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
. 1982 Sep;79(18):5485–5489. doi: 10.1073/pnas.79.18.5485

Neuropeptide Y: complete amino acid sequence of the brain peptide.

K Tatemoto
PMCID: PMC346928  PMID: 6957876

Abstract

The amino acid sequence of neuropeptide Y, a 36-residue peptide recently isolated from porcine brain, has been determined by using high performance liquid chromatography for separation of its tryptic and chymotryptic fragments and subsequent sequence analysis of the isolated fragments by an improved dansyl Edman subtractive technique. The amino acid sequence of neuropeptide Y has been found to be: Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-Glu-Asp-Ala-Pro-Ala-Glu-Asp-Leu-Ala-Arg-Tyr -Tyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-Thr-Arg-Gln-Arg-Tyr-NH2. Neuropeptide Y has a high degree of sequence homology with peptide YY (70%), the newly isolated porcine intestinal peptide, and pancreatic polypeptide (50%). It is therefore proposed that neuropeptide Y, peptide YY, and pancreatic polypeptide are members of a newly recognized peptide family.

Full text

PDF
5488

Selected References

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

  1. Bataille D., Gespach C., Laburthe M., Amiranoff B., Tatemoto K., Vauclin N., Mutt V., Rosselin G. Porcine peptide having N-terminal histidine and C-terminal isoleucine amide (PHI): vasoactive intestinal peptide (VIP) and secretin-like effects in different tissues from the rat. FEBS Lett. 1980 Jun 2;114(2):240–242. doi: 10.1016/0014-5793(80)81124-0. [DOI] [PubMed] [Google Scholar]
  2. Bodenmüller H., Schaller H. C. Conserved amino acid sequence of a neuropeptide, the head activator, from coelenterates to humans. Nature. 1981 Oct 15;293(5833):579–580. doi: 10.1038/293579a0. [DOI] [PubMed] [Google Scholar]
  3. Böhlen P., Brazeau P., Benoit R., Ling N., Esch F., Guillemin R. Isolation and amino acid composition of two somatostatin-like peptides from ovine hypothalamus: somatostatin-28 and somatostatin-25. Biochem Biophys Res Commun. 1980 Sep 30;96(2):725–734. doi: 10.1016/0006-291x(80)91415-1. [DOI] [PubMed] [Google Scholar]
  4. Carlquist M., Jörnvall H., Tatemoto K., Mutt V. A porcine brain polypeptide is identical to the vasoactive intestinal polypeptide. Gastroenterology. 1982 Jul;83(1 Pt 2):245–249. [PubMed] [Google Scholar]
  5. Carraway R., Kitabgi P., Leeman S. E. The amino acid sequence of radioimmunoassayable neurotensin from bovine intestine. J Biol Chem. 1978 Nov 25;253(22):7996–7998. [PubMed] [Google Scholar]
  6. Dimaline R., Dockray G. J. Actions of a new peptide from porcine intestine (PHI) on pancreatic secretion in the rat and turkey. Life Sci. 1980 Nov 24;27(21):1947–1951. doi: 10.1016/0024-3205(80)90413-0. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. GRAY W. R., HARTLEY B. S. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. doi: 10.1042/bj0890379. [DOI] [PubMed] [Google Scholar]
  9. Goldstein A., Fischli W., Lowney L. I., Hunkapiller M., Hood L. Porcine pituitary dynorphin: complete amino acid sequence of the biologically active heptadecapeptide. Proc Natl Acad Sci U S A. 1981 Nov;78(11):7219–7223. doi: 10.1073/pnas.78.11.7219. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hartley B. S. Strategy and tactics in protein chemistry. Biochem J. 1970 Oct;119(5):805–822. doi: 10.1042/bj1190805f. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jensen R. T., Tatemoto K., Mutt V., Lemp G. F., Gardner J. D. Actions of a newly isolated intestinal peptide PHI on pancreatic acini. Am J Physiol. 1981 Dec;241(6):G498–G502. doi: 10.1152/ajpgi.1981.241.6.G498. [DOI] [PubMed] [Google Scholar]
  12. Lorén I., Alumets J., Håkanson R., Sundler F. Immunoreactive pancreatic polypeptide (PP) occurs in the central and peripheral nervous system: preliminary immunocytochemical observations. Cell Tissue Res. 1979 Aug;200(2):179–186. doi: 10.1007/BF00236410. [DOI] [PubMed] [Google Scholar]
  13. Lundberg J. M., Hökfelt T., Anggård A., Kimmel J., Goldstein M., Markey K. Coexistence of an avian pancreatic polypeptide (APP) immunoreactive substance and catecholamine in some peripheral and central neurons. Acta Physiol Scand. 1980 Sep;110(1):107–109. doi: 10.1111/j.1748-1716.1980.tb06638.x. [DOI] [PubMed] [Google Scholar]
  14. Lundberg J. M., Tatemoto K., Terenius L., Hellström P. M., Mutt V., Hökfelt T., Hamberger B. Localization of peptide YY (PYY) in gastrointestinal endocrine cells and effects on intestinal blood flow and motility. Proc Natl Acad Sci U S A. 1982 Jul;79(14):4471–4475. doi: 10.1073/pnas.79.14.4471. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Olschowka J. A., O'Donohue T. L., Jacobowitz D. M. The distribution of bovine pancreatic polypeptide-like immunoreactive neurons in rat brain. Peptides. 1981 Fall;2(3):309–331. doi: 10.1016/s0196-9781(81)80125-8. [DOI] [PubMed] [Google Scholar]
  16. Pradayrol L., Jörnvall H., Mutt V., Ribet A. N-terminally extended somatostatin: the primary structure of somatostatin-28. FEBS Lett. 1980 Jan 1;109(1):55–58. doi: 10.1016/0014-5793(80)81310-x. [DOI] [PubMed] [Google Scholar]
  17. Schally A. V., Huang W. Y., Chang R. C., Arimura A., Redding T. W., Millar R. P., Hunkapiller M. W., Hood L. E. Isolation and structure of pro-somatostatin: a putative somatostatin precursor from pig hypothalamus. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4489–4493. doi: 10.1073/pnas.77.8.4489. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Szecówka J., Tatemoto K., Mutt V., Efendić S. Interaction of a newly isolated intestinal polypeptide (PHI) with glucose and arginine to effect the secretion of insulin and glucagon. Life Sci. 1980 Feb 11;26(6):435–438. doi: 10.1016/0024-3205(80)90162-9. [DOI] [PubMed] [Google Scholar]
  19. Tachibana S., Araki K., Ohya S., Yoshida S. Isolation and structure of dynorphin, an opioid peptide, from porcine duodenum. Nature. 1982 Jan 28;295(5847):339–340. doi: 10.1038/295339a0. [DOI] [PubMed] [Google Scholar]
  20. Tatemoto K., Carlquist M., Mutt V. Neuropeptide Y--a novel brain peptide with structural similarities to peptide YY and pancreatic polypeptide. Nature. 1982 Apr 15;296(5858):659–660. doi: 10.1038/296659a0. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. Tatemoto K., Mutt V. Chemical determination of polypeptide hormones. Proc Natl Acad Sci U S A. 1978 Sep;75(9):4115–4119. doi: 10.1073/pnas.75.9.4115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Tatemoto K., Mutt V. Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6603–6607. doi: 10.1073/pnas.78.11.6603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Tatemoto K., Mutt V. Isolation of two novel candidate hormones using a chemical method for finding naturally occurring polypeptides. Nature. 1980 Jun 5;285(5764):417–418. doi: 10.1038/285417a0. [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