Prolactin-releasing activity of porcine intestinal peptide (PHI-27)

Porcine intestinal peptide (PHI), a twenty-seven amino acid peptide isolated from porcine gut extracts, is a close structural homolog of the secretin family hormones. The structural and biological similarities of PHI to vasoactive intestinal peptide (VIP) together with its presence in the rat hypoth...

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Veröffentlicht in:Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1983-11, Vol.4 (6), p.817-819
Hauptverfasser: Samson, W.K., Lumpkin, M.D., McDonald, J.K., McCann, S.M.
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Sprache:eng
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Zusammenfassung:Porcine intestinal peptide (PHI), a twenty-seven amino acid peptide isolated from porcine gut extracts, is a close structural homolog of the secretin family hormones. The structural and biological similarities of PHI to vasoactive intestinal peptide (VIP) together with its presence in the rat hypothalamus suggested a possible role for the peptide in the control of prolactin (PRL) secretion. PHI induced significant, dose-related stimulations of PRL release from cultured, dispersed rat pituitary cells in vitro. The minimum effective dose is 10 7 molar, compared to 10 9 molar for VIP. No interactive effect with thyrotropin-releasing hormone was observed; however, PHI partially overcame the dopamine inhibition of PRL release.
ISSN:0196-9781
1873-5169
DOI:10.1016/0196-9781(83)90073-6