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Journal articles on the topic 'Matrice de collagène'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Van der Rest, M. "Biologie du collagène et maladies héréditaires de la matrice extracellulaire." médecine/sciences 3, no. 7 (1987): 411. http://dx.doi.org/10.4267/10608/3707.

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2

Gonçalves-Neto, Joaquim, S. S. Witzel, W. R. Teodoro, A. E. Carvaho-Junior, T. D. Fernandes, and N. H. Yoshinari. "Modifications de la composition de la matrice de collagène dans les tendinopathies du jambier postérieur." Revue du Rhumatisme 69, no. 3 (2002): 280–85. http://dx.doi.org/10.1016/s1169-8330(02)00286-7.

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3

Grosjean, Guillaume, Frédéric Sailhan, Mohamed Mezghani, and Jean-Pierre Courpied. "82 Efficacité de la rh-BMP-7/matrice collagène (OP-1) dans la consolidation des pseudarthroses post-fracturaires." Revue de Chirurgie Orthopédique et Réparatrice de l'Appareil Moteur 93, no. 7 (2007): 67. http://dx.doi.org/10.1016/s0035-1040(07)79455-2.

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4

Idoux, Romane, Sandrine Bretaud, Christine Berthier, Vincent Jacquemond, Florence Ruggiero, and Bruno Allard. "Étude physiopathologique de la myopathie de Bethlem à l’aide d’un modèle de poisson zèbre." médecine/sciences 35 (November 2019): 39–42. http://dx.doi.org/10.1051/medsci/2019182.

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La myopathie de Bethlem (BM) est une maladie caractérisée par des rétractions et une faiblesse musculaires. Cette pathologie résulte de mutations dans un des gènes codant l’une des trois chaînes α du collagène VI (COLVI), un composant de la matrice extracellulaire musculaire squelettique. Aujourd’hui, une question non résolue est de comprendre comment l’altération de COLVI présent à l’extérieur des cellules musculaires conduit à des modifications fonctionnelles dans les fibres musculaires. Le modèle poisson zèbre col6a1Δex14 est actuellement un modèle animal unique de la BM puisqu’il est le se

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5

Goldberg, A. J., D. A. Lee, D. L. Bader, and G. Bentley. "Un facteur de croissance durant la période de culture pourrait normaliser les capacités de synthèse (matrice et collagène) des chondrocytes autologues transplantés." Revue de Chirurgie Orthopédique et Réparatrice de l'Appareil Moteur 92, no. 7 (2006): 730. http://dx.doi.org/10.1016/s0035-1040(06)77669-3.

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6

PASTOUREAU, P. "Physiologie du développement du tissu osseux." INRAE Productions Animales 3, no. 4 (1990): 265–73. http://dx.doi.org/10.20870/productions-animales.1990.3.4.4385.

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Le tissu osseux est un tissu conjonctif qui a la particularité de se minéraliser. Ceci confère à l’os ses propriétés de banque minérale et de soutien mécanique de l’organisme. De son bon développement dépend celui de tous les autres tissus. Il est ainsi mis en place très tôt au cours de la période foetale et reste sous étroit contrôle, notamment endocrinien (GH et IGF-1), pendant toute la croissance mais aussi chez l’adulte dont le tissu osseux est le siège d’un remodelage permanent. La physiologie du développement du tissu osseux est bien connue, en particulier lorsqu’elle concerne l’ostéogen

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7

Atlan, M., M. Naouri, G. Lorette, E. Estève, and G. Zakine. "Traitement original des callosités plantaires douloureuses constitutionnelles par exérèse, matrice de collagène et d’élastine (MatriDerm®) et greffe de peau mince en un temps, associée à une thérapie par pression négative." Annales de Chirurgie Plastique Esthétique 56, no. 2 (2011): 163–69. http://dx.doi.org/10.1016/j.anplas.2009.11.013.

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8

Musiime, Moses, Joan Chang, Uwe Hansen, Karl E. Kadler, Cédric Zeltz, and Donald Gullberg. "Collagen Assembly at the Cell Surface: Dogmas Revisited." Cells 10, no. 3 (2021): 662. http://dx.doi.org/10.3390/cells10030662.

