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Titolo:
Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
Autore:
Visconti, PE; Ning, XP; Fornes, MW; Alvarez, JG; Stein, P; Connors, SA; Kopf, GS;
Indirizzi:
Univ Penn, Med Ctr, Ctr Res Reprod & Womens Hlth, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 mens Hlth, Philadelphia, PA 19104 USA Univ Penn, Med Ctr, Dept Biol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Dept Biol, Philadelphia, PA 19104 USA Harvard Univ, Sch Med, Beth Israel Deaconess Med Ctr, Dept Obstet & Gynecol, Boston, MA 02215 USA Harvard Univ Boston MA USA 02215 t Obstet & Gynecol, Boston, MA 02215 USA Univ Penn, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Dev Biol, Philadelphia, PA 19104 USA
Titolo Testata:
DEVELOPMENTAL BIOLOGY
fascicolo: 2, volume: 214, anno: 1999,
pagine: 429 - 443
SICI:
0012-1606(19991015)214:2<429:CESTIM>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
FILIPIN-STEROL COMPLEXES; HIGH-DENSITY-LIPOPROTEIN; CAMP-DEPENDENT PATHWAY; ACROSOME REACTION; HUMAN SPERMATOZOA; PLASMA-MEMBRANE; INTRAMEMBRANOUS PARTICLES; INVITRO CAPACITATION; HAMSTER SPERMATOZOA; PHOSPHOLIPID RATIO;
Keywords:
mouse; sperm; capacitation; cholesterol; cAMP; protein tyrosine phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Visconti, PE Univ Virginia, Dept Cell Biol & Anat, Charlottesville, VA 22903 USA Univ Virginia Charlottesville VA USA 22903 lle, VA 22903 USA
Citazione:
P.E. Visconti et al., "Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation", DEVELOP BIO, 214(2), 1999, pp. 429-443

Abstract

We previously demonstrated that mouse sperm capacitation is accompanied bya time-dependent increase in protein tyrosine phosphorylation that is dependent on the presence of BSA, Ca2+, and NaHCO3, all three of which are alsorequired for this maturational event. We also demonstrated that activationof protein kinase A (PK-A) is upstream of this capacitation-associated increase in protein tyrosine phosphorylation. BSA is hypothesized to modulate capacitation through the removal of cholesterol from the sperm plasma membrane. In this report, we demonstrate that incubation of mouse sperm medium containing BSA results in a release of cholesterol from the sperm plasma membrane to the medium; release of this sterol does not occur in medium devoidof BSA. We next determined whether cholesterol release leads to changes inprotein tyrosine phosphorylation. Blocking the action of BSA by adding exogenous cholesterol-SO4- to the BSA-containing medium inhibits the increase in protein tyrosine phosphorylation as well as capacitation. This inhibitory effect is overcome by (1) the addition of increasing concentrations of BSA at a given concentration of cholesterol-SO4- and (2) the addition of dibutyryl cAMP plus IBMX. High-density lipoprotein (HDL), another cholesterol binding protein, also supports the capacitation-associated increase in protein tyrosine phosphorylation through a cAMP-dependent pathway, whereas proteins that do not interact with cholesterol have no effect. HDL also supportssperm capacitation, as assessed by fertilization in vitro. Finally, we previously demonstrated that HCO3- is necessary for the capacitation-associated increase in protein tyrosine phosphorylation and demonstrate here, by examining the effectiveness of HCO3- or BSA addition to sperm on protein tyrosine phosphorylation, that the HCO3- effect is downstream of the site of BSAaction. Taken together, these data demonstrate that cholesterol release isassociated with the activation of a transmembrane signal transduction pathway involving PK-A and protein tyrosine phosphorylation, leading to functional maturation of the sperm. (C) 1999 Academic Press.

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Documento generato il 28/11/20 alle ore 03:48:36