Sequence of an Intestinal CDNA Encoding Human Gastric Inhibitory Polypeptide Precursor

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1987 Oct 1

PMID 2890159

Citations 24

Authors

J Takeda

Y Seino

K Tanaka

H Fukumoto

T Kayano

H Takahashi

T Mitani

M Kurono

T Suzuki

T Tobe

Affiliations

Soon will be listed here.

Abstract

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.

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