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. 1995 Jan 17;92(2):594–598. doi: 10.1073/pnas.92.2.594

Seminalplasmin: recent evolution of another member of the neuropeptide Y gene family.

H Herzog 1, Y Hort 1, R Schneider 1, J Shine 1
PMCID: PMC42788  PMID: 7831336

Abstract

Seminalplasmin, the major basic protein of bull semen, an important regulator of calcium transport in bovine sperm and a positive modulator of the zona pellucida-induced acrosome reaction, is shown to be a recently created member of the neuropeptide Y gene family. Sequence analysis of the bovine peptide YY-pancreatic polypeptide gene cluster reveals an unexpected and extensive homology between seminalplasmin and the neuropeptide Y gene family, at the level of both gene structure and primary amino acid and nucleotide sequences. The extremely high degree of homology to the peptide YY gene, in both coding and especially noncoding regions, suggests that the seminalplasmin gene has arisen by a very recent gene duplication of the bovine peptide YY gene. Despite the more than 95% nucleotide sequence identity, a few specific mutations in the seminalplasmin gene have resulted in both the loss of the amino- and carboxyl-terminal cleavage sites characteristic of all other members of the neuropeptide Y family and the acquisition of a function apparently unrelated to the neurotransmitter/endocrine role of peptide YY.

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Selected References

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

  1. Clark E. N., Corron M. E., Florman H. M. Caltrin, the calcium transport regulatory peptide of spermatozoa, modulates acrosomal exocytosis in response to the egg's zona pellucida. J Biol Chem. 1993 Mar 5;268(7):5309–5316. [PubMed] [Google Scholar]
  2. Comte M., Malnoë A., Cox J. A. Affinity purification of seminalplasmin and characterization of its interaction with calmodulin. Biochem J. 1986 Dec 1;240(2):567–573. doi: 10.1042/bj2400567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dumont Y., Martel J. C., Fournier A., St-Pierre S., Quirion R. Neuropeptide Y and neuropeptide Y receptor subtypes in brain and peripheral tissues. Prog Neurobiol. 1992;38(2):125–167. doi: 10.1016/0301-0082(92)90038-g. [DOI] [PubMed] [Google Scholar]
  4. Florman H. M., Corron M. E., Kim T. D., Babcock D. F. Activation of voltage-dependent calcium channels of mammalian sperm is required for zona pellucida-induced acrosomal exocytosis. Dev Biol. 1992 Aug;152(2):304–314. doi: 10.1016/0012-1606(92)90137-6. [DOI] [PubMed] [Google Scholar]
  5. Heilig M., Widerlöv E. Neuropeptide Y: an overview of central distribution, functional aspects, and possible involvement in neuropsychiatric illnesses. Acta Psychiatr Scand. 1990 Aug;82(2):95–114. doi: 10.1111/j.1600-0447.1990.tb01366.x. [DOI] [PubMed] [Google Scholar]
  6. Jingami H., Mizuno N., Takahashi H., Shibahara S., Furutani Y., Imura H., Numa S. Cloning and sequence analysis of cDNA for rat corticotropin-releasing factor precursor. FEBS Lett. 1985 Oct 21;191(1):63–66. doi: 10.1016/0014-5793(85)80994-7. [DOI] [PubMed] [Google Scholar]
  7. Kuhlmann J. K., Scheit K. H. Characterization of the gene for seminalplasmin, a secretory protein of the bovine seminal vesicle. Biochim Biophys Acta. 1993 Apr 29;1173(1):85–86. doi: 10.1016/0167-4781(93)90248-c. [DOI] [PubMed] [Google Scholar]
  8. Larhammar D., Blomqvist A. G., Söderberg C. Evolution of neuropeptide Y and its related peptides. Comp Biochem Physiol C. 1993 Nov;106(3):743–752. doi: 10.1016/0742-8413(93)90236-e. [DOI] [PubMed] [Google Scholar]
  9. Leiter A. B., Toder A., Wolfe H. J., Taylor I. L., Cooperman S., Mandel G., Goodman R. H. Peptide YY. Structure of the precursor and expression in exocrine pancreas. J Biol Chem. 1987 Sep 25;262(27):12984–12988. [PubMed] [Google Scholar]
  10. Lewis R. V., Agustin J. S., Kruggel W., Lardy H. A. The structure of caltrin, the calcium-transport inhibitor of bovine seminal plasma. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6490–6491. doi: 10.1073/pnas.82.19.6490. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Maurer T., Rüterjans H. Solution structure of seminal plasmin in the presence of micelles. Eur J Biochem. 1994 Feb 15;220(1):111–116. doi: 10.1111/j.1432-1033.1994.tb18604.x. [DOI] [PubMed] [Google Scholar]
  12. Reddy E. S., Bhargava P. M. Seminalplasmin--an antimicrobial protein from bovine seminal plasma which acts in E. coli by specific inhibition of rRNA synthesis. Nature. 1979 Jun 21;279(5715):725–728. doi: 10.1038/279725a0. [DOI] [PubMed] [Google Scholar]
  13. Taylor I. L., Solomon T. E., Walsh J. H., Grossman M. I. Pancreatic polypeptide. Metabolism and effect on pancreatic secretion in dogs. Gastroenterology. 1979 Mar;76(3):524–528. [PubMed] [Google Scholar]

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