| Literature DB >> 18789468 |
E Tsuruga1, A Sato, T Ueki, K Nakashima, Y Nakatomi, H Ishikawa, T Yajima, Y Sawa.
Abstract
Fibrillin-1 is the major structural component of extracellular microfibrils. However, the mechanism by which extracellular fibrillin-1 assembles into microfibrils is not fully understood. Fibrillin-1 contains the Arg-Gly-Asp (RGD) motif, which may allow binding to RGD-recognizing integrins. We hypothesized that integrin alphavbeta3 on the cell surface of human periodontal ligament (PDL) fibroblasts may influence fibrillin-1 assembly into cell/matrix layers. We treated PDL fibroblasts with an integrin alphavbeta3-specific antagonist to examine fibrillin-1 assembly. Western blotting and immunofluorescence analysis showed that treatment with the integrin alphavbeta3 antagonist at 5 muM clearly abolished fibrillin-1 deposition. These results provide for the first time evidence that integrin alphavbeta3 regulates extracellular assembly of fibrillin-1, thereby modulating cell-mediated homeostasis of microfibrils.Entities:
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Year: 2008 PMID: 18789468 DOI: 10.1016/j.tice.2008.07.005
Source DB: PubMed Journal: Tissue Cell ISSN: 0040-8166 Impact factor: 2.466