Aminopeptidase modulation of the pharmacological responses to synthetic thrombin receptor agonists.

@article{Godin1994AminopeptidaseMO,
  title={Aminopeptidase modulation of the pharmacological responses to synthetic thrombin receptor agonists.},
  author={Dominique Godin and François Marceau and Christian Beaul{\'e} and Frank Rioux and Guy Drapeau},
  journal={European journal of pharmacology},
  year={1994},
  volume={253 3},
  pages={225-30}
}
Thrombin is a contractile stimulus of isolated rabbit aortic rings and apparently produces its effects through the recently characterized cleavable receptor. A synthetic hexapeptide, NAT6-NH2 (new amino terminus), was found to be the minimal active structure for full activation of this receptor. The N-terminal Ser residue of NAT6-NH2 is crucial for biological activity. In this study we examined the metabolism of NAT6-NH2 in rabbit plasma, where it was rapidly degraded by aminopeptidase M. In… CONTINUE READING

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