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| Rádis-Baptista,G.. |
| Integrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis).... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Integrin; Angiogenesis; Cancer; Apoptosis; Snake toxin; Snake venom C-type lectin; Metalloprotease; Disintegrin. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000300002 |
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| Rádis-Baptista,G.; Moreno,F. B. M. B.; Nogueira,L. L.; Martins,A. M. C.; Toyama,D. O.; Toyama,M. H.; Azevedo Jr,W. F.; Cavada,B. S.; Yamane,T.. |
| Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins, which are able to interfere with hemostasis. They share significant similarity in their primary structures with C-type lectins of other animals, and also present a conserved carbohydrate recognition domain (CRD). A very well studied sv C-type lectin is the heterodimeric toxin, convulxin (CVX), from the venoms of South American rattlesnakes, Crotalus durissus terrificus and C. d. cascavella. It consists of two subunits, alfa (CVXalpha , 13.9 kDa) and beta (CVXbeta , 12.6 kDa), joined by inter and intra-chain disulfide bounds, and is arranged in a tetrameric alpha4beta4 conformation. Convulxin is able to activate platelet and induce their aggregation by acting via p62/GPVI collagen... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Crotalus durisssus venom; Snake venom C-type lectin; Homology modeling; Platelet aggregation; Antimicrobial activity. |
| Ano: 2005 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992005000400013 |
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