Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation

It has long been known that seminal plasma contains factors that influence the fertilizing capacity of spermatozoa in many different ways. However, little is understood of the biochemical cascades triggered when spermatozoa and seminal plasma interact. In this study, we examined how incubation with...

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Bibliographic Details
Published in:Molecular human reproduction 1998, Vol.4 (1), p.17-25
Main Authors: TOMES, C. N, CARBALLADA, R, MOSES, D. F, KATZ, D. F, SALING, P. M
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cell Survival
Fundamental and applied biological sciences. Psychology
Humans
Male
Mammalian male genital system
Morphology. Physiology
Phosphorylation
Phosphotyrosine - analysis
Proteins - metabolism
Semen - metabolism
Sperm Motility
Spermatozoa - chemistry
Spermatozoa - cytology
Spermatozoa - metabolism
Vertebrates: reproduction
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Summary:It has long been known that seminal plasma contains factors that influence the fertilizing capacity of spermatozoa in many different ways. However, little is understood of the biochemical cascades triggered when spermatozoa and seminal plasma interact. In this study, we examined how incubation with seminal plasma affected protein tyrosine phosphorylation in human spermatozoa. Increased protein tyrosine phosphorylation is a hallmark of sperm capacitation in several mammalian species, including human. Seminal plasma blocks protein tyrosine phosphorylation when added to washed, non-capacitated spermatozoa. Removal of seminal plasma and incubation in capacitating medium led to partial recovery of the tyrosine phosphorylation cascade. Addition of seminal plasma to a suspension of spermatozoa previously incubated for 5 h under capacitating conditions decreased the level of tyrosine phosphorylation on all proteins in a dose-dependent manner. In this case, the phosphotyrosine signal did not increase upon removal of seminal plasma followed by overnight incubation in fresh capacitating media, indicating that removal of seminal plasma was necessary but not sufficient for protein tyrosine phosphorylation to occur. These results indicate that human seminal plasma contains factors that influence the tyrosine phosphorylation status of human spermatozoa.
ISSN:1360-9947
1460-2407
1460-2407
DOI:10.1093/molehr/4.1.17