A monoclonal antibody inhibits adhesion to fibronectin and vitronectin of a colon carcinoma cell line and recognizes the integrins alpha v beta 3, alpha v beta 5, and alpha v beta 6

Lehmann, M.; Rabenandrasana, C.; Tamura, R.; Lissitzky, J.C.; Quaranta, V.; Pichon, J.; Marvaldi, J.

Cancer Research 54(8): 2102-2107

1994


ISSN/ISBN: 0008-5472
PMID: 7513610
Accession: 008048112

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Abstract
Using whole viable human colon carcinoma HT29 cells as immunogen, we produced a monoclonal antibody (mAb) termed 69-6-5. The antibody was functionally selected on its anti-cell-spreading activity. By immunoprecipitation of surface radiolabeled cell lysates from HT29-D4 cells (an HT29 cell clone), mAb 69-6-5 recognized a molecular complex resembling integrin heterodimers. Sequential immunodepletions with mAb to the integrin alpha-v subunit demonstrated that this complex was composed of alpha-v-containing integrins. Accordingly, mAb 69-6-5 reacted with integrin alpha-V-beta-3 immunopurified from melanoma cells and integrins alpha-V-beta-5 and alpha-v-beta-6 immunopurified from pancreatic carcinoma cells. In cell adhesion assays, the 69-6-5 mAb was able to inhibit strongly in a dose-dependent manner arginine-glycine-aspartic acid-mediated adhesion of HT29-D4 cells to vitronectin, fibronectin, or ProNectin F but not to laminin or collagen. Immunoprecipitations with beta chain-specific antisera indicated that these cells express integrins alpha-v-beta-5 (receptor for vitronectin) and alpha-v-beta-6 (receptor for fibronectin) but neither alpha-v-beta-1 nor alpha-v-beta-3. In summary, these results indicated that mAb 69-6-5 reacts with several alpha-v integrins and that it can effectively interfere with the adhesive functions of at least alpha-v-beta-5 and alpha-v-beta-6, which represent the major receptors on HT29-D4 cells responsible for their adhesion on vitronectin and fibronectin.