Takeda J, Seino Y, Tanaka K, Fukumoto H, Kayano T, Takahashi H, Mitani T, Kurono M, Suzuki T, Tobe T
Department of Internal Medicine, Kyoto University School of Medicine, Japan.
Proc Natl Acad Sci U S A. 1987 Oct;84(20):7005-8. doi: 10.1073/pnas.84.20.7005.
Gastric inhibitory polypeptide (GIP) is a 42-amino acid hormone that stimulates insulin secretion in the presence of glucose. Complementary DNA clones encoding human GIP were isolated from a library prepared with RNA from duodenum. The predicted amino acid sequence indicates that GIP is derived by proteolytic processing of a 153-residue precursor, preproGIP. The GIP moiety is flanked by polypeptide segments of 51 and 60 amino acids at its NH2 and COOH termini, respectively. The former includes a signal peptide of about 21 residues and an NH2-terminal propeptide of 30 amino acids. GIP is released from the precursor by processing at single arginine residues. There is a region of nine amino acids in the COOH-terminal propeptide of the GIP precursor that has partial homology with a portion of chromogranin A as well as pancreastatin.
胃抑制性多肽（GIP）是一种由42个氨基酸组成的激素，在有葡萄糖存在的情况下可刺激胰岛素分泌。从用十二指肠RNA制备的文库中分离出编码人GIP的互补DNA克隆。预测的氨基酸序列表明，GIP是由153个残基的前体即前胰高血糖素原经蛋白水解加工而来。GIP部分在其NH2和COOH末端分别由51个和60个氨基酸的多肽片段侧翼。前者包括一个约21个残基的信号肽和一个30个氨基酸的NH2末端前肽。GIP通过在单个精氨酸残基处加工从前体中释放出来。GIP前体的COOH末端前肽中有一个由九个氨基酸组成的区域，与嗜铬粒蛋白A以及胰抑制素的一部分有部分同源性。
