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Titolo:
Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins
Autore:
Tardif, S; Dube, C; Chevalier, S; Bailey, JL;
Indirizzi:
Univ Laval, Dept Anim Sci, Ctr Rech Biol Reprod, St Foy, PQ G1K 7P4, Canada Univ Laval St Foy PQ Canada G1K 7P4 ol Reprod, St Foy, PQ G1K 7P4, Canada McGill Univ, Montreal Gen Hosp, Inst Res, Div Urol Surg, Montreal, PQ H3G 1A4, Canada McGill Univ Montreal PQ Canada H3G 1A4 Surg, Montreal, PQ H3G 1A4, Canada McGill Univ, Dept Expt Med, Montreal, PQ H3G 1A4, Canada McGill Univ Montreal PQ Canada H3G 1A4 Med, Montreal, PQ H3G 1A4, Canada
Titolo Testata:
BIOLOGY OF REPRODUCTION
fascicolo: 3, volume: 65, anno: 2001,
pagine: 784 - 792
SICI:
0006-3363(200109)65:3<784:CIAWTP>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
EJACULATED BOAR SPERMATOZOA; CAMP-DEPENDENT PATHWAY; IN-VITRO; PLASMA-MEMBRANE; MOUSE SPERMATOZOA; ZONA-PELLUCIDA; BOVINE SPERM; INVITRO CAPACITATION; SIGNAL TRANSDUCTION; LIPID DIFFUSIBILITY;
Keywords:
gamete biology; kinases; signal transduction; sperm; sperm capacitation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Bailey, JL Univ Laval, Dept Anim Sci, Ctr Rech Biol Reprod, Pavillon Paul Comtois, StFoy, PQ G1K 7P4, Canada Univ Laval Pavillon Paul Comtois St Foy PQ Canada G1K 7P4 anada
Citazione:
S. Tardif et al., "Capacitation is associated with tyrosine phosphorylation and tyrosine kinase-like activity of pig sperm proteins", BIOL REPROD, 65(3), 2001, pp. 784-792

Abstract

Capacitation represents the final maturational steps that render mammaliansperm competent to fertilize, either in vivo or in vitro. Capacitation is defined as a series of events that enables sperm to bind the oocyte and undergo the acrosome reaction in response to the zona pellucida. Although the molecular mechanisms involved are not fully understood, sperm protein phosphorylation is associated with capacitation. The hypothesis of this study isthat protein tyrosine phosphorylation and kinase activity mediate capacitation of porcine sperm. Fresh sperm were incubated in noncapacitating or capacitating media for various times. Proteins were extracted with SDS, subjected to SDS-PAGE, and immunoblotted with an antiphosphotyrosine antibody. AnM-r 32 000 tyrosine-phosphorylated protein (designated as p32) appeared only when the sperm were incubated in capacitating medium and concomitant with capacitation as assessed by the ionophore-induced acrosome reaction. The p32 was soluble in Triton X-100. Fractionation of sperm proteins with Triton X-114 demonstrated that after capacitation, this tyrosine phosphoprotein is located in both the cytosol and the membrane. Enzyme renaturation of sperm proteins was conducted in gels with or without either poly glu:tyr (a tyrosine kinase substrate) or kemptide (a protein kinase A substrate). An M, 32 000 enzyme with kinase behavior was observed in all gels but was preferentially phosphorylated on tyrosine, as assessed by phosphorimagery and by thin layer chromotography to identify the phosphoamino acids. Indirect immunolocalization showed that the phosphotyrosine residues redistribute to the acrosome during capacitation, which is an appropriate location for a protein involved in the acquisition of fertility.

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Documento generato il 29/11/20 alle ore 02:29:12