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Biology of reproduction1994; 50(4); 912-916; doi: 10.1095/biolreprod50.4.912

Platelet-activating factor acetylhydrolase activity in seminal plasma from the bull, stallion, rabbit, and rooster.

Abstract: Platelet-activating factor (PAF) acetylhydrolase, which inactivates PAF, has been detected in human and bovine seminal plasma and may represent a mechanism for regulating sperm-derived PAF. This study was designed to characterize further PAF acetylhydrolase in seminal plasma from domestic animal species. Sperm-free seminal plasma from the bull, stallion, rabbit, and rooster was assayed for acetylhydrolase activity based on the release of [3H]acetate from PAF. As reported previously for bull seminal plasma, activity in stallion, rabbit, and rooster seminal plasma was linear with both time and protein concentration, with specific activities of 97.4, 1.2, and 0.33 nmol PAF hydrolyzed/mg protein/min, respectively. Activity in seminal plasma from the bull, rabbit, and rooster was calcium-independent whereas activity in stallion seminal plasma increased with added calcium (p < 0.01). Addition of EDTA partially inhibited acetylhydrolase activity in stallion seminal plasma but increased the specific activity in rabbit seminal plasma (p or = 60 degrees C). Very little activity was associated with bull seminal plasma lipoproteins isolated by KBr flotation or by precipitation with polyanions. These results demonstrate that PAF acetylhydrolase activity is present in seminal plasma from different species, with large differences in specific activity among species. These differences may be related to species differences in the physiological role of PAF and its regulation in sperm and male tract fluids.
Publication Date: 1994-04-01 PubMed ID: 8199270DOI: 10.1095/biolreprod50.4.912Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.

Summary

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This research explores the activity of platelet-activating factor acetylhydrolase, a compound that deactivates platelet-activating factor, in the seminal plasma of different domestic animal species such as bulls, stallions, rabbits, and roosters. It reveals that the degree of activity differs across species and could relate to each species’ unique physiological needs and the regulation of sperm.

Study Design and Methodology

  • The study was carried out with sperm-free seminal plasma from four different animal species: bull, stallion, rabbit, and rooster.
  • The researchers tested for acetylhydrolase activity by using the release of [3H]acetate from Platelet-Activating Factor (PAF) as a marker.
  • They measured this enzyme’s activity using time and protein concentration, yielding specific activities measured in nanomoles (nmol) of PAF hydrolyzed per milligram (mg) of protein per minute (min).

Findings and Observations

  • It was found that the enzyme activity in bull, stallion, rabbit, and rooster seminal plasma was proportional with time and protein concentration. The magnitude of the enzyme’s specific activity differed among these species, with bulls showing the highest activity.
  • Further, the enzyme activity in bull, rabbit, and rooster seminal plasma was observed to be independent of calcium, while in stallion seminal plasma, activity increased with added calcium.
  • The enzyme activity in these plasmas also showed varying responses to the addition of EDTA, a chelating agent that binds to metals in solutions. Inaction of acetylhydrolase increased in rabbit seminal plasma but decreased in stallion plasma with the addition of EDTA.
  • In terms of stability, the enzyme activity in bull seminal plasma was nondialyzable, stable at pH 5.0, and it became inactive or heat-labile under high temperatures (60 degrees Celsius or above).

Conclusions

  • The results show that PAF acetylhydrolase activity is present in the seminal plasma of different animal species, but its activity level and reaction to various conditions vary among species.
  • The observed differences might be related to individual species’ physiological requirements and how sperm is regulated in their male reproductive fluids.

Cite This Article

APA
Hough SR, Parks JE. (1994). Platelet-activating factor acetylhydrolase activity in seminal plasma from the bull, stallion, rabbit, and rooster. Biol Reprod, 50(4), 912-916. https://doi.org/10.1095/biolreprod50.4.912

Publication

ISSN: 0006-3363
NlmUniqueID: 0207224
Country: United States
Language: English
Volume: 50
Issue: 4
Pages: 912-916

Researcher Affiliations

Hough, S R
  • Department of Animal Science, Cornell University, Ithaca, New York 14853.
Parks, J E

    MeSH Terms

    • 1-Alkyl-2-acetylglycerophosphocholine Esterase
    • Acetates / metabolism
    • Animals
    • Calcium / pharmacology
    • Cattle
    • Chickens
    • Dialysis
    • Edetic Acid / pharmacology
    • Horses
    • Hydrogen-Ion Concentration
    • Male
    • Phospholipases A / metabolism
    • Platelet Activating Factor / metabolism
    • Rabbits
    • Semen / enzymology
    • Species Specificity

    Citations

    This article has been cited 2 times.
    1. Tomaszkiewicz M, Chalopin D, Schartl M, Galiana D, Volff JN. A multicopy Y-chromosomal SGNH hydrolase gene expressed in the testis of the platyfish has been captured and mobilized by a Helitron transposon. BMC Genet 2014 Apr 8;15:44.
      doi: 10.1186/1471-2156-15-44pubmed: 24712907google scholar: lookup
    2. Soubeyrand S, Lazure C, Manjunath P. Phospholipase A2 from bovine seminal plasma is a platelet-activating factor acetylhydrolase. Biochem J 1998 Jan 1;329 ( Pt 1)(Pt 1):41-7.
      doi: 10.1042/bj3290041pubmed: 9405273google scholar: lookup