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With the increased awareness about the importance of the composition, organization, and stiffness of the extracellular matrix (ECM) for tissue homeostasis, there is a renewed need to understand the details of how cells recognize, assemble and remodel the ECM during dynamic tissue reorganization events. Fibronectin (FN) and fibrillar collagens are major proteins in the ECM of interstitial matrices. Whereas FN is abundant in cell culture studies, it is often only transiently expressed in the acute phase of wound healing and tissue regeneration, by contrast fibrillar collagens form a persistent r

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9

Koide, Takaki. "Designed triple-helical peptides as tools for collagen biochemistry and matrix engineering." Philosophical Transactions of the Royal Society B: Biological Sciences 362, no. 1484 (2007): 1281–91. http://dx.doi.org/10.1098/rstb.2007.2115.

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Collagens, characterized by a unique triple-helical structure, are the predominant component of extracellular matrices (ECMs) existing in all multicellular animals. Collagens not only maintain structural integrity of tissues and organs, but also regulate a number of biological events, including cell attachment, migration and differentiation, tissue regeneration and animal development. The specific functions of collagens are generally triggered by specific interactions of collagen-binding molecules (membrane receptors, soluble factors and other ECM components) with certain structures displayed

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10

Lee, Jung-Seok, Goran Mitulović, Layla Panahipour, and Reinhard Gruber. "Proteomic Analysis of Porcine-Derived Collagen Membrane and Matrix." Materials 13, no. 22 (2020): 5187. http://dx.doi.org/10.3390/ma13225187.

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Collagen membranes and matrices being widely used in guided bone regeneration and soft tissue augmentation have characteristic properties based on their composition. The respective proteomic signatures have not been identified. Here, we performed a high-resolution shotgun proteomic analysis on two porcine collagen-based biomaterials designed for guided bone regeneration and soft tissue augmentation. Three lots each of a porcine-derived collagen membrane and a matrix derived from peritoneum and/or skin were digested and separated by nano-reverse-phase high-performance liquid chromatography. The

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11

Zou, Chao, Wen Jian Weng, Xu Liang Deng, et al. "Influence of Collagen Status on Microstructures of Porous Collagen/TCP Composites." Key Engineering Materials 330-332 (February 2007): 495–98. http://dx.doi.org/10.4028/www.scientific.net/kem.330-332.495.

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Two starting collagens, sponge and floc collagen, were used to prepare collagen/tricalcium phosphate (TCP) composites. The resulting composites were porous and had 200μm pore size. However, there was a difference in the microstructure of the pore walls for the composites derived from the two collagens, the pore walls in sponge collagen/TCP composite were still porous and had 200 nm micropores size, TCP particles were trapped in collagen matrices. While floc collagen/TCP composite had smooth and dense walls in which TCP particles were embedded. The difference could be attributed to the starting

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12

Keene, Douglas R., and Sara F. Tufa. "Strategies For Immunodissection Of The Connective Tissue Matrix And Basement Membranes." Microscopy and Microanalysis 5, S2 (1999): 1222–23. http://dx.doi.org/10.1017/s1431927600019437.

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Connective tissue matrices are quite diversified and include that composing skin, tendon, bone, cartilage, cornea and many others. The main component of the connective tissue matrix is collagen, composing approximately 70% of the dry weight of the human body. More members of the collagen family are discovered each year, with over twenty types described to date. Many of these collagens are tissue specific. In addition to the collagens, the connective tissue matrix is also the residence of epithelial and endothelial basement membranes and many other molecules including a variety of proteoglycans

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13

Rosenblum, N. D., D. M. Briscoe, M. J. Karnovsky, and B. R. Olsen. "Alpha 1-VIII collagen is expressed in the rat glomerulus and in resident glomerular cells." American Journal of Physiology-Renal Physiology 264, no. 6 (1993): F1003—F1010. http://dx.doi.org/10.1152/ajprenal.1993.264.6.f1003.

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Current knowledge regarding the molecular composition of extracellular matrices in the glomerulus does not explain how these components interact to form stable three-dimensional structures. The recent recognition that short-chain collagens such as type VIII collagen function as molecular bridges in some nonrenal tissues has raised the possibility that such molecules may serve a similar function in the glomerulus. We have recently shown that cultured rat mesangial cells synthesize and secrete several short-chain collagenous proteins, one of which has properties similar to alpha 1-VIII collagen.

