Domain IVa of laminin α5 chain is cell‐adhesive and binds β1 and αVβ3 integrins through Arg‐Gly‐Asp
- 27 November 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 509 (2) , 181-185
- https://doi.org/10.1016/s0014-5793(01)03167-2
Abstract
The globular domain IVa from the short arm region of mouse laminin alpha5 chain was obtained by recombinant production and shown to be a cell-adhesive substrate and to bind alphaVbeta3 integrin in solid-phase assays. These interactions were blocked by RGD peptides and a restricted panel of anti-integrin antibodies. The two RGD sequences present in alpha5IVa were shown by site-directed mutagenesis to make different contributions to cell adhesion but were equivalent in binding alphaVbeta3 integrin. A quantitative radioimmuno-inhibition assay was established based on domain alpha5IVa which demonstrated distinct amounts of alpha5 chain in various tissues, particularly in vessel walls. There it could play a role in angiogenesis steps requiring RGD-dependent integrins.Keywords
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