Title |
Conserved Structure and Adjacent Location of the Thrombin Receptor and Protease-Activated Receptor 2 Genes Define a Protease-Activated Receptor Gene Cluster
|
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Published in |
Molecular Medicine, May 1996
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DOI | 10.1007/bf03401632 |
Pubmed ID | |
Authors |
Mark Kahn, Kenji Ishii, Wen-Lin Kuo, Michael Piper, Andrew Connolly, Yu-Ping Shi, Richard Wu, C. C. Lin, Shaun R. Coughlin |
Abstract |
Thrombin is a serine protease that elicits a variety of cellular responses. Molecular cloning of a thrombin receptor revealed a G protein-coupled receptor that is activated by a novel proteolytic mechanism. Recently, a second protease-activated receptor was discovered and dubbed PAR2. PAR2 is highly related to the thrombin receptor by sequence and, like the thrombin receptor, is activated by cleavage of its amino terminal exodomain. Also like the thrombin receptor, PAR2 can be activated by the hexapeptide corresponding to its tethered ligand sequence independent of receptor cleavage. Thus, functionally, the thrombin receptor and PAR2 constitute a fledgling receptor family that shares a novel proteolytic activation mechanism. To further explore the relatedness of the two known protease-activated receptors and to examine the possibility that a protease-activated gene cluster might exist, we have compared the structure and chromosomal locations of the thrombin receptor and PAR2 genes. |
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Geographical breakdown
Country | Count | As % |
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Unknown | 13 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Doctoral Student | 2 | 15% |
Student > Master | 2 | 15% |
Professor > Associate Professor | 2 | 15% |
Student > Ph. D. Student | 2 | 15% |
Other | 1 | 8% |
Other | 3 | 23% |
Unknown | 1 | 8% |
Readers by discipline | Count | As % |
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Medicine and Dentistry | 3 | 23% |
Biochemistry, Genetics and Molecular Biology | 2 | 15% |
Unknown | 2 | 15% |