Edema induction by the disintegrin-like/cysteine-rich domains from a Bothrops atrox hemorrhagin.

Abstract

Viperine and crotaline snake venoms contain one or more hemorrhagic metalloproteases called hemorrhagins. The most potent hemorrhagins belong to the P-III class and have, in addition to the protease domain, disintegrin-like and cysteine-rich domains. Although proteolytic degradation of vascular endothelium basement membrane has been established to be the main factor responsible for hemorrhage, several studies reveal other factors that actually do facilitate this process. Recent evidence has shown that the nonprotease domains of the P-III class hemorrhagins are able to inhibit the platelet aggregation by blocking essential procoagulant integrins on platelets. In this study we report the identification of a hemorrhagin from Bothrops atrox venom. This enzyme, a P-III class metalloprotease, undergoes an apparent spontaneous degradation, releasing a proteic fragment containing the disintegrin-like/cysteine-rich domains. This fragment shows the capability to induce an edematogenic process, suggesting the existence of a still unknown nonenzymatic mechanism of vascular permeability increase.

• Authors: J H Petretski, M M Kanashiro, F R Rodrigues, E W Alves, O L Machado, T L Kipnis
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 276 Issue 1 Pg. 29-34 (Sep 16 2000) ISSN: 0006-291X [Print] United States
• PMID: 11006077 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright 2000 Academic Press.

Chemical References

• Crotalid Venoms
• Disintegrins
• Platelet Aggregation Inhibitors
• Endopeptidases
• hemorrhagic proteinase IV
• Cysteine

Topics

• Amino Acid Sequence
• Animals
• Bothrops
• Crotalid Venoms
• Cysteine
• Disintegrins (toxicity)
• Edema (chemically induced)
• Endopeptidases (chemistry, genetics, toxicity)
• Mice
• Mice, Inbred BALB C
• Molecular Sequence Data
• Platelet Aggregation Inhibitors (toxicity)