Hemorrhagic and procoagulant P-III snake venom metalloproteinases differ in their binding to the microvasculature of mouse cremaster muscle

 

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Detalles Bibliográficos
Autores: Herrera Arias, Cristina, Escalante Muñoz, Teresa, Rucavado Romero, Alexandra, Gutiérrez, José María
Formato: artículo original
Data de Publicación:2020
Descripción:Binding of two P-III snake venom metalloproteinase (SVMPs), one procoagulant and one hemorrhagic, to microvessels was compared in an ex vivo model. The procoagulant SVMP did not bind to the microvasculature, in contrast to the clear localization on microvessels of the hemorrhagic SVMP. Deglycosylation of the procoagulant enzyme did not enable this toxin to bind to microvessels, suggesting that glycosylation is not interfering with binding. These observations suggest that procoagulant SVMPs lack exosites for interaction with microvessels components.
País:Kérwá
Institución:Universidad de Costa Rica
Repositorio:Kérwá
Idioma:Inglés
OAI Identifier:oai:kerwa.ucr.ac.cr:10669/104174
Acceso en liña:https://hdl.handle.net/10669/104174
https://doi.org/10.1016/j.toxicon.2020.02.011
Palabra crave:snake venom metallopoteinases (SVMPs)
hemorrhagic enzymes
procoagulant enzymes
glycosylation
microvasculature
confocal microscopy