western blot in the kidney fibroblast cell line (NRK-49f). Results: Collagen IV protein levels were significantly increased by high glucose in a time-dependent manner. This was associated with a decrease in Thr72 phosphorylation of AMPK and an increase in phosphorylation of mTOR on Ser2448. High glucose-induced extracellular matrix accumulation and mTOR activation were significantly inhibited by the co-treatment of rAAV-AMPKα1312 (encoding constitutively active AMPKα1) whereas activated by r-AAV-AMPKα1D157A (encoding dominant negative AMPKα1). In cultured renal fibroblasts, overexpression of AMPKα1D157A upregulated mTOR signaling and matrix synthesis, which were ameliorated by co-treatment with the inhibitor of mTOR, rapamycin. Conclusion: Collectively, these findings indicate that AMPK exerts renoprotective effects by inhibiting the accumulation of extracellular matrix through mTOR signaling pathway.

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15

Stauber, W. T., P. M. Clarkson, V. K. Fritz y W. J. Evans. "Extracellular matrix disruption and pain after eccentric muscle action". Journal of Applied Physiology 69, n.º 3 (1 de septiembre de 1990): 868–74. http://dx.doi.org/10.1152/jappl.1990.69.3.868.

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Pain, stiffness, and indicators of muscle damage occur at different times after eccentric muscle action. After a single bout of maximal resisted lengthening of the elbow flexors, elbow position, pain perception, and indicators of cellular damage were measured. Immediately postexercise, a significant decrease in resting muscle length was observed that continued to 48 h. At this time, an increase in perceived muscle soreness was noted (P less than 0.05), and a biopsy of the biceps brachii revealed mast cell degranulation, separations of the extracellular matrix from myofibers, and increased plasma constituents in the extracellular space. It is proposed that myofiber disruption allows intracellular proteins to escape and extracellular proteins and ions to enter, causing swelling, whereas the disrupted extracellular matrix initiates the inflammatory response, which includes the release of mast cell granules seen at 48 h postexercise. Thus the delayed sensation of pain (soreness) after repeated eccentric muscle actions probably results from inflammation in response to extracellular matrix disruption.

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16

Arriazu, Elena, Marina Ruiz de Galarreta, Francisco Javier Cubero, Marta Varela-Rey, María Pilar Pérez de Obanos, Tung Ming Leung, Aritz Lopategi, Aitor Benedicto, Ioana Abraham-Enachescu y Natalia Nieto. "Extracellular Matrix and Liver Disease". Antioxidants & Redox Signaling 21, n.º 7 (septiembre de 2014): 1078–97. http://dx.doi.org/10.1089/ars.2013.5697.

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17

Arroyo, A. G. y M. L. Iruela-Arispe. "Extracellular matrix, inflammation, and the angiogenic response". Cardiovascular Research 86, n.º 2 (12 de febrero de 2010): 226–35. http://dx.doi.org/10.1093/cvr/cvq049.

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18

Abonnenc, Mélanie, Adam A. Nabeebaccus, Ursula Mayr, Javier Barallobre-Barreiro, Xuebin Dong, Friederike Cuello, Sumon Sur et al. "Extracellular Matrix Secretion by Cardiac Fibroblasts". Circulation Research 113, n.º 10 (25 de octubre de 2013): 1138–47. http://dx.doi.org/10.1161/circresaha.113.302400.

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19

Siefert, Suzanne A. y Rajabrata Sarkar. "Matrix metalloproteinases in vascular physiology and disease". Vascular 20, n.º 4 (agosto de 2012): 210–16. http://dx.doi.org/10.1258/vasc.2011.201202.

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Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that primarily degrade components of the extracellular matrix (ECM). Remodeling of the ECM by MMPs is important in both physiological and pathological processes, including organ generation/regeneration, angiogenesis, wound healing, inflammation and tumor growth. In the vasculature, MMPs play a role in beneficial processes such as angiogenesis, collateral artery formation and thrombus resolution. However, MMP expression is also implicated in the pathogenesis of vascular diseases such as atherosclerosis, aortic aneurysms, plaque rupture and neointimal hyperplasia after balloon angioplasty. Here, we review the structure, functions and roles of MMPs in both neovascularization and vascular pathology and discuss the potential of, and challenges that face, adapting MMPs as therapeutic targets in vascular disease.