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Patil, Vaidehi A., and Kristyn S. Masters. "Engineered Collagen Matrices." Bioengineering 7, no. 4 (2020): 163. http://dx.doi.org/10.3390/bioengineering7040163.

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Collagen is the most abundant protein in mammals, accounting for approximately one-third of the total protein in the human body. Thus, it is a logical choice for the creation of biomimetic environments, and there is a long history of using collagen matrices for various tissue engineering applications. However, from a biomaterial perspective, the use of collagen-only scaffolds is associated with many challenges. Namely, the mechanical properties of collagen matrices can be difficult to tune across a wide range of values, and collagen itself is not highly amenable to direct chemical modification

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15

Itoh, Yoshifumi, Noriko Ito, Hideaki Nagase, Richard D. Evans, Sarah A. Bird, and Motoharu Seiki. "Cell Surface Collagenolysis Requires Homodimerization of the Membrane-bound Collagenase MT1-MMP." Molecular Biology of the Cell 17, no. 12 (2006): 5390–99. http://dx.doi.org/10.1091/mbc.e06-08-0740.

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Pericellular degradation of interstitial collagens is a crucial event for cells to migrate through the dense connective tissue matrices, where collagens exist as insoluble fibers. A key proteinase that participates in this process is considered to be membrane-type 1 matrix metalloproteinase (MT1-MMP or MMP-14), but little is known about the mechanism by which it cleaves the insoluble collagen. Here we report that homodimerization of MT1-MMP through its hemopexin (Hpx) domain is essential for cleaving type I collagen fibers at the cell surface. When dimerization was blocked by coexpressing eith

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16

Nakanishi, Y., H. Nogawa, Y. Hashimoto, J. Kishi, and T. Hayakawa. "Accumulation of collagen III at the cleft points of developing mouse submandibular epithelium." Development 104, no. 1 (1988): 51–59. http://dx.doi.org/10.1242/dev.104.1.51.

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The distribution of collagens I, III, IV and V was studied by immunoperoxidase staining of early developing mouse submandibular glands. Collagen I was always present in the extracellular matrices of the mesenchyme and at the epithelial-mesenchymal interfaces of the 12-day gland with no clefts and of the 13-day gland with a few definite clefts. Collagen III was found in a similar fashion to that of collagen I in the mesenchyme, but the distribution at the epithelial-mesenchymal interfaces was very different. In the mid 12-day gland with a round lobule, collagen III was distributed at every slig

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17

Shitomi, Yasuyuki, Ida B. Thøgersen, Noriko Ito, Birgit Leitinger, Jan J. Enghild, and Yoshifumi Itoh. "ADAM10 controls collagen signaling and cell migration on collagen by shedding the ectodomain of discoidin domain receptor 1 (DDR1)." Molecular Biology of the Cell 26, no. 4 (2015): 659–73. http://dx.doi.org/10.1091/mbc.e14-10-1463.

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Discoidin domain receptor 1 (DDR1) is a receptor tyrosine kinase that binds and transmits signals from various collagens in epithelial cells. However, how DDR1–dependent signaling is regulated has not been understood. Here we report that collagen binding induces ADAM10-dependent ectodomain shedding of DDR1. DDR1 shedding is not a result of an activation of its signaling pathway, since DDR1 mutants defective in signaling were shed in an efficient manner. DDR1 and ADAM10 were found to be in a complex on the cell surface, but shedding did not occur unless collagen bound to DDR1. Using a shedding-

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18

Pozzi, Ambra, Kishore K. Wary, Filippo G. Giancotti та Humphrey A. Gardner. "Integrin α1β1 Mediates a Unique Collagen-dependent Proliferation Pathway In Vivo". Journal of Cell Biology 142, № 2 (1998): 587–94. http://dx.doi.org/10.1083/jcb.142.2.587.

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Activation of integrins upon binding to extracellular matrix proteins is believed to be a crucial step for the regulation of cell survival and proliferation. We have used integrin α1-null mice to investigate the role of this collagen receptor in the regulation of cell growth and survival in vivo. α1-deficient animals, which are viable and fertile, have a hypocellular dermis and a deficiency in dermal fibroblast proliferation as embryos. In vitro analysis of α1-null embryonic fibroblasts has revealed that their proliferation rate is markedly reduced when plated on collagenous substrata, despite

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19

Reddi, A. H. "Morphogenetic messages are in the extracellular matrix: biotechnology from bench to bedside." Biochemical Society Transactions 28, no. 4 (2000): 345–49. http://dx.doi.org/10.1042/bst0280345.

