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Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation

Cell, 1991-03, Vol.64 (6), p.1057-1068 [Peer Reviewed Journal]

1991 ;1991 INIST-CNRS ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/0092-8674(91)90261-V ;PMID: 1672265 ;CODEN: CELLB5

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Title:
Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
Author: Vu, Thien-Khai H. ; Hung, David T. ; Wheaton, Virginia I. ; Coughlin, Shaun R.
Subjects: Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Biotechnology ; Blood Platelets - metabolism ; Cell Line ; Cloning, Molecular ; Endothelium - metabolism ; Fundamental and applied biological sciences. Psychology ; Genetic engineering ; Genetic technics ; Humans ; Megakaryocytes - metabolism ; Methods. Procedures. Technologies ; Microinjections ; Molecular cloning ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oocytes - metabolism ; Peptide Fragments - metabolism ; Platelet Activation - physiology ; Poly A - genetics ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - genetics ; Receptors, Cell Surface - metabolism ; Receptors, Thrombin ; RNA, Messenger - genetics ; RNA, Messenger - physiology ; Thrombin - physiology ; Xenopus laevis
Is Part Of: Cell, 1991-03, Vol.64 (6), p.1057-1068
Description: We isolated a cDNA encoding a functional human thrombin receptor by direct expression cloning in Xenopus oocytes. mRNA encoding this receptor was detected in human platelets and vascular endothelial cells. The deduced amino acid sequence revealed a new member of the seven transmembrane domain receptor family with a large amino-terminal extracellular extension containing a remarkable feature. A putative thrombin cleavage site (LDPR/S) resembling the activation cleavage site in the zymogen protein C (LDPR/I) was noted 41 amino acids carboxyl to the receptor's start methionine. A peptide mimicking the new amino terminus created by cleavage at R41 was a potent agonist for both thrombin receptor activation and platelet activation. “Uncleavable” mutant thrombin receptors falled to respond to thrombin but were responsive to the new amino-terminal peptide. These data reveal a novel signaling mechanism in which thrombin cleaves its receptor's amino-terminal extension to create a new receptor amino terminus that functions as a tethered ligand and activates the receptor.
Publisher: Cambridge, MA: Elsevier Inc
Language: English
Identifier: ISSN: 0092-8674
EISSN: 1097-4172
DOI: 10.1016/0092-8674(91)90261-V
PMID: 1672265
CODEN: CELLB5
Source: MEDLINE
Alma/SFX Local Collection

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Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation

1991 ;1991 INIST-CNRS ;ISSN: 0092-8674 ;EISSN: 1097-4172 ;DOI: 10.1016/0092-8674(91)90261-V ;PMID: 1672265 ;CODEN: CELLB5

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