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| Selistre-de-Araujo,H.S.; Cominetti,M.R.; Terruggi,C.H.B.; Mariano-Oliveira,A.; De Freitas,M.S.; Crepin,M.; Figueiredo,C.C.; Morandi,V.. |
| The alpha2ß1 integrin is a major collagen receptor that plays an essential role in the adhesion of normal and tumor cells to the extracellular matrix. Alternagin-C (ALT-C), a disintegrin-like protein purified from the venom of the Brazilian snake Bothrops alternatus, competitively interacts with the alpha2ß1 integrin, thereby inhibiting collagen binding. When immobilized in plate wells, ALT-C supports the adhesion of fibroblasts as well as of human vein endothelial cells (HUVEC) and does not detach cells previously bound to collagen I. ALT-C is a strong inducer of HUVEC proliferation in vitro. Gene expression analysis was done using an Affimetrix HU-95A probe array with probe sets of ~10,000 human genes. In human fibroblasts growing on collagen-coated... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Alpha2ß1 integrin; Disintegrin; Snake venom; Adhesion; Gene expression; Extracellular matrix. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001000007 |
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