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
. 1984 Jul;81(14):4307–4310. doi: 10.1073/pnas.81.14.4307

Cloned cDNA to cholecystokinin mRNA predicts an identical preprocholecystokinin in pig brain and gut.

U Gubler, A O Chua, B J Hoffman, K J Collier, J Eng
PMCID: PMC345577  PMID: 6205394

Abstract

Molecular cloning has established the structure of preprocholecystokinin in porcine cerebral cortex and duodenal mucosa. This precursor is 114 amino acids long, is identical in brain and gut, contains all the cholecystokinin (CCK) peptides previously isolated, and has the characteristics of a prohormone. It contains a putative amino-terminal signal peptide, basic processing sites, and a carboxyl-terminal amidation signal. The CCK mRNAs from brain and gut are approximately 850 nucleotides long and differ by only a few single base changes. This analysis establishes by a strict criterion that CCK is synthesized in both brain and gut and that the different distributions of molecular forms of CCK in the two tissues are most probably a consequence of tissue-specific posttranslational events.

Full text

PDF
4307

Images in this article

4309Image
on p.4309
4309Image
on p.4309

Selected References

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

  1. Bradbury A. F., Finnie M. D., Smyth D. G. Mechanism of C-terminal amide formation by pituitary enzymes. Nature. 1982 Aug 12;298(5875):686–688. doi: 10.1038/298686a0. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Deschenes R. J., Lorenz L. J., Haun R. S., Roos B. A., Collier K. J., Dixon J. E. Cloning and sequence analysis of a cDNA encoding rat preprocholecystokinin. Proc Natl Acad Sci U S A. 1984 Feb;81(3):726–730. doi: 10.1073/pnas.81.3.726. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dockray G. J., Gregory R. A., Hutchison J. B., Harris J. I., Runswick M. J. Isolation, structure and biological activity of two cholecystokinin octapeptides from sheep brain. Nature. 1978 Aug 17;274(5672):711–713. doi: 10.1038/274711a0. [DOI] [PubMed] [Google Scholar]
  5. Dockray G. J. Immunochemical evidence of cholecystokinin-like peptides in brain. Nature. 1976 Dec 9;264(5586):568–570. doi: 10.1038/264568a0. [DOI] [PubMed] [Google Scholar]
  6. Eng J., Shiina Y., Pan Y. C., Blacher R., Chang M., Stein S., Yalow R. S. Pig brain contains cholecystokinin octapeptide and several cholecystokinin desoctapeptides. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6381–6385. doi: 10.1073/pnas.80.20.6381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Eng J., Shiina Y., Straus E., Yalow R. S. Post-translational processing of cholecystokinin in pig brain and gut. Proc Natl Acad Sci U S A. 1982 Oct;79(19):6060–6064. doi: 10.1073/pnas.79.19.6060. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Hagenbüchle O., Bovey R., Young R. A. Tissue-specific expression of mouse-alpha-amylase genes: nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland. Cell. 1980 Aug;21(1):179–187. doi: 10.1016/0092-8674(80)90125-7. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Hoffmann W., Bach T. C., Seliger H., Kreil G. Biosynthesis of caerulein in the skin of Xenopus laevis: partial sequences of precursors as deduced from cDNA clones. EMBO J. 1983;2(1):111–114. doi: 10.1002/j.1460-2075.1983.tb01390.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Jorpes E., Mutt V. Cholecystokinin and pancreozymin, one single hormone? Acta Physiol Scand. 1966 Jan-Feb;66(1):196–202. doi: 10.1111/j.1748-1716.1966.tb03185.x. [DOI] [PubMed] [Google Scholar]
  14. Lamb R. A., Lai C. J. Sequence of interrupted and uninterrupted mRNAs and cloned DNA coding for the two overlapping nonstructural proteins of influenza virus. Cell. 1980 Sep;21(2):475–485. doi: 10.1016/0092-8674(80)90484-5. [DOI] [PubMed] [Google Scholar]
  15. Larsson L. I., Rehfeld J. F. Evidence for a common evolutionary origin of gastrin and cholecystokinin. Nature. 1977 Sep 22;269(5626):335–338. doi: 10.1038/269335a0. [DOI] [PubMed] [Google Scholar]
  16. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  17. McMaster G. K., Carmichael G. G. Analysis of single- and double-stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc Natl Acad Sci U S A. 1977 Nov;74(11):4835–4838. doi: 10.1073/pnas.74.11.4835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Miyoshi K., Arentzen R., Huang T., Itakura K. Solid-phase synthesis of polynucleotides. IV. Usage of polystyrene resins for the synthesis of polydeoxyribonucleotides by the phosphostriester method. Nucleic Acids Res. 1980 Nov 25;8(22):5507–5517. doi: 10.1093/nar/8.22.5507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Muller J. E., Straus E., Yalow R. S. Cholecystokinin and its COOH-terminal octapeptide in the pig brain. Proc Natl Acad Sci U S A. 1977 Jul;74(7):3035–3037. doi: 10.1073/pnas.74.7.3035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Norgard M. V., Tocci M. J., Monahan J. J. On the cloning of eukaryotic total poly(A)-RNA populations in Escherichia coli. J Biol Chem. 1980 Aug 25;255(16):7665–7672. [PubMed] [Google Scholar]
  21. Payvar F., Schimke R. T. Methylmercury hydroxide enhancement of translation and transcription of ovalbumin and conalbumin mRNA's. J Biol Chem. 1979 Aug 25;254(16):7636–7642. [PubMed] [Google Scholar]
  22. Peacock S. L., McIver C. M., Monahan J. J. Transformation of E. coli using homopolymer-linked plasmid chimeras. Biochim Biophys Acta. 1981 Sep 28;655(2):243–250. doi: 10.1016/0005-2787(81)90014-9. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Rehfeld J. F. Immunochemical studies on cholecystokinin. II. Distribution and molecular heterogeneity in the central nervous system and small intestine of man and hog. J Biol Chem. 1978 Jun 10;253(11):4022–4030. [PubMed] [Google Scholar]
  25. 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]
  26. Smith A. J. DNA sequence analysis by primed synthesis. Methods Enzymol. 1980;65(1):560–580. doi: 10.1016/s0076-6879(80)65060-5. [DOI] [PubMed] [Google Scholar]
  27. 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]
  28. Straus E., Yalow R. S. Species specificity of cholecystokinin in gut and brain of several mammalian species. Proc Natl Acad Sci U S A. 1978 Jan;75(1):486–489. doi: 10.1073/pnas.75.1.486. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. 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]
  30. Vanderhaeghen J. J., Signeau J. C., Gepts W. New peptide in the vertebrate CNS reacting with antigastrin antibodies. Nature. 1975 Oct 16;257(5527):604–605. doi: 10.1038/257604a0. [DOI] [PubMed] [Google Scholar]
  31. Yoo O. J., Powell C. T., Agarwal K. L. Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1049–1053. doi: 10.1073/pnas.79.4.1049. [DOI] [PMC free article] [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