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The origin and evolution of multicellular metazoa was accompanied by the appearance of extracellular matrix. The demineralized extracellular matrix of bone is enriched in morphogenetic proteins that induce bone. Bone morphogenetic proteins (BMPs) are intimately bound to collagens. BMP-4 has high affinity for type-IV collagen, and other binding proteins such as noggin and chordin. Soluble morphogens are kept in the solid state by extracellular matrix. In this sense Nature used the principles of affinity matrices long before humans patented the principle of affinity chromatography.

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20

Kirkham, J. "Collagen and dental matrices." Journal of Dentistry 20, no. 3 (1992): 182. http://dx.doi.org/10.1016/0300-5712(92)90134-x.

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21

Weidmann, J., M. Freund, and B. McGeever. "Ultrastructure of cultured endometrial epithelial cells grown on two extracellular matrices." Proceedings, annual meeting, Electron Microscopy Society of America 45 (August 1987): 960–61. http://dx.doi.org/10.1017/s0424820100129085.

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Extracellular matrices (EMSA) have been used in tissue culture to mimic the in vivo growth of cells. ECMS have been made by investigators using collagen extraction procedures and now are commercially available either in pre-coated labware or as a liquid which can be poured to variable depths over the culture surface. Common constituents in all are the basement membrane collagens, laminin, and other minor proteoglycans. Cells grown on these matrices are thought to attach at a greater rate, have increased longevity, and mimic the in vivo characteristics. Endometrial epithelial cells were culture

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22

Miron-Mendoza, Miguel, Joachim Seemann, and Frederick Grinnell. "Collagen Fibril Flow and Tissue Translocation Coupled to Fibroblast Migration in 3D Collagen Matrices." Molecular Biology of the Cell 19, no. 5 (2008): 2051–58. http://dx.doi.org/10.1091/mbc.e07-09-0930.

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In nested collagen matrices, human fibroblasts migrate from cell-containing dermal equivalents into surrounding cell-free outer matrices. Time-lapse microscopy showed that in addition to cell migration, collagen fibril flow occurred in the outer matrix toward the interface with the dermal equivalent. Features of this flow suggested that it depends on the same cell motile machinery that normally results in cell migration. Collagen fibril flow was capable of producing large-scale tissue translocation as shown by closure of a ∼1-mm gap between paired dermal equivalents in floating, nested collage

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23

Zambrano, Maria C., Anastasia A. Beklemisheva, Anton V. Bryksin, Stuart A. Newman, and Felipe C. Cabello. "Borrelia burgdorferi Binds to, Invades, and Colonizes Native Type I Collagen Lattices." Infection and Immunity 72, no. 6 (2004): 3138–46. http://dx.doi.org/10.1128/iai.72.6.3138-3146.2004.

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ABSTRACT Borrelia burgdorferi binds strongly to the extracellular matrix and cells of the connective tissue, a binding apparently mediated by specific proteins and proteoglycans. We investigated the interactions between B. burgdorferi cells and intact type I collagen using hydrated lattices that reproduce features of in vivo collagen matrices. B. burgdorferi cells of several strains adhered avidly to these acellular matrices by a mechanism that was not mediated by decorin or other proteoglycans. Moreover, following adhesion to these matrices, B. burgdorferi grew and formed microcolonies. The c

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Varedi, M., E. E. Tredget, A. Ghahary та P. G. Scott. "Stress-relaxation and contraction of a collagen matrix induces expression of TGF-β and triggers apoptosis in dermal fibroblasts". Biochemistry and Cell Biology 78, № 4 (2000): 427–36. http://dx.doi.org/10.1139/o00-014.

