Collagen-induced secretion-dependent phase of platelet aggregation is inhibited by the snake venom metalloproteinase jararhagin

被引:53
作者
Kamiguti, AS
MouradaSilva, AM
Laing, GD
Knapp, T
Zuzel, M
Crampton, JM
Theakston, RDG
机构
[1] WOLFSON UNIT MOL GENET,LIVERPOOL,MERSEYSIDE,ENGLAND
[2] UNIV LIVERPOOL,LIVERPOOL SCH TROP MED,VENOM RES UNIT,LIVERPOOL L3 5QA,MERSEYSIDE,ENGLAND
[3] INST BUTANTAN,IMMUNOPATHOL LAB,SAO PAULO,BRAZIL
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 1997年 / 1335卷 / 1-2期
基金
英国惠康基金;
关键词
venom metalloproteinase; platelet aggregation; secretion; phosphorylation; disintegrin; (Bothrops jararaca);
D O I
10.1016/S0304-4165(96)00140-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Jararhagin, a 52 kDa metalloproteinase from Bothrops jararaca snake venom, belongs to the family of enzymes with an N-terminal Zn2+-containing enzymatic domain, a disintegrin-like domain and a cysteine-rich C-terminal domain. Both jararhagin and jararhagin C, a 28 kDa-protein from the same venom identical to the disintegrin-like domain of jararhagin, inhibit collagen-induced platelet aggregation. In this study, jararhagin and synthetic linear peptides based on the disintegrin-like domain of jararhagin overlapping with the RGD sequence of venom disintegrins, were shown for the first time to inhibit the release of 5-hydroxytryptamine (5-HT) from platelets preloaded with [C-14]S-HT and stimulated with collagen. The normal phosphorylation of the 21-kDa myosin light chain (p21) in response to the stimulation indicated that jararhagin and the peptides did not interfere with platelet shape change. The selective inhibition of the secretion-dependent phase of the platelet response to collagen by the enzyme and its peptides was confirmed by the defective phosphorylation of pleckstrin, a 47-kDa platelet protein (p47) involved in dense granule secretion.
引用
收藏
页码:209 / 217
页数:9
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