A Novel P-III Metalloproteinase from <i>Bothrops barnetti</i> Venom Degrades Extracellular Matrix Proteins, Inhibits Platelet Aggregation, and Disrupts Endothelial Cell Adhesion via α5β1 Integrin Receptors to Arginine–Glycine–Aspartic Acid (RGD)-Containing Molecules

A Novel P-III Metalloproteinase from <i>Bothrops barnetti</i> Venom Degrades Extracellular Matrix Proteins, Inhibits Platelet Aggregation, and Disrupts Endothelial Cell Adhesion via α5β1 Integrin Receptors to Arginine–Glycine–Aspartic Acid (RGD)-Containing Molecules

Viperid snake venoms are notably abundant in metalloproteinases (proteins) (SVMPs), which are primarily responsible for inducing hemorrhage and disrupting the hemostatic process and tissue integrity in envenomed victims. In this study, barnettlysin-III (Bar-III), a hemorrhagic P-III SVMP, was purifi...

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Bibliographic Details
Main Authors: Pedro Henrique de Caires Schluga, Debora Larangote, Ana Maria de Melo, Guilherme Kamienski Lobermayer, Daniel Torrejón, Luciana Souza de Oliveira, Valeria Gonçalves Alvarenga, Dan Erick Vivas-Ruiz, Silvio Sanches Veiga, Eladio Flores Sanchez, Luiza Helena Gremski
Format: Article
Language:English
Published: MDPI AG 2024-11-01
Series:Toxins
Subjects:
snake venom metalloproteinase
disintegrin
animal venoms
<i>Bothrops barnetti</i>
Online Access:https://www.mdpi.com/2072-6651/16/11/486
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