Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 Oct;84(20):7005–7008. doi: 10.1073/pnas.84.20.7005

Sequence of an intestinal cDNA encoding human gastric inhibitory polypeptide precursor.

J Takeda 1, Y Seino 1, K Tanaka 1, H Fukumoto 1, T Kayano 1, H Takahashi 1, T Mitani 1, M Kurono 1, T Suzuki 1, T Tobe 1, et al.
PMCID: PMC299217  PMID: 2890159

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.

Full text

PDF
7006

Images in this article

7007Image
on p.7007

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andersen D. K., Elahi D., Brown J. C., Tobin J. D., Andres R. Oral glucose augmentation of insulin secretion. Interactions of gastric inhibitory polypeptide with ambient glucose and insulin levels. J Clin Invest. 1978 Jul;62(1):152–161. doi: 10.1172/JCI109100. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bause E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J. 1983 Feb 1;209(2):331–336. doi: 10.1042/bj2090331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bell G. I., Sanchez-Pescador R., Laybourn P. J., Najarian R. C. Exon duplication and divergence in the human preproglucagon gene. 1983 Jul 28-Aug 3Nature. 304(5924):368–371. doi: 10.1038/304368a0. [DOI] [PubMed] [Google Scholar]
  5. Bell G. I. The glucagon superfamily: precursor structure and gene organization. Peptides. 1986;7 (Suppl 1):27–36. doi: 10.1016/0196-9781(86)90160-9. [DOI] [PubMed] [Google Scholar]
  6. Benedum U. M., Baeuerle P. A., Konecki D. S., Frank R., Powell J., Mallet J., Huttner W. B. The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells. EMBO J. 1986 Jul;5(7):1495–1502. doi: 10.1002/j.1460-2075.1986.tb04388.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Brown J. C. A gastric inhibitory polypeptide. I. The amino acid composition and the tryptic peptides. Can J Biochem. 1971 Feb;49(2):255–261. doi: 10.1139/o71-037. [DOI] [PubMed] [Google Scholar]
  8. Brown J. C., Pederson R. A., Jorpes E., Mutt V. Preparation of highly active enterogastrone. Can J Physiol Pharmacol. 1969 Jan;47(1):113–114. doi: 10.1139/y69-020. [DOI] [PubMed] [Google Scholar]
  9. Carlquist M., Maletti M., Jörnvall H., Mutt V. A novel form of gastric inhibitory polypeptide (GIP) isolated from bovine intestine using a radioreceptor assay. Fragmentation with staphylococcal protease results in GIP1-3 and GIP4-42, fragmentation with enterokinase in GIP1-16 and GIP17-42. Eur J Biochem. 1984 Dec 17;145(3):573–577. doi: 10.1111/j.1432-1033.1984.tb08595.x. [DOI] [PubMed] [Google Scholar]
  10. Chirgwin J. M., Przybyla A. E., MacDonald R. J., Rutter W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry. 1979 Nov 27;18(24):5294–5299. doi: 10.1021/bi00591a005. [DOI] [PubMed] [Google Scholar]
  11. Dagert M., Ehrlich S. D. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene. 1979 May;6(1):23–28. doi: 10.1016/0378-1119(79)90082-9. [DOI] [PubMed] [Google Scholar]
  12. Dupre J., Ross S. A., Watson D., Brown J. C. Stimulation of insulin secretion by gastric inhibitory polypeptide in man. J Clin Endocrinol Metab. 1973 Nov;37(5):826–828. doi: 10.1210/jcem-37-5-826. [DOI] [PubMed] [Google Scholar]
  13. Gubler U., Monahan J. J., Lomedico P. T., Bhatt R. S., Collier K. J., Hoffman B. J., Böhlen P., Esch F., Ling N., Zeytin F. Cloning and sequence analysis of cDNA for the precursor of human growth hormone-releasing factor, somatocrinin. Proc Natl Acad Sci U S A. 1983 Jul;80(14):4311–4314. doi: 10.1073/pnas.80.14.4311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hanahan D., Meselson M. Plasmid screening at high colony density. Gene. 1980 Jun;10(1):63–67. doi: 10.1016/0378-1119(80)90144-4. [DOI] [PubMed] [Google Scholar]
  15. Hubbard S. C., Ivatt R. J. Synthesis and processing of asparagine-linked oligosaccharides. Annu Rev Biochem. 1981;50:555–583. doi: 10.1146/annurev.bi.50.070181.003011. [DOI] [PubMed] [Google Scholar]
  16. Iacangelo A., Affolter H. U., Eiden L. E., Herbert E., Grimes M. Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues. Nature. 1986 Sep 4;323(6083):82–86. doi: 10.1038/323082a0. [DOI] [PubMed] [Google Scholar]
  17. Ito H., Ike Y., Ikuta S., Itakura K. Solid phase synthesis of polynucleotides. VI. Further studies on polystyrene copolymers for the solid support. Nucleic Acids Res. 1982 Mar 11;10(5):1755–1769. doi: 10.1093/nar/10.5.1755. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Itoh N., Obata K., Yanaihara N., Okamoto H. Human preprovasoactive intestinal polypeptide contains a novel PHI-27-like peptide, PHM-27. Nature. 1983 Aug 11;304(5926):547–549. doi: 10.1038/304547a0. [DOI] [PubMed] [Google Scholar]
