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Jararhagin, a hemorrhagic snake venom metalloproteinase from Bothrops jararaca.

Abstract
Jararhagin is a metalloproteinase isolated from Bothrops jararaca snake venom, which has been extensively studied. These studies showed its involvement on most of the systemic and local damaging effects of snakebite envenomings. In this review we comment on the major targets of jararhagin as the vascular endothelium, platelets and coagulation factors and also its action on other cell systems as inflammatory cells and their mediators, cancer and cell signaling. The mechanisms of jararhagin action are discussed together with structural features essential for the expression of its biological activities. The studies reviewed here denote jararhagin as a prototype for studies of snake venom metalloproteinases, bringing new insights into cellular-matrix interactions and adding for the improvement of snakebite treatment.
AuthorsAna M Moura-da-Silva, Cristiani Baldo
JournalToxicon : official journal of the International Society on Toxinology (Toxicon) Vol. 60 Issue 3 Pg. 280-9 (Sep 01 2012) ISSN: 1879-3150 [Electronic] England
PMID22534074 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
CopyrightCopyright © 2012 Elsevier Ltd. All rights reserved.
Chemical References
  • Anticoagulants
  • Crotalid Venoms
  • Inflammation Mediators
  • Integrins
  • Platelet Aggregation Inhibitors
  • Reptilian Proteins
  • Collagen
  • Metalloendopeptidases
  • jararhagin
Topics
  • Animals
  • Anticoagulants (chemistry, metabolism, pharmacology)
  • Binding Sites
  • Bothrops (metabolism)
  • Brazil
  • Cell Adhesion (drug effects)
  • Collagen (chemistry, metabolism)
  • Crotalid Venoms (chemistry, enzymology, metabolism, pharmacology)
  • Endothelial Cells (drug effects, metabolism)
  • Humans
  • Inflammation Mediators (metabolism)
  • Integrins (chemistry, metabolism)
  • Macrophages (drug effects, immunology, metabolism)
  • Metalloendopeptidases (chemistry, metabolism, pharmacology)
  • Platelet Aggregation Inhibitors (chemistry, metabolism, pharmacology)
  • Protein Conformation
  • Reptilian Proteins (chemistry, metabolism, pharmacology)

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