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20

Tran, Thai y Andrew J. Halayko. "Extracellular matrix and airway smooth muscle interactions: a target for modulating airway wall remodelling and hyperresponsiveness?This article is one of a selection of papers published in the Special Issue on Recent Advances in Asthma Research." Canadian Journal of Physiology and Pharmacology 85, n.º 7 (julio de 2007): 666–71. http://dx.doi.org/10.1139/y07-050.

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The airway smooth muscle from asthmatic airways produces increased amounts and an altered composition of extracellular matrix proteins. The extracellular matrix can in turn influence the phenotype and function of airway smooth muscle cells, affecting the biochemical, geometric, and mechanical properties of the airway wall. This review provides a brief overview of the current understanding of the biology associated with airway smooth muscle interactions with the extracellular matrix. We present future directions needed for the study of cellular and molecular mechanisms that determine the outcomes of extracellular matrix – airway smooth muscle interactions, and discuss their possible importance as determinants of airway function in asthma.

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21

Forget, Marie-Annick, Richard R. Desrosiers y Richard Béliveau. "Physiological roles of matrix metalloproteinases: implications for tumor growth and metastasis". Canadian Journal of Physiology and Pharmacology 77, n.º 7 (1 de agosto de 1999): 465–80. http://dx.doi.org/10.1139/y99-055.

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Physiological processes involving remodelling of the extracellular matrix, such as wound healing, embryogenesis, angiogenesis, and the female reproductive cycle, require the activity of matrix metalloproteinases (MMPs). This group of proteases degrades basal membranes and connective tissues and plays an essential role in the homeostasis of the extracellular matrix. An imbalance in the expression or activity of MMPs can have important consequences in diseases such as multiple sclerosis, Alzheimer's disease, or the development of cancers. Because of the pathophysiological importance of MMPs, their activity is highly controlled in order to confine them to specific areas. An activation cascade, initiated by the proteolysis of plasminogen, cleaves proMMPs, and every step is controlled by specific activators or inhibitors. MMPs destabilize the organization of the extracellular matrix and influence the development of cancer by contributing to cell migration, tumor cell proliferation, and angiogenesis. Accordingly, these proteases possess an important role in cell-matrix interactions by affecting fundamental processes such as cell differentiation and proliferation. Therefore, the characterization of MMPs involved in specific types and stages of tumors will significantly improve the diagnosis and treatment of these cancers in humans.Key words: matrix metalloproteinases, physiology, cancer, cell invasion, extracellular matrix.

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22

Graham, H. K., M. Horn y A. W. Trafford. "Extracellular matrix profiles in the progression to heart failure". Acta Physiologica 194, n.º 1 (septiembre de 2008): 3–21. http://dx.doi.org/10.1111/j.1748-1716.2008.01881.x.

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23

Rodgers, Raymond. "Extracellular Matrix in the Ovary". Seminars in Reproductive Medicine 24, n.º 4 (septiembre de 2006): 193–94. http://dx.doi.org/10.1055/s-2006-948548.

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24

Krishnan, Laxminarayanan, James B. Hoying, Hoa Nguyen, Helen Song y Jeffrey A. Weiss. "Interaction of angiogenic microvessels with the extracellular matrix". American Journal of Physiology-Heart and Circulatory Physiology 293, n.º 6 (diciembre de 2007): H3650—H3658. http://dx.doi.org/10.1152/ajpheart.00772.2007.

