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Tyrosine Phosphorylation Of Hsp-90 During Mammalian Sperm Capacitation, Heath Ecroyd, Russell Jones, Robert Aitken
Tyrosine Phosphorylation Of Hsp-90 During Mammalian Sperm Capacitation, Heath Ecroyd, Russell Jones, Robert Aitken
Heath Ecroyd
The process of sperm capacitation is correlated with activation of a signal transduction pathway leading to protein tyrosine phosphorylation. Whereas phosphotyrosine expression is an essential prerequisite for fertilization, the proteins that are phosphorylated during capacitation have not yet been identified. In the present study, we observed that a major target of this signaling pathway is the molecular chaperone protein, heat shock protein (HSP)-86, a member of the HSP-90 family of HSPs. We used cross-immunoprecipitation experiments to confirm the tyrosine phosphorylation of HSP-86, a process that is not inhibited by the ansamycin antibiotic, geldanamycin. The general significance of these findings was …
The Development Of Signal Transduction Pathways During Epididymal Maturation Is Calcium Dependent, Heath W. Ecroyd, Kelly Asquith, Russell C. Jones, Robert J. Aitken
The Development Of Signal Transduction Pathways During Epididymal Maturation Is Calcium Dependent, Heath W. Ecroyd, Kelly Asquith, Russell C. Jones, Robert J. Aitken
Heath Ecroyd
Capacitation has been correlated with the activation of a cAMP-PKA-dependent signaling pathway leading to protein tyrosine phosphorylation. The ability to exhibit this response to cAMP matures during epididymal maturation in concert with the ability of the sperrnatozoa to capacitate. In this study, we have addressed the mechanisms by which spermatozoa gain the potential to activate this signaling pathway during epididymal maturation. In a modified Tyrode's medium containing 1.7 mM calcium, caput spermatozoa had significantly higher [Ca2+](i) than caudal cells and could not tyrosine phosphorylate in response to cAMP. However, in calcium-depleted medium both caput and caudal cells could exhibit a …