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Extracellular matrix serves as a scaffold for cells and can also regulate gene expression and ultimately cell behaviour. In this study, we compared the effects of three forms of type I collagen matrix, which differed only in their mechanical properties, and plastic on the expression of transforming growth factor-β1 (TGF-β1), matrix metalloproteinase-1 (collagenase), and type I collagen and on the growth and survival of human dermal fibroblasts. These effects were correlated with alterations in cell morphology and organization of intracellular actin. Cells in detached or stress-relaxed matrices

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25

Rosenblum, N. D., M. J. Karnovsky, and B. R. Olsen. "Non-fibrillar collagenous proteins synthesized by rat mesangial cells." Journal of the American Society of Nephrology 1, no. 5 (1990): 785–91. http://dx.doi.org/10.1681/asn.v15785.

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Recent studies have shown that nonrenal extracellular matrices are composed of collagenous proteins with properties that are different from those of fibrillar collagens and type IV collagen. The structures of these newly described collagens suggest that they may provide connections between specific matrix molecules and, in so doing, partially determine the three-dimensional structure of the matrix. The molecular composition and organization of normal and diseased mesangial matrix are incompletely understood. As a means to further understand the structure of the mesangial matrix, we have furthe

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Serna-Márquez, Nathalia, Adriana Rodríguez-Hernández, Marisol Ayala-Reyes, et al. "Fibrillar Collagen Type I Participates in the Survival and Aggregation of Primary Hepatocytes Cultured on Soft Hydrogels." Biomimetics 5, no. 2 (2020): 30. http://dx.doi.org/10.3390/biomimetics5020030.

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Liver is an essential organ that carries out multiple functions such as glycogen storage, the synthesis of plasma proteins, and the detoxification of xenobiotics. Hepatocytes are the parenchyma that sustain almost all the functions supported by this organ. Hepatocytes and non-parenchymal cells respond to the mechanical alterations that occur in the extracellular matrix (ECM) caused by organogenesis and regenerating processes. Rearrangements of the ECM modify the composition and mechanical properties that result in specific dedifferentiation programs inside the hepatic cells. Quiescent hepatocy

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27

Lin, YC, and F. Grinnell. "Decreased level of PDGF-stimulated receptor autophosphorylation by fibroblasts in mechanically relaxed collagen matrices." Journal of Cell Biology 122, no. 3 (1993): 663–72. http://dx.doi.org/10.1083/jcb.122.3.663.

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The goal of our studies was to characterize the interrelationship between extracellular matrix organization and fibroblast proliferation in response to growth factors. We compared fibroblasts in monolayer culture with cells in contracted collagen matrices that were mechanically stressed or relaxed. In response to platelet-derived growth factor (PDGF), DNA synthesis by fibroblasts in mechanically relaxed collagen matrices was 80-90% lower than in monolayer culture and 50% lower than in mechanically stressed matrices. Fibroblasts in monolayer and contracted collagen matrix cultures contained sim

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28

Fujioka, K. "Protein release from collagen matrices." Advanced Drug Delivery Reviews 31, no. 3 (1998): 247–66. http://dx.doi.org/10.1016/s0169-409x(97)00119-1.

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29

Kee, Matthew F., David R. Myers, Yumiko Sakurai, Wilbur A. Lam, and Yongzhi Qiu. "Platelet Mechanosensing of Collagen Matrices." PLOS ONE 10, no. 4 (2015): e0126624. http://dx.doi.org/10.1371/journal.pone.0126624.

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Kee, Matthew F., Yongzhi Qiu, David R. Myers, Yumiko Sakurai, and Wilbur A. Lam. "Platelet Mechanosensing of Collagen Matrices." Blood 124, no. 21 (2014): 1437. http://dx.doi.org/10.1182/blood.v124.21.1437.1437.

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Abstract Background: Vascular injury causes platelets to initiate hemostasis by first adhering to exposed subendothelial matrix proteins such as collagen. While the biochemical and biological aspects of platelet adhesion via collagen and von willebrand factor are well characterized, if and whether the mechanical properties of the subendothelial matrix affect platelet function is relatively unknown. As purely mechanical cues, such as substrate stiffness, from collagen matrices are sensed and transduced by endothelial cells to alter their physiological processes, platelets may also exhibit simil

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31

Whittington, Catherine F., Eric Brandner, Ka Yaw Teo, Bumsoo Han, Eric Nauman, and Sherry L. Voytik-Harbin. "Oligomers Modulate Interfibril Branching and Mass Transport Properties of Collagen Matrices." Microscopy and Microanalysis 19, no. 5 (2013): 1323–33. http://dx.doi.org/10.1017/s1431927613001931.