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The extracellular matrix (ECM) plays a critical role in angiogenesis by providing biochemical and positional cues, as well as by mechanically influencing microvessel cell behavior. Considerable information is known concerning the biochemical cues relevant to angiogenesis, but less is known about the mechanical dynamics during active angiogenesis. The objective of this study was to characterize changes in the material properties of a simple angiogenic tissue before and during angiogenesis. During sprouting, there was an overall decrease in tissue stiffness followed by an increase during neovessel elongation. The fall in matrix stiffness coincided with peak matrix metalloproteinase mRNA expression and elevated proteolytic activity. An elevated expression of genes for ECM components and cell-ECM interaction molecules and a subsequent drop in proteolytic activity (although enzyme levels remained elevated) coincided with the subsequent stiffening. The results of this study show that the mechanical properties of a scaffold tissue may be actively modified during angiogenesis by the growing microvasculature.

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25

Haas, Tara L. "Endothelial cell regulation of matrix metalloproteinases". Canadian Journal of Physiology and Pharmacology 83, n.º 1 (1 de enero de 2005): 1–7. http://dx.doi.org/10.1139/y04-120.

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The process of sprouting angiogenesis requires that the endothelial cells degrade the basement membrane matrix and migrate into the interstitial matrix. Matrix metalloproteinases are enzymes capable of cleaving numerous extracellular matrix proteins. Increased production and activity of matrix metalloproteinases in any cell type is associated with a more migratory and invasive phenotype. This paper describes results of recent in-vitro studies of the regulation of transcription and activation of MMP-2 and MT1-MMP in endothelial cells, as well as studies that examined roles of matrix metalloproteinases in activity-induced angiogenesis.Key words: proteolysis, extracellular matrix, angiogenesis, mechanotransduction.

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26

Adams, Josephine Clare. "Molecular organisation of cell–matrix contacts: essential multiprotein assemblies in cell and tissue function". Expert Reviews in Molecular Medicine 4, n.º 1 (11 de febrero de 2002): 1–24. http://dx.doi.org/10.1017/s1462399402004039.

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The adhesion of cells to their surrounding extracellular matrix has vital roles in embryonic development, inflammatory responses, wound healing and adult tissue homeostasis. Cells attach to extracellular matrix by specific cell-surface receptors, of which the integrins and transmembrane proteoglycans are major representatives. The engagement of adhesion receptors triggers assembly of functional matrix contacts, in which bound matrix components, adhesion receptors and associated intracellular cytoskeletal and signalling molecules form large, localised multiprotein complexes. This review discusses the functional categories of matrix contacts, examples of the biological roles of matrix contacts in normal physiology, and examples of the ways in which abnormalities of matrix contacts are associated with major human diseases.

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27

McGowan, S. E. y R. J. Thompson. "Extracellular matrix proteoglycan degradation by human alveolar macrophages and neutrophils". Journal of Applied Physiology 66, n.º 1 (1 de enero de 1989): 400–409. http://dx.doi.org/10.1152/jappl.1989.66.1.400.

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Degradation and restructuring of the elastin fiber network of the lung is a pivotal process in the pathogenesis of emphysema. Alveolar macrophages and neutrophils are probably directly involved in elastin degradation, but they may also indirectly influence elastin structure and function by altering other extracellular matrix components such as proteoglycans. In this study the mechanisms of proteoglycan degradation by human alveolar macrophages and neutrophils have been explored. Macrophages appear to utilize plasminogen in solubilizing 35SO4-labeled proteoglycans in extracellular matrix produced by neonatal rat vascular smooth muscle cells. Proteoglycan degradation by macrophages is significantly augmented in the presence of 1% human serum. In contrast, neutrophils apparently utilize intrinsic proteinases to solubilize extracellular matrix proteoglycans, and serum inhibits proteoglycan degradation by these cells. Persistent inflammation in the terminal airways of cigarette smokers may produce proteoglycan degradation and influence elastin fiber architecture where the earliest physiological and anatomic evidence of emphysema appears.

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28

Ito, Akira, Tomoki Aoyama, Hirotaka Iijima, Momoko Nagai, Shoki Yamaguchi, Junichi Tajino, Xiangkai Zhang, Haruhiko Akiyama y Hiroshi Kuroki. "Optimum temperature for extracellular matrix production by articular chondrocytes". International Journal of Hyperthermia 30, n.º 2 (5 de febrero de 2014): 96–101. http://dx.doi.org/10.3109/02656736.2014.880857.

