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Functional roles of the two distinct domains of halysase, a snake venom metalloprotease, to inhibit human platelet aggregation.

Abstract：

:Halysase, a hemorrhagic metalloprotease, has an apparent molecular weight of 66kDa and belongs to the class P-III snake venom metalloprotease. Class P-III snake venom metalloproteases have multifunctional domains including a protease domain and a disintegrin-like domain. Halysase was able to preferentially hydrolyze the alpha-chain of fibrinogen. Proteolytic activity of the enzyme was completely inhibited by metal chelating agents but not by other typical protease inhibitors. The enzyme principally cleaves X-Leu, X-Tyr, X-Phe, and X-Ala peptide bonds of the oxidized insulin B-chain. Halysase strongly suppresses collagen-induced human platelet aggregation in a dose-dependent manner. Apohalysase that is devoid of its metalloprotease activity was also able to inhibit the platelet aggregation to a certain extent. Experimental evidence clearly indicates that each of the two distinct domains of halysase, the metalloprotease and the disintegrin-like domains, plays its characteristic role to inhibit human platelet aggregation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

You WK,Jang YJ,Chung KH,Jeon OH,Kim DS

doi

10.1016/j.bbrc.2005.11.083

subject

Has Abstract

pub_date

2006-01-20 00:00:00

pages

964-70

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02630-6

journal_volume

339

pub_type

杂志文章

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