Borgstrom A, Wider M, Marks W, Lloyd R, Herman G, Vinik A
Histochemistry. 1986;86(1):101-5. doi: 10.1007/BF00492352.
The tissue distribution of a polypeptide purified from pig ileal mucosa tentatively called porcine ileal polypeptide (PIP) and known to have potent acid secretagogue activity has been studied with immunohistochemical methods together with extraction of different tissues followed by radioimmunoassay for PIP content. Histochemically the peptide is found in superficial epithelial cells in the mucosa of the distal 20% of the small intestine and to some extent in the mucosa of the urinary tract. There is no staining of goblet cells or crypt cells. The staining in the urinary tract mucosa is due to antigenic peptides with Mr identical to PIP. While the presence of PIP in the ileum is compatible with a function as an enterooxyntin, it is not possible at present to explain the physiologic role of PIP entirely as a hormone regulating acid secretion in light of the immunohistochemical distribution.
从猪回肠黏膜中纯化出一种多肽，暂称为猪回肠多肽（PIP），已知其具有强大的促胃酸分泌活性。本研究采用免疫组化方法，并对不同组织进行提取，随后通过放射免疫分析法测定PIP含量，以研究该多肽的组织分布。组织化学研究发现，该肽存在于小肠远端20%黏膜的表层上皮细胞中，在一定程度上也存在于泌尿道黏膜中。杯状细胞或隐窝细胞无染色。泌尿道黏膜中的染色是由于分子量与PIP相同的抗原性肽所致。虽然回肠中存在PIP与作为肠泌酸素的功能相符，但根据免疫组化分布，目前尚无法完全解释PIP作为调节胃酸分泌的激素的生理作用。