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29

de Haas, Hans J., Eloisa Arbustini, Valentin Fuster, Christopher M. Kramer y Jagat Narula. "Molecular Imaging of the Cardiac Extracellular Matrix". Circulation Research 114, n.º 5 (28 de febrero de 2014): 903–15. http://dx.doi.org/10.1161/circresaha.113.302680.

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30

Andreeva, E. R. y D. K. Matveeva. "Multipotent Mesenchymal Stromal Cells and Extracellular Matrix: Regulation under Hypoxia". Human Physiology 44, n.º 6 (noviembre de 2018): 696–705. http://dx.doi.org/10.1134/s0362119718060038.

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31

Kennett, Eleanor C. y Michael J. Davies. "Degradation of extracellular matrix by peroxynitrite/peroxynitrous acid". Free Radical Biology and Medicine 45, n.º 5 (septiembre de 2008): 716–25. http://dx.doi.org/10.1016/j.freeradbiomed.2008.05.027.

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32

Borojevic, R. "Extracellular matrix: understanding the complexity". Brazilian Journal of Medical and Biological Research 32, n.º 5 (mayo de 1999): 497–99. http://dx.doi.org/10.1590/s0100-879x1999000500001.

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33

Stauber, W. T., V. K. Fritz, T. E. Burkovskaya y E. I. Ilyina-Kakueva. "Effect of spaceflight on the extracellular matrix of skeletal muscle after a crush injury". Journal of Applied Physiology 73, n.º 2 (1 de agosto de 1992): S74—S81. http://dx.doi.org/10.1152/jappl.1992.73.2.s74.

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The organization and composition of the extracellular matrix were studied in the crush-injured gastrocnemius muscle of rats subjected to 0 G. After 14 days of flight on COSMOS 2044, the gastrocnemius muscle was removed and evaluated by histochemical and immunohistochemical techniques from the five injured flight rodents and various Earth-based treatment groups. In general, the repair process was similar in all injured muscle samples with regard to the organization of the extracellular matrix and myofibers. Small and large myofibers were present within an expanded extracellular matrix, indicative of myogenesis and muscle regeneration. In the tail-suspended animals, a more complete repair was observed with no enlarged area of nonmuscle cells or matrix material visible. In contrast, the muscle samples from the flight animals were less well organized and contained more macrophages and blood vessels in the repair region, indicative of a delayed repair process, but did not demonstrate any chronic inflammation. Myofiber repair did vary in muscles from the different groups, being slowest in the flight animals and most complete in the tail-suspended ones.

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34

Syková, Eva y Charles Nicholson. "Diffusion in Brain Extracellular Space". Physiological Reviews 88, n.º 4 (octubre de 2008): 1277–340. http://dx.doi.org/10.1152/physrev.00027.2007.

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Diffusion in the extracellular space (ECS) of the brain is constrained by the volume fraction and the tortuosity and a modified diffusion equation represents the transport behavior of many molecules in the brain. Deviations from the equation reveal loss of molecules across the blood-brain barrier, through cellular uptake, binding, or other mechanisms. Early diffusion measurements used radiolabeled sucrose and other tracers. Presently, the real-time iontophoresis (RTI) method is employed for small ions and the integrative optical imaging (IOI) method for fluorescent macromolecules, including dextrans or proteins. Theoretical models and simulations of the ECS have explored the influence of ECS geometry, effects of dead-space microdomains, extracellular matrix, and interaction of macromolecules with ECS channels. Extensive experimental studies with the RTI method employing the cation tetramethylammonium (TMA) in normal brain tissue show that the volume fraction of the ECS typically is ∼20% and the tortuosity is ∼1.6 (i.e., free diffusion coefficient of TMA is reduced by 2.6), although there are regional variations. These parameters change during development and aging. Diffusion properties have been characterized in several interventions, including brain stimulation, osmotic challenge, and knockout of extracellular matrix components. Measurements have also been made during ischemia, in models of Alzheimer's and Parkinson's diseases, and in human gliomas. Overall, these studies improve our conception of ECS structure and the roles of glia and extracellular matrix in modulating the ECS microenvironment. Knowledge of ECS diffusion properties is valuable in contexts ranging from understanding extrasynaptic volume transmission to the development of paradigms for drug delivery to the brain.

