Molecular cloning of a potential proteinase activated receptor

Sverker Nystedt, Kjell Emilsson, Claes Wahlestedt, Johan Sundelin

Research output: Contribution to journalArticle

788 Scopus citations

Abstract

A DNA sequence encoding a G-protein-coupled receptor was isolated from a mouse genomic library. The predicted protein is similar in structure to the thrombin receptor and has a similar activation mechanism. When expressed in Xenopus laevis oocytes, the receptor was activated by low concentrations of trypsin (EC 3.4.21.4) and by a peptide (SLIGRL) derived from the receptor sequence, but was not activated by thrombin (EC 3.4.21.5). Trypsin failed to activate a mutant receptor in which the presumed cleavage site Arg-34-Ser-35 was changed to an Arg-Pro sequence. The agonist peptide (SLIGRL) activated equally well mutant and wild-type receptors. Northern blot analysis demonstrated receptor transcripts in highly vascularized tissues such as kidney, small intestine, and stomach. Because this, to our knowledge, is the second example, besides the thrombin receptor, of a proteolytically activated seven-transmembrane G-protein-coupled receptor, we have provisionally named it proteinase activated receptor 2.

Original languageEnglish (US)
Pages (from-to)9208-9212
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue number20
DOIs
StatePublished - Sep 27 1994
Externally publishedYes

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