Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1986 Nov 15;240(1):69–74. doi: 10.1042/bj2400069

Cat pancreatic eicosapeptide and its biosynthetic intermediate. Conservation of a monobasic processing site.

H V Nielsen, U Gether, T W Schwartz
PMCID: PMC1147377  PMID: 3827854

Abstract

Pancreatic eicosapeptide is synthesized together with the hormone pancreatic polypeptide in a common precursor in the major endocrine cell type of the duodenal pancreas. This processing has been previously demonstrated in man and in the dog. In the present study the cat pancreatic eicosapeptide and a C-terminally extended form of this were isolated and characterized from acid/ethanol extracts of pancreas by gel filtration and reverse-phase h.p.l.c. The sequence homology in the C-terminal part of the eicosapeptides from different species was shown to continue to the other side of the monobasic cleavage site in the extended intermediate form, whereas the end of the extension differed both in chain length and amino acid sequence. It is concluded that the processing site in the intermediate form of the pancreatic eicosapeptide is an example of a proline-directed monobasic cleavage site that has been conserved during evolution.

Full text

PDF
69

Selected References

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

  1. Boel E., Schwartz T. W., Norris K. E., Fiil N. P. A cDNA encoding a small common precursor for human pancreatic polypeptide and pancreatic icosapeptide. EMBO J. 1984 Apr;3(4):909–912. doi: 10.1002/j.1460-2075.1984.tb01904.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bostian K. A., Elliott Q., Bussey H., Burn V., Smith A., Tipper D. J. Sequence of the preprotoxin dsRNA gene of type I killer yeast: multiple processing events produce a two-component toxin. Cell. 1984 Mar;36(3):741–751. doi: 10.1016/0092-8674(84)90354-4. [DOI] [PubMed] [Google Scholar]
  3. Cone R. I., Weber E., Barchas J. D., Goldstein A. Regional distribution of dynorphin and neo-endorphin peptides in rat brain, spinal cord, and pituitary. J Neurosci. 1983 Nov;3(11):2146–2152. doi: 10.1523/JNEUROSCI.03-11-02146.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hayashi R., Bai Y., Hata T. Kinetic studies of carboxypeptidase Y. I. Kinetic parameters for the hydrolysis of synthetic substrates. J Biochem. 1975 Jan 1;77(1?):69–79. [PubMed] [Google Scholar]
  5. Heinrikson R. L., Meredith S. C. Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate. Anal Biochem. 1984 Jan;136(1):65–74. doi: 10.1016/0003-2697(84)90307-5. [DOI] [PubMed] [Google Scholar]
  6. Hudson P., Haley J., John M., Cronk M., Crawford R., Haralambidis J., Tregear G., Shine J., Niall H. Structure of a genomic clone encoding biologically active human relaxin. Nature. 1983 Feb 17;301(5901):628–631. doi: 10.1038/301628a0. [DOI] [PubMed] [Google Scholar]
  7. Hunkapiller M. W., Hewick R. M., Dreyer W. J., Hood L. E. High-sensitivity sequencing with a gas-phase sequenator. Methods Enzymol. 1983;91:399–413. doi: 10.1016/s0076-6879(83)91038-8. [DOI] [PubMed] [Google Scholar]
  8. Hunkapiller M. W., Hood L. E. Analysis of phenylthiohydantoins by ultrasensitive gradient high-performance liquid chromatography. Methods Enzymol. 1983;91:486–493. doi: 10.1016/s0076-6879(83)91045-5. [DOI] [PubMed] [Google Scholar]
  9. Kangawa K., Tawaragi Y., Oikawa S., Mizuno A., Sakuragawa Y., Nakazato H., Fukuda A., Minamino N., Matsuo H. Identification of rat gamma atrial natriuretic polypeptide and characterization of the cDNA encoding its precursor. Nature. 1984 Nov 8;312(5990):152–155. doi: 10.1038/312152a0. [DOI] [PubMed] [Google Scholar]
  10. Leiter A. B., Keutmann H. T., Goodman R. H. Structure of a precursor to human pancreatic polypeptide. J Biol Chem. 1984 Dec 10;259(23):14702–14705. [PubMed] [Google Scholar]
