In:
Pathophysiology of Haemostasis and Thrombosis, S. Karger AG, Vol. 34, No. 4-5 ( 2005), p. 209-214
Abstract:
Snake venoms contain four classes of metalloproteases that all have a typical zinc-chelating sequence (HEXXHGXXH). N-terminal sequences and internal sequences of different purified metalloproteases were determined using Edman sequencing and LC MS/MS technique. Oligonucleotideswere designed and used as primers for cDNA cloning from 〈 i 〉 Vipera lebetina 〈 /i 〉 venom gland cDNA library. We found that isoforms of fibrinolytic enzyme lebetase Le-4 and Le-3 are synthesized in different way: Le-4 is synthesized as P-I type metalloprotease, Le-3 is synthesized with disintegrin-like domain as P-II type protease and processed post-translationally. An endothelial cell apoptosis-inducing heterodimeric glycosylated metalloprotease, 〈 i 〉 V. lebetina 〈 /i 〉 apoptosis-inducing protease (VLAIP), belongs to P-III type containing metalloprotease, disintegrin-like and cysteine-rich domains. All these enzymes hydrolyze the Aα-chain and more slowly the Bβ-chain of fibrinogen. Treatment of HUVEC cells with VLAIP induces changes in the attachment of cells to the substrate and causes apoptosis. 〈 i 〉 V. lebetina 〈 /i 〉 venom contains also P-IV type-specific coagulant factor X activator (VLFXA) that cleaves the Arg 〈 sup 〉 52 〈 /sup 〉 -Ile 〈 sup 〉 53 〈 /sup 〉 bond in the heavy chain of human factor X. VLFXA is a glycoprotein composed of a heavy chain and two C-type lectin-like light chains linked by disulfide bonds. The heavy and light chains of VLFXA are synthesized from different genes.
Type of Medium:
Online Resource
ISSN:
1424-8832
,
1424-8840
Language:
English
Publisher:
S. Karger AG
Publication Date:
2005
detail.hit.zdb_id:
2081182-2