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AbstractMass transport within collagen-based matrices is critical to tissue development, repair, and pathogenesis, as well as the design of next-generation tissue engineering strategies. This work shows how collagen precursors, specified by intermolecular cross-link composition, provide independent control of collagen matrix mechanical and transport properties. Collagen matrices were prepared from tissue-extracted monomers or oligomers. Viscoelastic behavior was measured in oscillatory shear and unconfined compression. Matrix permeability and diffusivity were measured using gravity-driven perm

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Sewing, Judith, Matthias Klinger, and Holger Notbohm. "Jellyfish collagen matrices conserve the chondrogenic phenotype in two- and three-dimensional collagen matrices." Journal of Tissue Engineering and Regenerative Medicine 11, no. 3 (2015): 916–25. http://dx.doi.org/10.1002/term.1993.

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Ferdous, Zannatul, Victoria Mariko Wei, Renato Iozzo, Magnus Höök та Kathryn Jane Grande-Allen. "Decorin-transforming Growth Factor-β Interaction Regulates Matrix Organization and Mechanical Characteristics of Three-dimensional Collagen Matrices". Journal of Biological Chemistry 282, № 49 (2007): 35887–98. http://dx.doi.org/10.1074/jbc.m705180200.

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The small leucine-rich proteoglycan decorin has been demonstrated to be a key regulator of collagen fibrillogenesis; decorin deficiencies lead to irregularly shaped collagen fibrils and weakened material behavior in postnatal murine connective tissues. In an in vitro investigation of the contributions of decorin to tissue organization and material behavior, model tissues were engineered by seeding embryonic fibroblasts, harvested from 12.5–13.5 days gestational aged decorin null (Dcn-/-) or wild-type mice, within type I collagen gels. The resulting three-dimensional collagen matrices were cult

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Grupe, Gisela, and Susanne Turban-Just. "Amino acid composition of degraded matrix collagen from archaeological human bone." Anthropologischer Anzeiger 56, no. 3 (1998): 213–26. http://dx.doi.org/10.1127/anthranz/56/1998/213.

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RAMTANI, SALAH, YOSHIYUKI TAKAHASHI-IÑIGUEZ, CHRISTOPHE HELARY, DIDIER GEIGER, and MARIE MADELEINE GIRAUD GUILLE. "MECHANICAL BEHAVIOR UNDER UNCONFINED COMPRESSION LOADINGS OF DENSE FIBRILLAR COLLAGEN MATRICES MIMETIC OF LIVING TISSUES." Journal of Mechanics in Medicine and Biology 10, no. 01 (2010): 35–55. http://dx.doi.org/10.1142/s0219519410003290.

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Bio-artificial tissues are being developed as replacements for damaged biologic tissues and their mechanical properties are critical for load-bearing applications. Reconstituted dense three-dimensional (3D) fibrillar collagen matrices are promising materials for tissue engineering, at the light of their interaction with fibroblasts.1,2 The mechanical properties of these fibrillar collagen matrices are now being characterized under unconfined compression loading for various strain rates and collagen concentrations. The data were compared to those obtained in the same conditions with a biologica

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Lin, Zhikai, Cristina Nica, Anton Sculean, and Maria B. Asparuhova. "Enhanced Wound Healing Potential of Primary Human Oral Fibroblasts and Periodontal Ligament Cells Cultured on Four Different Porcine-Derived Collagen Matrices." Materials 13, no. 17 (2020): 3819. http://dx.doi.org/10.3390/ma13173819.

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Xenogenic collagen-based matrices represent an alternative to subepithelial palatal connective tissue autografts in periodontal and peri-implant soft tissue reconstructions. In the present study, we aimed to investigate the migratory, adhesive, proliferative, and wound-healing potential of primary human oral fibroblasts (hOF) and periodontal ligament cells (hPDL) in response to four commercially available collagen matrices. Non-crosslinked collagen matrix (NCM), crosslinked collagen matrix (CCM), dried acellular dermal matrix (DADM), and hydrated acellular dermal matrix (HADM) were all able to

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Yamagata, M., K. M. Yamada, S. S. Yamada, et al. "The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site." Journal of Cell Biology 115, no. 1 (1991): 209–21. http://dx.doi.org/10.1083/jcb.115.1.209.

