The Influence of Corneal Stromal Matrix Proteins on the Migration of Human Corneal Fibroblasts

Andresen, Jens; Ledet, Thomas; Hager, Henrik; Josephsen, Kaj; Ehlers, Niels

doi:10.1006/exer.2000.0850

Cited by 43 publications

(27 citation statements)

References 43 publications

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“…However, cell binding to collagen VI by integrin receptors is complex and appears to be cell type dependent (Tulla et al, 2001). Integrin receptors can bind this molecule either in an RGD or a non-RGD dependent manner (Andresen et al, 2000;Aumailley et al, 1989;Doane et al, 1998;Du et al, 2007;Leitinger and Hohenester, 2007;Pfaff et al, 1993;Tulla et al, 2001). Herein, we showed that the anti-β1 integrin antibody blocked approximately half of the intestinal cell adhesion to fibronectin, consistent with the presence of both β1 and αv integrins on these cells (Benoit et al, 2009), but almost completely blocked cell adhesion to collagen VI indicating that αv integrins are not involved.…”

Section: Discussionmentioning

confidence: 98%

Collagen VI is a basement membrane component that regulates epithelial cell–fibronectin interactions

et al. 2011

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Collagen VI is a heterotrimer composed of three α chains (α1, α2, α3) widely expressed throughout various interstitial matrices. Collagen VI is also found near the basement membranes of many tissues where it serves as an anchoring meshwork. The aim of this study was to investigate the distribution and role of collagen VI at the epithelial-stromal interface in the intestine. Results showed that collagen VI is a bona fide epithelial basal lamina component and constitutes the major collagen type of epithelial origin in this organ. In vitro, collagen VI co-distributes with fibronectin. Targeted knockdown of collagen VI expression in intestinal epithelial cells was used to investigate its function. Depletion of collagen VI from the matrix led to a significant increase in cell spreading and fibrillar adhesion formation coinciding with an upregulation of fibronectin expression, deposition and organization as well as activation of myosin light chain phosphorylation by the myosin light chain kinase and Rho kinase dependent mechanisms. Plating cells deficient for collagen VI on collagen VI rescued the phenotype. Taken together, these data demonstrate that collagen VI is an important basal lamina component involved in the regulation of epithelial cell behavior most notably as a regulator of epithelial cell-fibronectin interactions.

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Section: Discussionmentioning

confidence: 98%

Collagen VI is a basement membrane component that regulates epithelial cell–fibronectin interactions

et al. 2011

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“…Both interfere with fibronectin-mediated attachment and both impede TM (tenascin C data not shown) but not corneal fibroblast migration (Anderson et al, 2000). These proteins are also found present in the ECM of TM tissues, but they localize largely to different sites and co-localize only to a minor extent , suggesting distinct functions in the TM.…”

Section: Effects Of Extracellular Myocilinmentioning

confidence: 88%

Extracellular myocilin affects activity of human trabecular meshwork cells

Wentz‐Hunter

Kubota

Shen

et al. 2004

Journal Cellular Physiology

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The trabecular meshwork (TM), a specialized eye tissue, is a major site for regulation of the aqueous humor outflow. Malfunctioning of this tissue is believed to be responsible for development of glaucoma, a blinding disease. Myocilin is a gene linked to the most common form of glaucoma. The protein product has been localized to both intra and extracellular sites, but its function still remains unclear. This study was to determine whether extracellular myocilin presented in the matrix affects adhesion, morphology, and migratory and phagocytic activities of human TM cells in culture. Cell adhesion assays indicated that TM cells, while adhering readily on fibronectin, failed to attach on recombinant myocilin purified from bacterial cultures. Adhesion on fibronectin was also compromised by myocilin in a dose dependent manner. Myocilin in addition triggered TM cells to assume a stellate appearance with broad cell bodies and microspikes. Loss of actin stress fibers and focal adhesions was observed. TM cell migration on fibronectin/myocilin to scratched wounds was reduced compared to fibronectin controls. Myocilin, however, had little impact on phagocytic activities of TM cells. Cell attachment on fibronectin and migration of corneal fibroblasts, a control cell type, were not altered by myocilin. These results demonstrate that extracellular myocilin elicits anti-adhesive and counter-migratory effects on TM cells. Myocilin in the matrix of tissues could be exerting a similar influence on TM cells in vivo, impacting the flexibility and resilience required for maintenance of the normal aqueous outflow.

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“…7), and of RGD-containing peptides (Table I), to reverse the effect of tenascin on chemotaxis may reflect either their ability to block interactions of ␣ 5 ␤ 1 integrins with RGD ligands on tenascin, or their ability to generate a qualitatively different intracellular signal than the one that is generated when ␣ 5 ␤ 1 integrins interact with tenascin itself. Interestingly, Andersen et al (48) reported that addition of tenascin to fibronectin-containing matrices significantly reduced migration of corneal fibroblasts through these matrices. Furthermore, they found that anti-␣ 5 ␤ 1 IgG blocked attachment of corneal fibroblasts to fibronectin/tenascin-coated surfaces more effectively than to surfaces coated with only fibronectin.…”

Section: Discussionmentioning

confidence: 99%

Blockade of α5β1 Integrins Reverses the Inhibitory Effect of Tenascin on Chemotaxis of Human Monocytes and Polymorphonuclear Leukocytes Through Three-Dimensional Gels of Extracellular Matrix Proteins

Loike

Cao

Budhu

et al. 2001

The Journal of Immunology

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Tenascin is an extracellular matrix protein found in adults in T cell-dependent areas of lymphoid tissues, sites of inflammation, and tumors. We report here that it inhibited chemotaxis of chemoattractant-stimulated human monocytes and chemoattractant-stimulated polymorphonuclear leukocytes (PMN) through three-dimensional gels composed of collagen I or Matrigel, and chemotaxis of leukotriene B4-stimulated PMN through fibrin gels. The inhibitory effect of tenascin on monocyte or PMN chemotaxis through these matrices was reversed by Abs directed against α5β1 integrins or by a peptide (GRGDSP) that binds to β1 integrins. Tenascin did not affect leukotriene B4- or fMLP-stimulated expression of β1 or β2 integrins, but did exert a small inhibitory effect on PMN adhesion and closeness of apposition to fibrin(ogen)-containing surfaces. Thus, α5β1 integrins mediate the inhibitory effect of tenascin on monocyte and PMN chemotaxis, without promoting close apposition between these leukocytes and surfaces coated with tenascin alone or with tenascin bound to other matrix proteins. This contrasts with the role played by α5β1 integrins in promoting close apposition between fMLP-stimulated PMN and fibrin containing surfaces, thereby inhibiting chemotaxis of fMLP-stimulated PMN through fibrin gels. Thus, chemoattractants and matrix proteins regulate chemotaxis of phagocytic leukocytes by at least two different mechanisms: one in which specific chemoattractants promote very tight adhesion of leukocytes to specific matrix proteins and another in which specific matrix proteins signal cessation of migration without markedly affecting strength of leukocyte adhesion.

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The Influence of Corneal Stromal Matrix Proteins on the Migration of Human Corneal Fibroblasts

Cited by 43 publications

References 43 publications

Collagen VI is a basement membrane component that regulates epithelial cell–fibronectin interactions

Collagen VI is a basement membrane component that regulates epithelial cell–fibronectin interactions

Extracellular myocilin affects activity of human trabecular meshwork cells

Blockade of α5β1 Integrins Reverses the Inhibitory Effect of Tenascin on Chemotaxis of Human Monocytes and Polymorphonuclear Leukocytes Through Three-Dimensional Gels of Extracellular Matrix Proteins

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