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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Purification of a fragment obtained by autolysis of a PIIIb-SVMP from Bothrops alternatus venom

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Author(s):
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]
Total Authors: 10
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 113, p. 205-211, JUL 1 2018.
Web of Science Citations: 2
Abstract

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)

FAPESP's process: 13/00798-2 - The extracellular matrix in aging, exercise and in the tumor microenvironment
Grantee:Heloisa Sobreiro Selistre de Araújo
Support Opportunities: Research Projects - Thematic Grants