  11. Leiter A. B., Montminy M. R., Jamieson E., Goodman R. H. Exons of the human pancreatic polypeptide gene define functional domains of the precursor. J Biol Chem. 1985 Oct 25;260(24):13013–13017. [PubMed] [Google Scholar]
  12. Matsuo H., Miyata A., Mizuno K. Novel C-terminally amidated opioid peptide in human phaeochromocytoma tumour. Nature. 1983 Oct 20;305(5936):721–723. doi: 10.1038/305721a0. [DOI] [PubMed] [Google Scholar]
  13. Minth C. D., Bloom S. R., Polak J. M., Dixon J. E. Cloning, characterization, and DNA sequence of a human cDNA encoding neuropeptide tyrosine. Proc Natl Acad Sci U S A. 1984 Jul;81(14):4577–4581. doi: 10.1073/pnas.81.14.4577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nakanishi S., Inoue A., Kita T., Nakamura M., Chang A. C., Cohen S. N., Numa S. Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor. Nature. 1979 Mar 29;278(5703):423–427. doi: 10.1038/278423a0. [DOI] [PubMed] [Google Scholar]
  15. Nawa H., Hirose T., Takashima H., Inayama S., Nakanishi S. Nucleotide sequences of cloned cDNAs for two types of bovine brain substance P precursor. Nature. 1983 Nov 3;306(5938):32–36. doi: 10.1038/306032a0. [DOI] [PubMed] [Google Scholar]
  16. Reeve J. R., Jr, Walsh J. H., Chew P., Clark B., Hawke D., Shively J. E. Amino acid sequences of three bombesin-like peptides from canine intestine extracts. J Biol Chem. 1983 May 10;258(9):5582–5588. [PubMed] [Google Scholar]
  17. Schwartz T. W., Gingerich R. L., Tager H. S. Biosynthesis of pancreatic polypeptide. Identification of a precursor and a co-synthesized product. J Biol Chem. 1980 Dec 10;255(23):11494–11498. [PubMed] [Google Scholar]
  18. Schwartz T. W., Hansen H. F., Håkanson R., Sundler F., Tager H. S. Human pancreatic icosapeptide: isolation, sequence, and immunocytochemical localization of the COOH-terminal fragment of the pancreatic polypeptide precursor. Proc Natl Acad Sci U S A. 1984 Feb;81(3):708–712. doi: 10.1073/pnas.81.3.708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Schwartz T. W., Hansen H. F. Isolation of ovine pancreatic icosapeptide: a peptide product containing one cysteine residue. FEBS Lett. 1984 Mar 26;168(2):293–298. doi: 10.1016/0014-5793(84)80265-3. [DOI] [PubMed] [Google Scholar]
  20. Schwartz T. W. Pancreatic polypeptide: a hormone under vagal control. Gastroenterology. 1983 Dec;85(6):1411–1425. [PubMed] [Google Scholar]
  21. Schwartz T. W., Tager H. S. Isolation and biogenesis of a new peptide from pancreatic islets. Nature. 1981 Dec 10;294(5841):589–591. doi: 10.1038/294589a0. [DOI] [PubMed] [Google Scholar]
  22. 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]
  23. Steiner D. F., Kemmler W., Tager H. S., Peterson J. D. Proteolytic processing in the biosynthesis of insulin and other proteins. Fed Proc. 1974 Oct;33(10):2105–2115. [PubMed] [Google Scholar]
  24. Takeuchi T., Yamada T. Isolation of a cDNA clone encoding pancreatic polypeptide. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1536–1539. doi: 10.1073/pnas.82.5.1536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Tatemoto K. Isolation and characterization of peptide YY (PYY), a candidate gut hormone that inhibits pancreatic exocrine secretion. Proc Natl Acad Sci U S A. 1982 Apr;79(8):2514–2518. doi: 10.1073/pnas.79.8.2514. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tatemoto K. Neuropeptide Y: complete amino acid sequence of the brain peptide. Proc Natl Acad Sci U S A. 1982 Sep;79(18):5485–5489. doi: 10.1073/pnas.79.18.5485. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Vlasak R., Kreil G. Nucleotide sequence of cloned cDNAs coding for preprosecapin, a major product of queen-bee venom glands. Eur J Biochem. 1984 Dec 3;145(2):279–282. doi: 10.1111/j.1432-1033.1984.tb08549.x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES