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Inhibition of platelet aggregation by the recombinant cysteine-rich domain of the hemorrhagic snake venom metalloproteinase, atrolysin A.

Abstract：

:The P-III class of venom metalloproteinases has, in addition to the proteinase domain, a disintegrin-like domain and a cysteine-rich domain. Recent evidence has shown that the nonproteinase domains of the P-III class of hemorrhagic metalloproteinases function in the inhibition of platelet aggregation by blocking essential procoagulant integrins on platelets. A specific role for the highly conserved cysteine-rich domain has yet to be described. In this study, we expressed the cysteine-rich domain from the hemorrhagic metalloproteinase atrolysin A and demonstrated its ability to inhibit collagen-stimulated platelet aggregation. Additionally, the cysteine-rich domain was shown to interact with MG-63 cells to inhibit adhesion to collagen I. These data suggest a functional role for the cysteine-rich domain of the P-III toxins in the observed coagulopathy by targeting the toxin to platelets and inhibiting collagen-stimulated platelet aggregation. These characteristics may function to synergistically increase the hemorrhagic effect of the toxins.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Jia LG,Wang XM,Shannon JD,Bjarnason JB,Fox JW

doi

10.1006/abbi.1999.1517

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

281-6

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(99)91517-5

journal_volume

373

pub_type

杂志文章

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