Migration of keratinocytes through tunnels of digested fibrin

Ronfard, Vincent; Barrandon, Yann

doi:10.1073/pnas.071631698

Cited by 30 publications

(31 citation statements)

References 52 publications

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“…167,189 Furthermore, it forms a useful matrix into which fusion proteins (such as growth factors) can be attached to the matrix via the clotting transglutaminase factor XIIIa. 168 Cells must proteolytically degrade the dense fibrin mesh by releasing plasmin activators or MMPs (matrix metalloproteinases) in order to successfully migrate; 97,117,162 thus, fibrin is a useful matrix to study protease-dependent cell migration. The structural architectures of typical in vitro gels made of type I collagen and fibrin as seen by confocal reflectance microscopy are shown in Fig.…”

Section: Reconstituted Type I Collagen and Fibrin Matricesmentioning

confidence: 99%

Mechanobiology in the Third Dimension

2005

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Abstract-Cells are mechanically coupled to their extracellular environments, which play critical roles in both communicating the state of the mechanical environment to the cell as well as in mediating cellular response to a variety of stimuli. Along with the molecular composition and mechanical properties of the extracellular matrix (ECM), recent work has demonstrated the importance of dimensionality in cell-ECM associations for controlling the sensitive communication between cells and the ECM. Matrix forces are generally transmitted to cells differently when the cells are on two-dimensional (2D) vs. within three-dimensional (3D) matrices, and cells in 3D environments may experience mechanical signaling that is unique vis-à-vis cells in 2D environments, such as the recently described 3D-matrix adhesion assemblies. This review examines how the dimensionality of the extracellular environment can affect in vitro cell mechanobiology, focusing on collagen and fibrin systems.

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Section: Reconstituted Type I Collagen and Fibrin Matricesmentioning

confidence: 99%

Mechanobiology in the Third Dimension

2005

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“…The relevance of any particular integrin appears to be primarily dependent on the matrix environment (eg, adult, embryonic, wound, tumor) where the EC tube morphogenic process takes place. 3,9,[15][16][17][18][19] Extracellular matrix (ECM) proteolysis is thought to be an important step in how cells move through 3D matrix environments [20][21][22][23][24][25][26][27] and has been implicated in vessel formation 11,21,[28][29][30][31][32] as well as vessel regression. [33][34][35][36] Recently, we reported that pericyte recruitment to EC tubes induced stabilization by affecting the production and function of EC-derived tissue inhibitor of metalloproteinases (TIMP)-2 and pericyte-derived TIMP-3, which led to inhibition of both tube morphogenic and regression events.…”

Section: Introductionmentioning

confidence: 99%

Endothelial cell lumen and vascular guidance tunnel formation requires MT1-MMP–dependent proteolysis in 3-dimensional collagen matrices

Stratman

Saunders

Sacharidou

et al. 2009

Blood

215

310

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Here we show that endothelial cells (EC) require matrix type 1-metalloproteinase (MT1-MMP) for the formation of lumens and tube networks in 3-dimensional (3D) collagen matrices. A fundamental consequence of EC lumen formation is the generation of vascular guidance tunnels within collagen matrices through an MT1-MMP-dependent proteolytic process. Vascular guidance tunnels represent a conduit for EC motility within these spaces (a newly remodeled 2D matrix surface) to both assemble and remodel tube structures. Interestingly, it appears that twice as many tunnel spaces are created than are occupied by tube networks after several days of culture. After tunnel formation, these spaces represent a 2D migratory surface within 3D collagen matrices allowing for EC migration in an MMPindependent fashion. Blockade of EC lumenogenesis using inhibitors that interfere with the process (eg, integrin, MMP, PKC, Src) completely abrogates the formation of vascular guidance tunnels. Thus, the MT1-MMP-dependent proteolytic process that creates tunnel spaces is directly and functionally coupled to the signaling mechanisms required for EC lumen and tube network formation. In summary, a fundamental and previously unrecognized purpose of EC tube morphogenesis is to create networks of matrix conduits that are necessary for EC migration and tube remodeling events critical to blood vessel assembly. (Blood. 2009;114: 237-247) IntroductionMuch progress has occurred in our understanding of the molecular events controlling the processes underlying vascularization of tissues in the context of development and disease. [1][2][3][4][5][6][7] Work that is receiving increasing attention focuses on identifying specific steps required for vascular morphogenesis, including those involving endothelial cell (EC) lumen formation. [8][9][10][11][12] In addition to the identification of specific molecules required for these events, it is important to determine how different cell types such as endothelial cells, pericytes, and vascular smooth muscle cells interact and assemble to form the different characteristic blood vessel types. 1,6,13,14 Recent work from our laboratory reveals that ECs form lumens in 3-dimensional (3D) collagen matrices through a signaling cascade involving integrins, Rho GTPases, and membrane-type matrix metalloproteinases (MT-MMPs). [8][9][10][11][12] These signaling events stimulate EC intracellular vacuole formation and coalescence that controls EC lumen formation in vitro and in vivo. 8,10,12 A variety of integrins have been described to be relevant in regulating angiogenesis and tube formation including both ␤1 and ␣v integrins. The relevance of any particular integrin appears to be primarily dependent on the matrix environment (eg, adult, embryonic, wound, tumor) where the EC tube morphogenic process takes place. 3,9,[15][16][17][18][19] Extracellular matrix (ECM) proteolysis is thought to be an important step in how cells move through 3D matrix environments [20][21][22][23][24][25][26][27] and has been implicated in vessel for...

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“…1 This fibrin-fibronectin scaffolding functions initially as a structural support for infiltrating cells, leading to cell re-colonization and subsequent tissue healing. [2][3][4] Fibrin polymerization favors the adhesion of many cell types, including inflammatory cells, 5,6 epithelial cells, 7 endothelial cells, 8,9 and fibroblasts. 10 Cell adhesion to fibrin matrices is mediated by several molecules including cell adhesion molecules, 11 cadherins, 8,9 and arginine glycine aspartic acid (RGD)-binding integrins.…”

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confidence: 99%