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Title: Prolactin-releasing activity of porcine intestinal peptide (PHI-27). Author: Samson WK, Lumpkin MD, McDonald JK, McCann SM. Journal: Peptides; 1983; 4(6):817-9. PubMed ID: 6689504. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]