Grace D. Moore

TL;DR: Caput epididymal sperm, which lack the ability to undergo capacitation in vitro, do not display this capacitation-dependent subset of tyrosine phosphorylated proteins in complete media even after extended incubation periods, and do not fertilize metaphase II-arrested eggs in vitro.

TL;DR: Up-regulation of protein tyrosine phosphorylation by cAMP/PKA in sperm is, to the authors' knowledge, the first demonstration of such an interrelationship between tyrosin kinase/phosphatase and PKA signaling pathways.

TL;DR: β-cyclodextrins can completely replace BSA in media to support signal transduction leading to capacitation, further support the coupling of cholesterol efflux to theactivation of membrane and transmembrane signaling events leading to the activation of a unique signaling pathway involving the cross-talk between cAMP and tyrosine kinase second messenger systems.

TL;DR: A brief review will consider some of the recent findings made toward an understanding of capacitation using in vitro models and offers an offer of an exhaustive analysis of this important event.

TL;DR: Preventing the fertilization-induced decrease in MAP kinase activity was correlated with inhibiting pronucleus formation, and elevating MAPKinase activity subsequent to pron nucleus formation resulted in precocious pronuclear envelope breakdown prior to entry into M phase.