猪肠道肽（PHI-27）的催乳素释放活性。

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

作者信息

Samson W K, Lumpkin M D, McDonald J K, McCann S M

出版信息

Peptides. 1983 Nov-Dec;4(6):817-9. doi: 10.1016/0196-9781(83)90073-6.

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.

摘要

猪肠肽（PHI）是一种从猪肠道提取物中分离出的含27个氨基酸的肽，是促胰液素家族激素的紧密结构同源物。PHI与血管活性肠肽（VIP）在结构和生物学上的相似性，以及它在大鼠下丘脑的存在，提示该肽在催乳素（PRL）分泌的控制中可能发挥作用。在体外，PHI能显著地、剂量依赖性地刺激培养的分散大鼠垂体细胞释放PRL。最小有效剂量为10^(-7)摩尔，而VIP为10^(-9)摩尔。未观察到与促甲状腺激素释放激素的相互作用；然而，PHI部分克服了多巴胺对PRL释放的抑制作用。