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- W2015336799 abstract "We have examined the biological activities of thrombin and the thrombin-receptor-related polypeptides, S42FLLRNPNDKYEPF55(TRP42–55), S42FLLRNPND50(TRP42–50), and A42FLLRNPND50(A42-TRP42–50) as well as an arginine-containing basic peptide beginning with the SF motif (SFRGHITR), in rat aortic (RA) rings and in a gastric guinea pig longitudinal (LM) smooth muscle preparation. In the RA preparation, thrombin, as well as the three receptor-related peptides caused a relaxation in tissue that was precontracted with noradrenaline; the basic peptide, SFRGHITR, was inactive either as an agonist or as an antagonist to TRP42–55. In the LM bioassay, which unlike the RA preparation did not persistently desensitize in response to thrombin, all three receptor-related peptides, like thrombin, caused a prompt phasic reproducible contraction. The basic peptide, SFRGHITR, was inactive. In the LM assay, TRP42–55, TRP42–50 and A42-TRP42–55 all caused comparable contractile responses. We conclude that the gastric LM smooth muscle possesses a thrombin receptor and provides a convenient and reliable assay for the activities of thrombin receptor-related peptides. Our data also demonstrated that neither the C-terminal hirudin-related pentapeptide nor the N-terminal serine hydroxyl group are required for the biological activity of the thrombin receptor-derived peptide previously described (TRP42–55). Based on our findings we suggest that only a small portion of the N-terminal sequence of TRP42–55 may be required for thrombin-like biological activity." @default.
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- W2015336799 date "1992-01-01" @default.
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- W2015336799 title "Actions of thrombin and thrombin receptor peptide analogues in gastric and aortic smooth muscle: Development of bioassays for structure-activity studies" @default.
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- W2015336799 doi "https://doi.org/10.1016/0024-3205(92)90631-x" @default.
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