  19. Jörnvall H., Carlquist M., Kwauk S., Otte S. C., McIntosh C. H., Brown J. C., Mutt V. Amino acid sequence and heterogeneity of gastric inhibitory polypeptide (GIP). FEBS Lett. 1981 Jan 26;123(2):205–210. doi: 10.1016/0014-5793(81)80288-8. [DOI] [PubMed] [Google Scholar]
  20. Maxam A. M., Gilbert W. A new method for sequencing DNA. Proc Natl Acad Sci U S A. 1977 Feb;74(2):560–564. doi: 10.1073/pnas.74.2.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Maxwell V., Shulkes A., Brown J. C., Solomon T. E., Walsh J. H., Grossman M. I. Effect of gastric inhibitory polypeptide on pentagastrin-stimulated acid secretion in man. Dig Dis Sci. 1980 Feb;25(2):113–116. doi: 10.1007/BF01308308. [DOI] [PubMed] [Google Scholar]
  22. Mayo K. E., Vale W., Rivier J., Rosenfeld M. G., Evans R. M. Expression-cloning and sequence of a cDNA encoding human growth hormone-releasing factor. Nature. 1983 Nov 3;306(5938):86–88. doi: 10.1038/306086a0. [DOI] [PubMed] [Google Scholar]
  23. Moody A. J., Thim L., Valverde I. The isolation and sequencing of human gastric inhibitory peptide (GIP). FEBS Lett. 1984 Jul 9;172(2):142–148. doi: 10.1016/0014-5793(84)81114-x. [DOI] [PubMed] [Google Scholar]
  24. Noller H. F. Structure of ribosomal RNA. Annu Rev Biochem. 1984;53:119–162. doi: 10.1146/annurev.bi.53.070184.001003. [DOI] [PubMed] [Google Scholar]
  25. Okayama H., Berg P. High-efficiency cloning of full-length cDNA. Mol Cell Biol. 1982 Feb;2(2):161–170. doi: 10.1128/mcb.2.2.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Pederson R. A., Brown J. C. Inhibition of histamine-, pentagastrin-, and insulin-stimulated canine gastric secretion by pure "gastric inhibitory polypeptide". Gastroenterology. 1972 Mar;62(3):393–400. [PubMed] [Google Scholar]
  27. Pederson R. A., Brown J. C. The insulinotropic action of gastric inhibitory polypeptide in the perfused isolated rat pancreas. Endocrinology. 1976 Sep;99(3):780–785. doi: 10.1210/endo-99-3-780. [DOI] [PubMed] [Google Scholar]
  28. Pederson R. A., Schubert H. E., Brown J. C. Gastric inhibitory polypeptide. Its physiologic release and insulinotropic action in the dog. Diabetes. 1975 Dec;24(12):1050–1056. doi: 10.2337/diab.24.12.1050. [DOI] [PubMed] [Google Scholar]
  29. Perlman D., Halvorson H. O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol. 1983 Jun 25;167(2):391–409. doi: 10.1016/s0022-2836(83)80341-6. [DOI] [PubMed] [Google Scholar]
  30. Polak J. M., Bloom S. R., Kuzio M., Brown J. C., Pearse A. G. Cellular localization of gastric inhibitory polypeptide in the duodenum and jejunum. Gut. 1973 Apr;14(4):284–288. doi: 10.1136/gut.14.4.284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Proudfoot N. J., Brownlee G. G. 3' non-coding region sequences in eukaryotic messenger RNA. Nature. 1976 Sep 16;263(5574):211–214. doi: 10.1038/263211a0. [DOI] [PubMed] [Google Scholar]
  32. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  33. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Schwartz T. W. The processing of peptide precursors. 'Proline-directed arginyl cleavage' and other monobasic processing mechanisms. FEBS Lett. 1986 May 5;200(1):1–10. doi: 10.1016/0014-5793(86)80500-2. [DOI] [PubMed] [Google Scholar]
  35. Steiner D. F., Quinn P. S., Chan S. J., Marsh J., Tager H. S. Processing mechanisms in the biosynthesis of proteins. Ann N Y Acad Sci. 1980;343:1–16. doi: 10.1111/j.1749-6632.1980.tb47238.x. [DOI] [PubMed] [Google Scholar]
  36. Tatemoto K., Efendić S., Mutt V., Makk G., Feistner G. J., Barchas J. D. Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion. Nature. 1986 Dec 4;324(6096):476–478. doi: 10.1038/324476a0. [DOI] [PubMed] [Google Scholar]
  37. Thomas F. B., Shook D. F., O'Dorisio T. M., Cataland S., Mekhjian H. S., Caldwell J. H., Mazzaferri E. L. Localization of gastric inhibitory polypeptide release by intestinal glucose perfusion in man. Gastroenterology. 1977 Jan;72(1):49–54. [PubMed] [Google Scholar]
  38. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Winkler H. The composition of adrenal chromaffin granules: an assessment of controversial results. Neuroscience. 1976;1(2):65–80. doi: 10.1016/0306-4522(76)90001-4. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES