scholarly journals Localization of Extracellular Matrix Receptors on the Chondrocyte Primary Cilium

2006 ◽  
Vol 54 (9) ◽  
pp. 1005-1014 ◽  
Author(s):  
Susan R. McGlashan ◽  
Cynthia G. Jensen ◽  
C. Anthony Poole
Keyword(s):  
Extracellular Matrix ◽  
Primary Cilium ◽  
Extracellular Matrix Receptors

Cytotrophoblast Expression of Integrin Extracellular Matrix Receptors Is Altered in Preeclampsia

1993 ◽  
pp. 109-122
Author(s):  
Yan Zhou ◽  
Caroline H. Damsky ◽  
King Chiu ◽  
James M. Roberts ◽  
Susan J. Fisher
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Receptors

scholarly journals Microinjection of antibodies against talin inhibits the spreading and migration of fibroblasts

1992 ◽  
Vol 102 (4) ◽  
pp. 753-762
Author(s):  
G.H. Nuckolls ◽  
L.H. Romer ◽  
K. Burridge
Keyword(s):  
Extracellular Matrix ◽  
Tissue Culture ◽  
Actin Filaments ◽  
Focal Adhesions ◽  
Cell Spreading ◽  
And Migration ◽  
Extracellular Matrix Receptors

Talin is believed to be one of the key proteins involved in linking actin filaments to extracellular matrix receptors in focal adhesions. Our strategy for studying the function of talin has been to inactivate talin in living fibroblasts in tissue culture through the microinjection of affinity-purified, polyclonal anti-talin antibodies. The effect of the injected anti-talin antibodies on cell spreading was found to depend on how recently the cells had been plated. Cells that were in the process of spreading on a fibronectin substratum, and which had newly developed focal adhesions, were induced to round up and to disassemble many of the adhesions. However, if fibroblasts were allowed to spread completely before they were microinjected with the anti-talin antibody, focal adhesions remained intact and the flat morphology of the cells was unaffected. The percentage of cells that were able to maintain a spread morphology despite the injection of anti-talin antibodies increased during the first few hours after plating on fibronectin substrata. Fibroblasts that were allowed to spread completely before microinjection with the anti-talin antibody retained both intact focal adhesions and a flat, well-spread morphology, but failed to migrate effectively. Our experiments do not directly address the role of talin in mature focal adhesions, but they indicate that talin is essential for the spreading and migration of fibroblasts on fibronectin as well as for the development and initial maintenance of focal adhesions on this substratum.

scholarly journals Integrin α5β1 nano-presentation regulates collective keratinocyte migration independent of substrate rigidity

2021 ◽  
Author(s):  
Jacopo Di Russo ◽  
Jennifer L. Young ◽  
Julian W. R. Wegner ◽  
Timmy Steins ◽  
Horst Kessler ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Migration ◽  
Cell Monolayer ◽  
Collective Cell Migration ◽  
Integrin Α5β1 ◽  
Migration Ability ◽  
Fibronectin Receptor ◽  
Substrate Rigidity ◽  
Scale Properties ◽  
Extracellular Matrix Receptors

AbstractNanometer-scale properties of the extracellular matrix influence many biological processes, including cell motility. While much information is available for single cell migration, to date, no knowledge exists on how the nanoscale presentation of extracellular matrix receptors influences collective cell migration. In wound healing, basal keratinocytes collectively migrate on a fibronectin-rich provisional basement membrane to re-epithelialize the injured skin. Among other receptors, the fibronectin receptor integrin α5β1 plays a pivotal role in this process. Using a highly specific integrin α5β1 peptidomimetic combined with nanopatterned hydrogels, we show that keratinocyte sheets regulate their migration ability at an optimal integrin α5β1 nanospacing. This efficiency relies on the effective propagation of stresses within the cell monolayer independent of substrate stiffness. For the first time, this work highlights the importance of extracellular matrix receptor nanoscale organization required for efficient tissue regeneration.

