Thrombin interaction with a recombinant N-terminal extracellular domain of the thrombin receptor in an acellular system
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چکیده
منابع مشابه
The N-terminal thrombin receptor fragment SFLLRN, but not catalytically inactive thrombin-derived agonists, activate U937 human monocytic cells: evidence for receptor hydrolysis in thrombin-dependent signalling.
It has previously been reported that murine macrophages can respond chemotactically and mitogenically to the serine proteinase thrombin. There is a similar response in these macrophages to catalytically inactivated thrombin or to peptide fragments of the thrombin B-chain [Bar-Shavit, Kahn, Mann and Wilner (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 976-980]. However, the existence of a non-proteol...
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Intact human platelets contain on their outer surface a glycoprotein, glycocalicin (M, = 150,000). which is released in soluble form following platelet homogenization while glycoprotein I, which has a similar electrophoretic mobility, remains bound to the plasma membrane (Okumura, T., and Jamieson, G. A. (1976)5. Bid. Chem. 251, 5944-5949). Purified glycocalicin has now been shown to be a compe...
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The protease-activated thrombin receptor-1 (PAR-1) can be activated by both the tethered ligand exposed by thrombin cleavage and a synthetic peptide having the tethered ligand sequence (thrombin receptor agonist peptide or TRAP). We conducted a mutational analysis of extracellular residues of the receptor potentially involved in interaction with both the tethered ligand and the soluble peptide ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1995
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3050635