Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8327428 | International Journal of Biological Macromolecules | 2018 | 19 Pages |
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 PIIIb-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 °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.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Andrea Carolina Van de Velde, Claudia Carolina Gay, Milene Nóbrega de Oliveira Moritz, Patty Karina dos Santos, Soledad Bustillo, Juan Pablo RodrÃguez, Ofelia Cristina Acosta, Mirtha Josefa Biscoglio, Heloisa Sobreiro Selistre-de-Araujo,