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Regulation Of Na,K-Atpase Activity By Tyrosine Phosphorylation In Lens Cells., Larry Darko Bozulic 1974-
Regulation Of Na,K-Atpase Activity By Tyrosine Phosphorylation In Lens Cells., Larry Darko Bozulic 1974-
Electronic Theses and Dissertations
Na,K-ATPase is essential for the regulation of cytoplasmic Na+ and K+ levels in lens cells. Insufficient Na,K-ATPase activity is associated with cataract formation. Based on earlier studies in which Src-tyrosine kinase inhibitors were found to suppress Na,K-ATPase activity changes that occur in response to either thrombin, endothelin, or dopamine, I hypothesize that regulation of Na,K-ATPase activity might occur through phosphorylation of the Na,K-ATPase a1 (catalytic) subunit by Src-family tyrosine kinases. Here, I tested the influence of Src-kinase family members on tyrosine phosphorylation and Na,K-ATPase activity in membrane material isolated from porcine lens epithelium. Western blot studies indicated the expression of …
Tyrosine Phosphorylation Of Hsp-90 During Mammalian Sperm Capacitation, Heath W. Ecroyd, Russell C. Jones, Robert J. Aitken
Tyrosine Phosphorylation Of Hsp-90 During Mammalian Sperm Capacitation, Heath W. Ecroyd, Russell C. Jones, Robert J. Aitken
Faculty of Science - Papers (Archive)
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 …
Endogenous Redox Activity In Mouse Spermatozoa And Its Role In Regulating The Tyrosine Phosphorylation Events Associated With Sperm Capacitation, Heath W. Ecroyd, Russell C. Jones, Robert J. Aitken
Endogenous Redox Activity In Mouse Spermatozoa And Its Role In Regulating The Tyrosine Phosphorylation Events Associated With Sperm Capacitation, Heath W. Ecroyd, Russell C. Jones, Robert J. Aitken
Faculty of Science - Papers (Archive)
We investigated the role of endogenous redox activity in regulating the signal transduction pathway leading to tyrosine phosphorylation in mouse spermatozoa. Endogenous redox activity was monitored using a luminol-peroxidase chemiluminescent probe. Chemiluminescence increased in spermatozoa that were actively undergoing cAMP-mediated tyrosine phosphorylation events associated with capacitation and was inhibited in a dose-dependent manner by addition of catalase or diphenylene iodonium, both of which also inhibited tyrosine phosphorylation within the cell at points downstream of cAMP. Excluding bicarbonate from the incubation medium reduced the redox activity of sperm by 80-90% and dramatically reduced tyrosine phosphorylation. This study provides the first evidence …