| Texto completo | |
| Autor(es): |
Carolina Van de Velde, Andrea
[1]
;
Carolina Gay, Claudia
[1]
;
de Oliveira Moritz, Milene Nobrega
[2]
;
dos Santos, Patty Karina
[2]
;
Bustillo, Soledad
[1]
;
Pablo Rodriguez, Juan
[1]
;
Cristina Acosta, Ofelia
[3]
;
Josefa Biscoglio, Mirtha
[4]
;
Selistre-de-Araujo, Heloisa Sobreiro
[2]
;
Cristina Leiva, Laura
[1]
Número total de Autores: 10
|
| Afiliação do(s) autor(es): | [1] Inst Quim Basica & Aplicada Nordeste Argentino UN, Lab Invest Prot, Corrientes - Argentina
[2] Univ Fed Sao Carlos, Dept Ciencias Fisiol, Sao Carlos, SP - Brazil
[3] Univ Nacl Nordeste, Fac Ciencias Vet, Lab Farmacol, Corrientes - Argentina
[4] Inst Quim & Fis Quim Biol UBA CONICET, Buenos Aires, DF - Argentina
Número total de Afiliações: 4
|
| Tipo de documento: | Artigo Científico |
| Fonte: | International Journal of Biological Macromolecules; v. 113, p. 205-211, JUL 1 2018. |
| Citações Web of Science: | 2 |
| Resumo | |
Snake Venom Metalloproteinases (SVMPs) represent 43.1% of the components in Bothrops alternatus venom and play an important role in envenomation. Disintegrins and disintegrin-like domains are released by proteolytic processing of PII and PIII classes of SVMPs respectively and are potent inhibitors of integrin-ligand interaction. Baltergin is a PIllb-SVMP isolated from this venom and able to undergo autolysis in vitro, giving rise to a stable disintegrin-like/cystein-rich fragment (baltergin-DC). Conditions of baltergin autolysis were adjusted in order to carry out the purification of baltergin-DC and its effect on cell adhesion was studied. Autolysis was maximal at 37 degrees C and a pH range of 7.0-8.0. Baltergin-DC amino-terminal sequence begins with IISPPVCGNELLEVGEECDCGTPENCQNECCDAATC, which shows a high degree of homology with other disintegrin-like proteins. Baltergin and purified baltergin-DC were both able to inhibit C2C12 adhesion to fetal bovine serum (FBS) coated plates, indicating that a non-catalytic process is involved, probably mediated by binding to membrane integrins. Baltergin-DC, lacking proteolytic action, becomes an attractive molecule for future studies on blocking integrin-ligand interactions. (C) 2018 Elsevier B.V. All rights reserved. (AU) | |
| Processo FAPESP: | 13/00798-2 - A matriz extracelular no envelhecimento, no exercício e no microambiente tumoral |
| Beneficiário: | Heloisa Sobreiro Selistre de Araújo |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |