Skip to main content
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 Feb;84(4):959–962. doi: 10.1073/pnas.84.4.959

Gonadotropin-releasing peptide from human follicular fluid: isolation, characterization, and chemical synthesis.

C H Li, K Ramasharma, D Yamashiro, D Chung
PMCID: PMC304339  PMID: 3547404

Abstract

A gonadotropin-releasing peptide has been isolated from human follicular fluid. Its amino acid composition and sequence are completely different from the hypothalamic lutropin-releasing hormone. It is designated human follicular gonadotropin-releasing peptide and abbreviated as hF-GRP. The primary structure of this peptide (H-Thr-Asp-Thr-Ser-His-His-Asp-Gln-Asp-His-Pro-Thr-Phe-Asn-OH) has been confirmed by chemical synthesis. In the mouse pituitary incubation assay, the ED50 value for follitropin or lutropin release is estimated to be 1.2-1.6 nM.

Full text

PDF
959

Selected References

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

  1. Bollen A., Herzog A., Cravador A., Hérion P., Chuchana P., Vander Straten A., Loriau R., Jacobs P., van Elsen A. Cloning and expression in Escherichia coli of full-length complementary DNA coding for human alpha 1-antitrypsin. DNA. 1983;2(4):255–264. doi: 10.1089/dna.1983.2.255. [DOI] [PubMed] [Google Scholar]
  2. Carrell R. W., Jeppsson J. O., Laurell C. B., Brennan S. O., Owen M. C., Vaughan L., Boswell D. R. Structure and variation of human alpha 1-antitrypsin. Nature. 1982 Jul 22;298(5872):329–334. doi: 10.1038/298329a0. [DOI] [PubMed] [Google Scholar]
  3. Chen E. Y., Howley P. M., Levinson A. D., Seeburg P. H. The primary structure and genetic organization of the bovine papillomavirus type 1 genome. Nature. 1982 Oct 7;299(5883):529–534. doi: 10.1038/299529a0. [DOI] [PubMed] [Google Scholar]
  4. Chrétien M., Seidah N. G. Precursor polyproteins in endocrine and neuroendocrine systems. Int J Pept Protein Res. 1984 Apr;23(4):335–341. doi: 10.1111/j.1399-3011.1984.tb02728.x. [DOI] [PubMed] [Google Scholar]
  5. Douglass J., Civelli O., Herbert E. Polyprotein gene expression: generation of diversity of neuroendocrine peptides. Annu Rev Biochem. 1984;53:665–715. doi: 10.1146/annurev.bi.53.070184.003313. [DOI] [PubMed] [Google Scholar]
  6. Hagenmaier H., Frank H. Increased coupling yields in solid phase peptide synthesis with a modified carbodiimide coupling procedure. Hoppe Seylers Z Physiol Chem. 1972 Dec;353(12):1973–1976. [PubMed] [Google Scholar]
  7. Kurachi K., Chandra T., Degen S. J., White T. T., Marchioro T. L., Woo S. L., Davie E. W. Cloning and sequence of cDNA coding for alpha 1-antitrypsin. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6826–6830. doi: 10.1073/pnas.78.11.6826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. König W., Geiger R. Eine neue Methode zur Synthese von Peptiden: Aktivierung der Carboxylgruppe mit Dicyclohexycarbodiimid unter Zusatz von 1-Hydroxy-benzotriazolen. Chem Ber. 1970;103(3):788–798. doi: 10.1002/cber.19701030319. [DOI] [PubMed] [Google Scholar]
  9. Ling N., Ying S. Y., Ueno N., Shimasaki S., Esch F., Hotta M., Guillemin R. Pituitary FSH is released by a heterodimer of the beta-subunits from the two forms of inhibin. Nature. 1986 Jun 19;321(6072):779–782. doi: 10.1038/321779a0. [DOI] [PubMed] [Google Scholar]
  10. Millar R. P., Wormald P. J., Milton R. C. Stimulation of gonadotropin release by a non-GnRH peptide sequence of the GnRH precursor. Science. 1986 Apr 4;232(4746):68–70. doi: 10.1126/science.3082009. [DOI] [PubMed] [Google Scholar]
  11. Ramasharma K., Sairam M. R., Ranganathan M. R. Effect of inhibin like factors on gonadotrophin release by the mouse pituitary in vitro. Acta Endocrinol (Copenh) 1981 Dec;98(4):496–505. doi: 10.1530/acta.0.0980496. [DOI] [PubMed] [Google Scholar]
  12. Rivier J., Spiess J., McClintock R., Vaughan J., Vale W. Purification and partial characterization of inhibin from porcine follicular fluid. Biochem Biophys Res Commun. 1985 Nov 27;133(1):120–127. doi: 10.1016/0006-291x(85)91849-2. [DOI] [PubMed] [Google Scholar]
  13. Seeburg P. H., Adelman J. P. Characterization of cDNA for precursor of human luteinizing hormone releasing hormone. Nature. 1984 Oct 18;311(5987):666–668. doi: 10.1038/311666a0. [DOI] [PubMed] [Google Scholar]
  14. 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]
  15. Vale W., Rivier J., Vaughan J., McClintock R., Corrigan A., Woo W., Karr D., Spiess J. Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid. Nature. 1986 Jun 19;321(6072):776–779. doi: 10.1038/321776a0. [DOI] [PubMed] [Google Scholar]
  16. Yamashiro D., Li C. H., Ramasharma K., Sairam M. R. Synthesis and biological activity of human inhibin-like peptide-(1-31). Proc Natl Acad Sci U S A. 1984 Sep;81(17):5399–5402. doi: 10.1073/pnas.81.17.5399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ying S. Y., Becker A., Baird A., Ling N., Ueno N., Esch F., Guillemin R. Type beta transforming growth factor (TGF-beta) is a potent stimulator of the basal secretion of follicle stimulating hormone (FSH) in a pituitary monolayer system. Biochem Biophys Res Commun. 1986 Mar 28;135(3):950–956. doi: 10.1016/0006-291x(86)91020-x. [DOI] [PubMed] [Google Scholar]
  18. Ying S. Y., Ling N., Böhlen P., Guillemin R. Gonadocrinins: peptides in ovarian follicular fluid stimulating the secretion of pituitary gonadotropins. Endocrinology. 1981 Apr;108(4):1206–1215. doi: 10.1210/endo-108-4-1206. [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