Atroxlysin-III, A Metalloproteinase from the Venom of the Peruvian Pit Viper Snake Bothrops atrox (Jergon) Induces Glycoprotein VI Shedding and Impairs Platelet Function.

ABSTRACT: Atroxlysin-III (Atr-III) was purified from the venom of Bothrops atrox. This 56-kDa protein bears N-linked glycoconjugates and is a P-III hemorrhagic metalloproteinase. Its cDNA-deduced amino acid sequence reveals a multidomain structure including a proprotein, a metalloproteinase, a disintegrin-like and a cysteine-rich domain. Its identity with bothropasin and jararhagin from Bothrops jararaca is 97% and 95%, respectively. Its enzymatic activity is metal ion-dependent. The divalent cations, Mg²⁺ and Ca²⁺, enhance its activity, whereas excess Zn²⁺ inhibits it. Chemical modification of the Zn²⁺-complexing histidine residues within the active site by using diethylpyrocarbonate (DEPC) inactivates it. Atr-III degrades plasma fibronectin

SUBMITTER: Oliveira LS 

PROVIDER: S-EPMC6803841 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature