Isolation and characterization of four medium-size disintegrins from the venoms of Central American viperid snakes of the genera Atropoides, Bothrops, Cerrophidion and Crotalus

Four disintegrins were isolated from the venoms of the Central American viperid snakes Atropoides mexicanus (atropoimin), Bothrops asper (bothrasperin), Cerrophidion sasai (sasaimin), and Crotalus simus (simusmin). Purifications were performed by reverse-phase HPLC. The four disintegrins have bioche...

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Detalles Bibliográficos
Autores: Angulo Ugalde, Yamileth, Castro Godínez, Adriana, Lomonte, Bruno, Rucavado Romero, Alexandra, Fernández Ulate, Julián, Calvete Chornet, Juan José, Gutiérrez, José María
Tipo de recurso: artículo
Fecha de publicación:2014
País:Costa Rica
Institución:Universidad de Costa Rica
Repositorio:Kérwá
OAI Identifier:oai:kerwa.ucr.ac.cr:10669/30339
Acceso en línea:http://www.sciencedirect.com/science/article/pii/S030090841400296X
https://hdl.handle.net/10669/30339
Access Level:acceso embargado
Palabra clave:Disintegrins
Snake venom
Platelet aggregation
Cell adhesion
Integrins
Descripción
Sumario:Four disintegrins were isolated from the venoms of the Central American viperid snakes Atropoides mexicanus (atropoimin), Bothrops asper (bothrasperin), Cerrophidion sasai (sasaimin), and Crotalus simus (simusmin). Purifications were performed by reverse-phase HPLC. The four disintegrins have biochemical characteristics, i.e. molecular mass and location of Cys, which allow their classification within the group of medium-size disintegrins. All of them present the canonical RGD sequence, which determines their interaction with integrins in cell membranes. The disintegrins inhibited ADP and collagen-induced human platelet aggregation, with similar IC50s in the nM range. In addition, disintegrins inhibited the adhesion of an endothelial cell line and a melanoma cell line to the extracellular matrix proteins type I collagen, laminin, fibronectin, and vitronectin, albeit showing variable ability to exert this activity. This study expands the inventory of this family of viperid venom proteins, and reports, for the first time, disintegrins from the venoms of species of the genera Atropoides and Cerrophidion.