Distribution of extracellular matrix receptors in various forms of glomerulonephritis

1995 ◽  
Vol 25 (5) ◽  
pp. 680-688 ◽  
Author(s):  
Kenichi Shikata ◽  
Hirofumi Makino ◽  
Shigeru Morioka ◽  
Tadatoshi Kashitani ◽  
Kyoji Hirata ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Receptors

scholarly journals Integrins and Their Extracellular Matrix Ligands in Lymphangiogenesis and Lymph Node Metastasis

2012 ◽  
Vol 2012 ◽  
pp. 1-12 ◽  
Author(s):  
Jie Chen ◽  
J. Steven Alexander ◽  
A. Wayne Orr
Keyword(s):  
Extracellular Matrix ◽  
Lymph Node ◽  
Lymph Node Metastasis ◽  
Tumor Angiogenesis ◽  
Current Knowledge ◽  
Therapeutic Targets ◽  
Node Metastasis ◽  
Tumor Lymphangiogenesis ◽  
Vessel Development ◽  
Extracellular Matrix Receptors

In the 1970s, the late Judah Folkman postulated that tumors grow proportionately to their blood supply and that tumor angiogenesis removed this limitation promoting growth and metastasis. Work over the past 40 years, varying from molecular examination to clinical trials, verified this hypothesis and identified a host of therapeutic targets to limit tumor angiogenesis, including the integrin family of extracellular matrix receptors. However, the propensity for some tumors to spread through lymphatics suggests that lymphangiogenesis plays a similarly important role. Lymphangiogenesis inhibitors reduce lymph node metastasis, the leading indicator of poor prognosis, whereas inducing lymphangiogenesis promotes lymph node metastasis even in cancers not prone to lymphatic dissemination. Recent works highlight a role for integrins in lymphangiogenesis and suggest that integrin inhibitors may serve as therapeutic targets to limit lymphangiogenesis and lymph node metastasis. This review discusses the current literature on integrin-matrix interactions in lymphatic vessel development and lymphangiogenesis and highlights our current knowledge on how specific integrins regulate tumor lymphangiogenesis.

scholarly journals Responses of fibroblasts to anchorage of dorsal extracellular matrix receptors

2004 ◽  
Vol 101 (52) ◽  
pp. 18024-18029 ◽  
Author(s):  
K. A. Beningo ◽  
M. Dembo ◽  
Y.-l. Wang
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Receptors

Development and validation of competition binding assays for affinity to the extracellular matrix receptors, αvβ3 and αIIbβ3 integrin

2012 ◽  
Vol 423 (1) ◽  
pp. 70-77 ◽  
Author(s):  
Alexander M. Szabo ◽  
Nicholas R. Howell ◽  
Paul Pellegrini ◽  
Ivan Greguric ◽  
Andrew Katsifis
Keyword(s):  
Extracellular Matrix ◽  
Binding Assays ◽  
Competition Binding ◽  
Extracellular Matrix Receptors ◽  
Development And Validation ◽  
Αiibβ3 Integrin

Functional down-regulation of alpha 5 beta 1 integrin in keratinocytes is reversible but commitment to terminal differentiation is not

1993 ◽  
Vol 106 (4) ◽  
pp. 1131-1138 ◽  
Author(s):  
N.A. Hotchin ◽  
N.L. Kovach ◽  
F.M. Watt
Keyword(s):  
Extracellular Matrix ◽  
Ligand Binding ◽  
Terminal Differentiation ◽  
Binding Ability ◽  
Cell Extracts ◽  
Beta 1 Integrin ◽  
Loss Of Contact ◽  
Differentiation Marker ◽  
Extracellular Matrix Receptors ◽  
Integrin Family

Extracellular matrix receptors of the integrin family have a dual role in the epidermis, regulating both adhesion and differentiation. Loss of contact with the extracellular matrix causes keratinocytes to become committed to terminal differentiation, and results in a decrease in the ability of the alpha 5 beta 1 integrin to bind fibronectin. We have investigated whether the decrease in ligand-binding ability is reversible and, if so, whether commitment to terminal differentiation can also be reversed. Keratinocytes that had been placed in suspension for 5 hours to induce commitment were compared with the starting population (0 hour cells) in the presence or absence of 8A2, an activating anti-beta 1 antibody. 8A2 IgG or FAb fragments increased the amount of alpha 5 beta 1 in cell extracts that bound to fibronectin-Sepharose and in the presence of 8A2 the amount of bound alpha 5 beta 1 in 0 hour and 5 hour extracts was equal. 8A2 also restored alpha 5 beta 1 function in adhesion assays of intact 5 hour cells. Ca2+, Mg2+ and Mn2+ alone, at concentrations of up to 1 mM, did not increase the adhesiveness of 5 hour cells relative to 0 hour cells; however, the effect of 8A2 on keratinocytes was dependent on Ca2+. Although 8A2 restored alpha 5 beta 1 ligand-binding ability it did not prevent committed cells from withdrawing from the cell cycle and expressing involucrin, a differentiation marker.(ABSTRACT TRUNCATED AT 250 WORDS)

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