| First Author | Sasaki T | Year | 2001 |
| Journal | FEBS Lett | Volume | 509 |
| Issue | 2 | Pages | 181-5 |
| PubMed ID | 11741585 | Mgi Jnum | J:73332 |
| Mgi Id | MGI:2154892 | Doi | 10.1016/s0014-5793(01)03167-2 |
| Citation | Sasaki T, et al. (2001) Domain IVa of laminin alpha5 chain is cell-adhesive and binds beta1 and alphaVbeta3 integrins through Arg-Gly-Asp. FEBS Lett 509(2):181-5 |
| abstractText | 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. |
