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 |
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Format: | Artikel |
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. |
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ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/0196-9781(83)90073-6 |