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Rat PHI, PHI-GLY and PHV(1-42) stimulate adenylate cyclase in six rat tissue and cell membranes

par Cauvin, Annick ;Vandermeers-Piret, Marie-Claire ;Vandermeers, André ;Coussaert, Edouard ;De Neef, Philippe ;Robberecht, Patrick ;Christophe, Jean
Référence Peptides, 11, 5, page (1009-1014)
Publication Publié, 1990

Article révisé par les pairs

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Résumé :

PHI and the two C-terminally extended forms PHI-GLY and PHV(1-42) coexist in rat tissues. We compared the relative potency and efficacy of these three PHI forms and of VIP to stimulate adenylate cyclase activity and, when feasible, to occupy VIP receptors in six rat tissue and cell membranes. With the exception of lung membranes, all three PHI forms were markedly less potent than VIP but all were systematically as efficacious. PHI-GLY and PHV(1-42) were never more potent than PHI itself and their relative potencies revealed four spectra, depending on the membrane preparation tested: 1) PHI = PHI-GLY = PHV(1-42) in hepatic, pulmonary and pancreatic membranes; 2) PHI > PHV(1-42) = PHI-GLY in membranes from circulating lymphocytes; 3) PHI = PHV(1-42) > PHI-GLY in membranes from teh thymocyte cell line 51E; and 4) PHI > PHI-GLY = PHV(1-42) in anterior pituitary membranes. These results indicate that the two naturally observed C-terminal extensions of rat PHI variously affected peptide potency on 6 rat membrane preparations.