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35

Bijian, Krikor, Tomoko Takano, Joan Papillon, Abdelkrim Khadir y Andrey V. Cybulsky. "Extracellular matrix regulates glomerular epithelial cell survival and proliferation". American Journal of Physiology-Renal Physiology 286, n.º 2 (febrero de 2004): F255—F266. http://dx.doi.org/10.1152/ajprenal.00259.2003.

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Glomerular epithelial cell (GEC) injury and apoptosis may contribute to sclerosis in glomerulonephritis. The present study addresses signals that regulate survival of GEC in culture and in the acute puromycin aminonucleoside nephrosis (PAN) model of GEC injury in vivo. Compared with GEC on plastic substratum, adhesion to collagen increased activation of focal adhesion kinase (FAK), c-Src, and ERK and facilitated survival (prevented apoptosis). GEC on plastic exhibited increased caspase-8 and -9 activities, increased expression of the proapoptotic protein, Bax, and decreased the antiapoptotic protein, Bcl-XL, compared with collagen. Stable expression of constitutively active mutants of FAK (CD2-FAK) or MEK (R4F-MEK) activated the ERK pathway and supplanted the requirement of collagen for survival. In contrast, expression of a Ras mutant that activates phosphatidylinositol 3-kinase but blocks ERK activation or pharmacological inhibition of the ERK pathway decreased survival on collagen. Glomeruli isolated from rats with PAN revealed increased β1-integrin expression, along with increased activation of FAK, c-Src, and ERK, compared with controls. EGF receptor activation was undetectable in PAN. Therefore, adhesion to collagen, resulting in activation of FAK and the Ras-ERK pathway, supports GEC survival. Analogous signals for GEC survival are activated in PAN.

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36

Bruggeman, L. A., E. A. Horigan, S. Horikoshi, P. E. Ray y P. E. Klotman. "Thromboxane stimulates synthesis of extracellular matrix proteins in vitro". American Journal of Physiology-Renal Physiology 261, n.º 3 (1 de septiembre de 1991): F488—F494. http://dx.doi.org/10.1152/ajprenal.1991.261.3.f488.

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The vasoconstrictor eicosanoid thromboxane plays an important role in the pathogenesis of several renal diseases. As an autacoid, its local release alters blood flow and induces platelet aggregation. We report a direct stimulatory effect of thromboxane on extracellular matrix protein production and gene expression in vitro. Treatment of two cell types, differentiated mouse teratocarcinoma cells (F9+) and human glomerular mesangial cells, with two different thromboxane analogues resulted in increased production of components of the extracellular matrix including fibronectin and the basement membrane proteins laminin and type IV collagen. These responses to thromboxane were not the result of a mitogenic effect of thromboxane nor the result of an increase in total cellular protein. The increased production of extracellular matrix proteins was, at least in part, due to an increase in the steady-state level of mRNA for these genes. Furthermore, the effect of thromboxane was markedly inhibited by cotreatment with a thromboxane-receptor antagonist. These results suggest a new potential role for thromboxane as a mediator of the sclerotic and fibrotic responses to injury.

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37

Savino, Wilson y Joseli Lannes Vieira. "Is there a role for extracellular matrix in thymus physiology and pathology?" Memórias do Instituto Oswaldo Cruz 86, suppl 3 (1991): 91–97. http://dx.doi.org/10.1590/s0074-02761991000700013.

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38

Astudillo, Pablo. "Extracellular matrix stiffness and Wnt/β-catenin signaling in physiology and disease". Biochemical Society Transactions 48, n.º 3 (15 de mayo de 2020): 1187–98. http://dx.doi.org/10.1042/bst20200026.

