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Domains specifying thrombin-receptor interaction
Nature (London), 1991-10, Vol.353 (6345), p.674-677
[Peer Reviewed Journal]
1992 INIST-CNRS ;Copyright Macmillan Journals Ltd. Oct 17, 1991 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/353674a0 ;PMID: 1717851 ;CODEN: NATUAS
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Title:
Domains specifying thrombin-receptor interaction
Author:
Vu, Thien-Khai H
;
Wheaton, Virginia I
;
Hung, David T
;
Charo, Israel
;
Coughlin, Shaun R
Subjects:
Amino Acid Sequence
;
Animals
;
Anions
;
Binding Sites
;
Binding sites (Biochemistry)
;
Biochemistry
;
Biological and medical sciences
;
Blood
;
Cell receptors
;
Cell structures and functions
;
Enzymes
;
Fundamental and applied biological sciences. Psychology
;
Gene Expression
;
Hirudins - chemistry
;
Humans
;
Medical research
;
Molecular and cellular biology
;
Molecular Sequence Data
;
Mutagenesis
;
Neuropeptide receptors
;
Oocytes - metabolism
;
Physiological aspects
;
Receptors, Cell Surface - chemistry
;
Receptors, Cell Surface - genetics
;
Receptors, Cell Surface - metabolism
;
Receptors, Thrombin
;
RNA - genetics
;
RNA, Complementary
;
Thrombin
;
Thrombin - metabolism
;
Thrombin - pharmacology
;
Thrombosis
;
Xenopus
Is Part Of:
Nature (London), 1991-10, Vol.353 (6345), p.674-677
Description:
Platelet activation by the coagulation protease thrombin is central to arterial thrombosis, a major cause of morbidity and mortality. We recently isolated a complementary DNA encoding the platelet thrombin receptor. The extracellular amino-terminal extension of this seven transmembrane domain receptor contains the putative thrombin cleavage site LDPR/S which is critical for receptor activation. By replacing this cleavage site with the cleavage site for enterokinase, we have created a functional enterokinase receptor. This result demonstrates that all information necessary for receptor activation is provided by receptor proteolysis. Nanomolar enterokinase concentrations are required to activate this new receptor, in contrast to the picomolar thrombin concentrations that activate wild-type thrombin receptor. We identified a receptor domain critical for thrombin's remarkable potency at its receptor. This domain resembles the carboxyl tail of the leech anticoagulant hirudin and functions by binding to thrombin's anion-binding exosite. Our studies thus define a model for thrombin-receptor interaction. The utility of this model was demonstrated by the design of novel thrombin inhibitors based on receptor peptides.
Publisher:
London: Nature Publishing
Language:
English
Identifier:
ISSN: 0028-0836
EISSN: 1476-4687
DOI: 10.1038/353674a0
PMID: 1717851
CODEN: NATUAS
Source:
ProQuest One Psychology
MEDLINE
Alma/SFX Local Collection
ProQuest Central
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