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Extracellular matrix molecules are generally categorized as collagens, elastin, proteoglycans, or other noncollagenous structural/cell interaction proteins. Many of these extracellular proteins contain distinctive repetitive modules, which can sometimes be found in other proteins. We describe the complete primary structure of an alpha 1 chain of type XII collagen from chick embryonic fibroblasts. This large, structurally chimeric molecule identified by cDNA analysis combines previously unrelated molecular domains into a single large protein 3,124 residues long (approximately 340 kD). The deduc

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Young, W. C., and I. M. Herman. "Extracellular matrix modulation of endothelial cell shape and motility following injury in vitro." Journal of Cell Science 73, no. 1 (1985): 19–32. http://dx.doi.org/10.1242/jcs.73.1.19.

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We utilized fluorescence microscopy and affinity-purified antibodies to probe the form and function of cytoplasmic actin in endothelial cells (EC) recovering from injury and grown on extracellular matrices in vitro. Bovine aortic EC were seeded onto glass microscope coverslips that had been coated with either BSA, fibronectin, type I and III (interstitial) collagens, type IV (basement membrane) collagen or gelatin. After EC that had been grown on glass, glass-BSA or extracellular matrix-coated coverslips reached confluence, a 300–400 micron zone of cells was mechanically removed to stimulate E

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Hall, Matthew S., Farid Alisafaei, Ehsan Ban, et al. "Fibrous nonlinear elasticity enables positive mechanical feedback between cells and ECMs." Proceedings of the National Academy of Sciences 113, no. 49 (2016): 14043–48. http://dx.doi.org/10.1073/pnas.1613058113.

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In native states, animal cells of many types are supported by a fibrous network that forms the main structural component of the ECM. Mechanical interactions between cells and the 3D ECM critically regulate cell function, including growth and migration. However, the physical mechanism that governs the cell interaction with fibrous 3D ECM is still not known. In this article, we present single-cell traction force measurements using breast tumor cells embedded within 3D collagen matrices. We recreate the breast tumor mechanical environment by controlling the microstructure and density of type I co

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Poole, C. A., S. Ayad, and R. T. Gilbert. "Chondrons from articular cartilage. V. Immunohistochemical evaluation of type VI collagen organisation in isolated chondrons by light, confocal and electron microscopy." Journal of Cell Science 103, no. 4 (1992): 1101–10. http://dx.doi.org/10.1242/jcs.103.4.1101.

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The pericellular microenvironment around articular cartilage chondrocytes must play a key role in regulating the interaction between the cell and its extracellular matrix. The potential contribution of type VI collagen to this interaction was investigated in this study using isolated canine tibial chondrons embedded in agarose monolayers. The immunohistochemical distribution of an anti-type VI collagen antibody was assessed in these preparations using fluorescence, peroxidase and gold particle probes in combination with light, confocal and transmission electron microscopy. Light and confocal m

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Abraham, Leah C., J. Fred Dice, Kyongbum Lee, and David L. Kaplan. "Phagocytosis and remodeling of collagen matrices." Experimental Cell Research 313, no. 5 (2007): 1045–55. http://dx.doi.org/10.1016/j.yexcr.2006.12.019.

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Fringer, Jeanne, and Frederick Grinnell. "Fibroblast Quiescence in Floating Collagen Matrices." Journal of Biological Chemistry 278, no. 23 (2003): 20612–17. http://dx.doi.org/10.1074/jbc.m212365200.

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Radhika, M., Mary Babu, and P. K. Sehgal. "Cellular proliferation on desamidated collagen matrices." Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology 124, no. 2 (1999): 131–39. http://dx.doi.org/10.1016/s0742-8413(99)00042-0.

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Li, Fengfu, David J. Carlsson, Chris Lohmann, Donna Bueckert, Rejean Munger, and May Griffith. "Corneal Implantation with Collagen-Copolymer Matrices." Key Engineering Materials 288-289 (June 2005): 389–92. http://dx.doi.org/10.4028/www.scientific.net/kem.288-289.389.

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RHEE, S., and F. GRINNELL. "Fibroblast mechanics in 3D collagen matrices☆." Advanced Drug Delivery Reviews 59, no. 13 (2007): 1299–305. http://dx.doi.org/10.1016/j.addr.2007.08.006.

