Tryptase inhibits motility of human spermatozoa mainly by activation of the mitogen-activated protein kinase pathway

Autor: E. Wunn, R. Hollweck, Johannes Ring, Lars Kunz, Frank-Michael Köhn, M. Sbornik, Artur Mayerhofer, Stephan Weidinger, Martin Albrecht
Rok vydání: 2005
Předmět:
Zdroj: Human Reproduction. 20:456-461
ISSN: 1460-2350
0268-1161
DOI: 10.1093/humrep/deh618
Popis: BACKGROUND: We previously localized protease-activated receptor 2 (PAR-2) on human spermatozoa and demonstrated that activation of PAR-2 by the mast cell (MC) product tryptase inhibits sperm motility. Importantly, tryptase-secreting MCs are encountered in the male and female genital tract, implying that MC-spermatozoa interactions may be as yet unrecognized factors affecting sperm fertilizing ability. In order to elucidate how tryptase via activation of PAR-2 acts in human spermatozoa, we studied intracellular signal transduction events. METHODS AND RESULTS: Impairment of sperm motility by tryptase was not dependent on the presence of extracellular Ca 2+ and tryptase did not alter intracellular Ca 2+ levels. Pre-incubation with pertussis toxin (PTX) failed to prevent tryptase effects on sperm motility. Western blot analyses revealed that tryptase increased phosphorylation of the mitogen-activated protein kinases (MAPK) ERK1/2, an effect which was blocked by the MAPK pathway inhibitor PD98059. Pre-treatment of spermatozoa with this inhibitor also blocked the inhibtion of sperm motility evoked by tryptase. CONCLUSIONS: These results indicate that tryptase acts via the ERK1/2 pathway to inhibit motility of human spermatozoa.
Databáze: OpenAIRE