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The Wnt/β-catenin signaling pathway plays fundamental roles during development, stem cell differentiation, and homeostasis, and its abnormal activation can lead to diseases. In recent years, it has become clear that this pathway integrates signals not only from Wnt ligands but also from other proteins and signaling routes. For instance, Wnt/β-catenin signaling involves YAP and TAZ, which are transcription factors with crucial roles in mechanotransduction. On the other hand, Wnt/β-catenin signaling is also modulated by integrins. Therefore, mechanical signals might similarly modulate the Wnt/β-catenin pathway. However, and despite the relevance that mechanosensitive Wnt/β-catenin signaling might have during physiology and diseases such as cancer, the role of mechanical cues on Wnt/β-catenin signaling has received less attention. This review aims to summarize recent evidence regarding the modulation of the Wnt/β-catenin signaling by a specific type of mechanical signal, the stiffness of the extracellular matrix. The review shows that mechanical stiffness can indeed modulate this pathway in several cell types, through differential expression of Wnt ligands, receptors and inhibitors, as well as by modulating β-catenin levels. However, the specific mechanisms are yet to be fully elucidated.

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39

Schmidt, Roland, Andreas Bültmann, Martin Ungerer, Nader Joghetaei, Özgür Bülbül, Sven Thieme, Triantafyllos Chavakis et al. "Extracellular Matrix Metalloproteinase Inducer Regulates Matrix Metalloproteinase Activity in Cardiovascular Cells". Circulation 113, n.º 6 (14 de febrero de 2006): 834–41. http://dx.doi.org/10.1161/circulationaha.105.568162.

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40

Zou, Huan, Rongdi Yuan, Qijun Zheng, Yan Huo, Min Lang, Shuxing Ji, Zheng Zheng y Jian Ye. "Fluctuations in Intraocular Pressure Increase the Trabecular Meshwork Extracellular Matrix". Cellular Physiology and Biochemistry 33, n.º 4 (2014): 1215–24. http://dx.doi.org/10.1159/000358691.

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41

Casals, Gregori, Guillermo Fernández-Varo, Pedro Melgar-Lesmes, Santi Marfà, Vedrana Reichenbach, Manuel Morales-Ruiz y Wladimiro Jiménez. "Factors Involved in Extracellular Matrix Turnover in Human Derived Cardiomyocytes". Cellular Physiology and Biochemistry 32, n.º 5 (2013): 1125–36. http://dx.doi.org/10.1159/000354513.

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42

McGee, Maria P., Michael J. Morykwas, James E. Jordan, Rui Wang y Louis C. Argenta. "Local fluid transfer regulation in heart extracellular matrix". Journal of Physiology and Biochemistry 72, n.º 2 (9 de marzo de 2016): 255–68. http://dx.doi.org/10.1007/s13105-016-0473-9.

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43

Coffey, Elizabeth C., Mary Astumian, Sarah S. Alrowaished, Claire Schaffer y Clarissa A. Henry. "Lysosomal Function Impacts the Skeletal Muscle Extracellular Matrix". Journal of Developmental Biology 9, n.º 4 (23 de noviembre de 2021): 52. http://dx.doi.org/10.3390/jdb9040052.

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Muscle development and homeostasis are critical for normal muscle function. A key aspect of muscle physiology during development, growth, and homeostasis is modulation of protein turnover, the balance between synthesis and degradation of muscle proteins. Protein degradation depends upon lysosomal pH, generated and maintained by proton pumps. Sphingolipid transporter 1 (spns1), a highly conserved gene encoding a putative late endosome/lysosome carbohydrate/H+ symporter, plays a pivotal role in maintaining optimal lysosomal pH and spns1−/− mutants undergo premature senescence. However, the impact of dysregulated lysosomal pH on muscle development and homeostasis is not well understood. We found that muscle development proceeds normally in spns1−/− mutants prior to the onset of muscle degeneration. Dysregulation of the extracellular matrix (ECM) at the myotendinous junction (MTJ) coincided with the onset of muscle degeneration in spns1−/− mutants. Expression of the ECM proteins laminin 111 and MMP-9 was upregulated. Upregulation of laminin 111 mitigated the severity of muscle degeneration, as inhibition of adhesion to laminin 111 exacerbated muscle degeneration in spns1−/− mutants. MMP-9 upregulation was induced by tnfsf12 signaling, but abrogation of MMP-9 did not impact muscle degeneration in spns1−/− mutants. Taken together, these data indicate that dysregulated lysosomal pH impacts expression of ECM proteins at the myotendinous junction.

