PMID: 10819763May 20, 2000Paper

Protein tyrosine phosphorylation during prolonged in vitro incubation of ejaculated bovine spermatozoa is regulated by the oxidative state of the medium

Biology of Reproduction
J KrzyzosiakR Vishwanath


Protein tyrosine phosphorylation plays a regulatory role in a multitude of physiological processes in sperm. Changes in protein tyrosine phosphorylation, viability, and motility were studied as a function of extended incubation of bovine sperm in vitro at ambient temperature (18-20 degrees C). Fresh ejaculates were incubated after dilution for 8 days. On Days 0, 2, 5, and 8, an aliquot of sperm was incubated with or without theophylline at 37 degrees C for 30 min prior to assessing sperm viability, motility, and tyrosine phosphorylation of soluble and whole-cell proteins. There was a time-dependent decline in sperm motility, which was to some extent reversed by incubation with theophylline. The sum of the phosphotyrosine signal from two soluble proteins (M(r) 67 000 and 36 000) declined with incubation time in both theophylline-treated and untreated sperm. There were major differences in the pattern of tyrosine phosphorylation during incubation between ejaculates from different bulls. Tyrosine phosphorylation of a number of proteins from whole-cell extracts increased in a time-dependent manner during in vitro incubation and was unaffected by the presence of theophylline in the medium. The oxygenation state of the incubation med...Continue Reading


May 1, 1989·Journal of Reproduction and Fertility·K AshizawaK Okauchi
Jul 1, 1983·Journal of Reproduction and Fertility·J W BaasP Shannon
Mar 1, 1982·Fertility and Sterility·A I TraubW Thompson
Feb 1, 1993·Free Radical Biology & Medicine·E de Lamirande, C Gagnon
Feb 1, 1993·International Journal of Andrology·E de Lamirande, C Gagnon
Jan 1, 1997·Reproduction, Fertility, and Development·R Vishwanath, P Shannon

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