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Jimi, S., S. Takebayashi, S. Ryu, K. Saku, and N. Sakata. "Higher Migratory Activity of Arterial Smooth Muscle Cells Than of Venous Smooth Muscle Cells on Different Collagen Matrices." Phlebology: The Journal of Venous Disease 13, no. 3 (1998): 120–25. http://dx.doi.org/10.1177/026835559801300307.

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Objective: To examine the biological differences between arteries and veins, we compared the migratory activities of arterial and venous smooth muscle cells (SMCs) using a modified Boyden chamber method. Design: Migratory activities of porcine arterial and venous smooth muscle cells (SMCs) were compared by a modified Boyden chamber method using coated filters with type I, III, IV and V collagens. Results: At the basal level of migration activity without stimulation, arterial SMCs showed greater migratory activity than venous SMCs in all of the substrata. When platelet-derived growth factor was

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A. Matthews, Jamil, Gary E. Wnek, David G. Simpson, and Gary L. Bowlin. "Vascular Tissue Engineering Utilizing Electrospun Matrices: Microscopic Evaluations." Microscopy and Microanalysis 7, S2 (2001): 142–43. http://dx.doi.org/10.1017/s1431927600026787.

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The development of a seamless, collagen-based vascular prosthetic scaffolding (< 4 mm I.D.) has been accomplished using an electrospinning fiber production technique (Patents Pending). Electrospinning is the deliberate application of the phenomenon of electrostatic spraying which occurs when electrical forces at the surface of the polymer solution overcome the surface tension, creating a splay. The splay produces fibers with diameters in the nano-scale range (<500 nm). The collagen-based scaffold production method (flexible, quick, and simple) utilizes the splaying of the collagen-based

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Kulakov, Anatoliy, Evgenia Kogan, Tatiana Brailovskaya, et al. "Mesenchymal Stromal Cells Enhance Vascularization and Epithelialization within 7 Days after Gingival Augmentation with Collagen Matrices in Rabbits." Dentistry Journal 9, no. 9 (2021): 101. http://dx.doi.org/10.3390/dj9090101.

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Soft gingival tissue deficiency remains a severe problem leading to postoperative recession, peri-implantitis, and bone resorption. The use of collagen matrices does not always lead to complete rebuilding of the gingiva volume. The application of mesenchymal stromal cells (MSCs) simultaneously with collagen materials represents a promising approach for the restoration of soft gingival tissues. However, short-term effects of MSCs-enriched collagen grafts after gingival augmentation have not yet been studied properly. Mucograft and Mucoderm matrices were implanted in rabbits (n = 12) simultaneou

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Fitch, J. M., A. Mentzer, R. Mayne, and T. F. Linsenmayer. "Independent deposition of collagen types II and IX at epithelial-mesenchymal interfaces." Development 105, no. 1 (1989): 85–95. http://dx.doi.org/10.1242/dev.105.1.85.

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Previous studies have demonstrated the presence of type II collagen (in mature chickens predominantly a ‘cartilage-specific’ collagen) in a variety of embryonic extracellular matrices that separate epithelia from mesenchyme. In an immunohistochemical study using collagen type-specific monoclonal antibodies, we asked whether type IX collagen, another ‘cartilage-specific’ collagen, is coexpressed along with type II at such interfaces. We confirmed that, in the matrix underlying a variety of cranial ectodermal derivatives and along the ventrolateral surfaces of neuroepithelia, type II collagen is

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Sgambato, Antonella, Valentina Pastori, Laura Russo, Simone Vesentini, Marzia Lecchi, and Laura Cipolla. "Neoglycosylated Collagen: Effect on Neuroblastoma F-11 Cell Lines." Molecules 25, no. 19 (2020): 4361. http://dx.doi.org/10.3390/molecules25194361.

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The regeneration of the nervous system is a challenging task. Currently, regenerative medicine approaches that exploit nature-inspired cues are being studied and hold great promise. The possibility to use protein-based matrices functionalized with small oligo- and monosaccharides is of interest since these can be finely tuned to better mimic the native environment. Collagen has been selected as a promising material that has the potential to be further tailored to incorporate carbohydrates in order to drive cell behavior towards neuroregeneration. Indeed, the grafting of carbohydrates to collag

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