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44

Yen, Chung-Jen, Cheng-Chung Fang, Yung-Ming Chen, Rong-Hwa Lin, Kwan-Dun Wu, Po-Huang Lee y Tun-Jun Tsai. "Extracellular Matrix Proteins Modulate Human Peritoneal Mesothelial Cell Behavior". Nephron 75, n.º 2 (1997): 188–95. http://dx.doi.org/10.1159/000189530.

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45

Freitas, Ana, Miguel Aroso, António Barros, Miriam Fernández, Eduardo Conde-Sousa, Marina Leite, Eva Daniela Carvalho et al. "Characterization of the Striatal Extracellular Matrix in a Mouse Model of Parkinson’s Disease". Antioxidants 10, n.º 7 (8 de julio de 2021): 1095. http://dx.doi.org/10.3390/antiox10071095.

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Parkinson’s disease’s etiology is unknown, although evidence suggests the involvement of oxidative modifications of intracellular components in disease pathobiology. Despite the known involvement of the extracellular matrix in physiology and disease, the influence of oxidative stress on the matrix has been neglected. The chemical modifications that might accumulate in matrix components due to their long half-live and the low amount of extracellular antioxidants could also contribute to the disease and explain ineffective cellular therapies. The enriched striatal extracellular matrix from a mouse model of Parkinson’s disease was characterized by Raman spectroscopy. We found a matrix fingerprint of increased oxalate content and oxidative modifications. To uncover the effects of these changes on brain cells, we morphologically characterized the primary microglia used to repopulate this matrix and further quantified the effects on cellular mechanical stress by an intracellular fluorescence resonance energy transfer (FRET)-mechanosensor using the U-2 OS cell line. Our data suggest changes in microglia survival and morphology, and a decrease in cytoskeletal tension in response to the modified matrix from both hemispheres of 6-hydroxydopamine (6-OHDA)-lesioned animals. Collectively, these data suggest that the extracellular matrix is modified, and underscore the need for its thorough investigation, which may reveal new ways to improve therapies or may even reveal new therapies.

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46

Penberthy, T. W., Y. Jiang, F. W. Luscinskas y D. T. Graves. "MCP-1-stimulated monocytes preferentially utilize beta 2-integrins to migrate on laminin and fibronectin". American Journal of Physiology-Cell Physiology 269, n.º 1 (1 de julio de 1995): C60—C68. http://dx.doi.org/10.1152/ajpcell.1995.269.1.c60.

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Recruitment of monocytes to inflammatory sites involves a series of sequential attachments and detachments to extracellular matrix proteins in response to a chemoattractant gradient. In this study we compared the migration of human peripheral blood monocytes on different extracellular matrix proteins in response to monocyte chemoattractant protein-1 (MCP-1) and N-formylmethionyl-leucyl-phenylalanine. Monocytes migrated more effectively on laminin compared with other extracellular matrix proteins. In contrast, this preference was not observed with neutrophils, suggesting that the monocytes and neutrophils may have differences in their migration on extracellular matrix proteins. To study this further, function-blocking monoclonal antibodies were used to examine mechanistically whether beta 1- and beta 2-integrins were involved in monocyte migration on fibronectin or laminin in response to MCP-1. Monocyte migration on both laminin and fibronectin was blocked 100% (P < 0.05) by intact monoclonal antibody, F(ab') fragments, and F(ab')2 fragments to beta 2-integrins. We also determined that antibodies to beta 2-integrins block monocyte migration that has already been initiated. In contrast, antibody to the beta 1-integrins inhibited monocyte migration by approximately 40% (P < 0.05). Thus monocytes that express both beta 1- and beta 2-integrins require utilization of beta 2-integrins in migration on extracellular matrix proteins. The results also suggest that beta 1-integrins facilitate monocyte migration but that monocyte migration is not absolutely dependent on the interaction of beta 1-integrins with extracellular matrix proteins. In contrast, neutrophil migration is beta 2-integrin dependent and is not facilitated by beta 1-integrins.

