Organ distribution and characterization of porcine peptides (VIP, CGRP and PHI) that increase cAMP in rat platelets
- 30 September 1992
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 187 (3) , 1587-1593
- https://doi.org/10.1016/0006-291x(92)90484-3
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Isolation and characterization of peptides which act on rat platelets, from a pheochromocytomaBiochemical and Biophysical Research Communications, 1992
- Isolation of NPY-25 (neuropeptide Y[12–36]), a potent inhibitor of calmodulin, from porcine brainBiochemical and Biophysical Research Communications, 1990
- Isolation of a novel 38 residue-hypothalamic polypeptide which stimulates adenylate cyclase in pituitary cellsBiochemical and Biophysical Research Communications, 1989
- Biochemical mechanisms of platelet activationBlood, 1989
- Effects of TRK-100, a stable prostacyclin analogue, on regulation of cyclic AMP metabolism in plateletsProstaglandins, 1989
- Neuropeptide control of thyroid blood flow and hormone secretion in the ratLife Sciences, 1986
- VIP elevates platelet cyclic AMP (cAMP) levels and inhibits in vitro platelet activation induced by platelet-activating factor (PAF)Peptides, 1984
- Human preprovasoactive intestinal polypeptide contains a novel PHI-27-like peptide, PHM-27Nature, 1983