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47

Fissell, William H., Christina L. Hofmann, Nicholas Ferrell, Lisa Schnell, Anna Dubnisheva, Andrew L. Zydney, Peter D. Yurchenco y Shuvo Roy. "Solute partitioning and filtration by extracellular matrices". American Journal of Physiology-Renal Physiology 297, n.º 4 (octubre de 2009): F1092—F1100. http://dx.doi.org/10.1152/ajprenal.00162.2009.

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The physiology of glomerular filtration remains mechanistically obscure despite its importance in disease. The correspondence between proteinuria and foot process effacement suggests podocytes as the locus of the filtration barrier. If so, retained macromolecules ought to accumulate at the filtration barrier, an effect called concentration polarization. Literature data indicate macromolecule concentrations decrease from subendothelial to subepithelial glomerular basement membrane (GBM), as would be expected if the GBM were itself the filter. The objective of this study was to obtain insights into the possible role of the GBM in protein retention by performing fundamental experimental and theoretical studies on the properties of three model gels. Solute partitioning and filtration through thin gels of a commercially available laminin-rich extracellular matrix, Matrigel, were measured using a polydisperse polysaccharide tracer molecule, Ficoll 70. Solute partitioning into laminin gels and lens basement membrane (LBM) were measured using Ficoll 70. A novel model of a laminin gel was numerically simulated, as well as a mixed structure-random-fiber model for LBM. Experimental partitioning was predicted by numerical simulations. Sieving coefficients through thin gels of Matrigel were size dependent and strongly flux dependent. The observed flux dependence arose from compression of the gel in response to the applied pressure. Gel compression may alter solute partitioning into extracellular matrix at physiologic pressures present in the glomerular capillary. This suggests a physical mechanism coupling podocyte structure to permeability characteristics of the GBM.

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48

Aicher, Brittany O., Jackie Zhang, Selen C. Muratoglu, Rebeca Galisteo, Allison L. Arai, Vicki L. Gray, Brajesh K. Lal, Dudley K. Strickland y Areck A. Ucuzian. "Moderate aerobic exercise prevents matrix degradation and death in a mouse model of aortic dissection and aneurysm". American Journal of Physiology-Heart and Circulatory Physiology 320, n.º 5 (1 de mayo de 2021): H1786—H1801. http://dx.doi.org/10.1152/ajpheart.00229.2020.

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Moderate aerobic exercise was shown to significantly reduce mortality, extracellular matrix degradation, and thoracic aortic aneurysm and dissection formation associated with lysyl oxidase inhibition in a mouse model. Gene expression suggested a reversal of TGF-β, inflammation, and extracellular matrix remodeling pathway dysregulation, along with augmented elastogenesis with exercise.

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49

Irving-Rodgers, Helen, Jan Roger, Martin Luck y Raymond Rodgers. "Extracellular Matrix of the Corpus Luteum". Seminars in Reproductive Medicine 24, n.º 4 (septiembre de 2006): 242–50. http://dx.doi.org/10.1055/s-2006-948553.

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50

Berkholtz, Courtney, Lonnie Shea y Teresa Woodruff. "Extracellular Matrix Functions in Follicle Maturation". Seminars in Reproductive Medicine 24, n.º 4 (septiembre de 2006): 262–69. http://dx.doi.org/10.1055/s-2006-948555.

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