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Titolo:
Phosphorylation of Bcl-2 and Bax proteins during hypoxia in newborn piglets
Autore:
Ashraf, QM; Zanelli, SA; Mishra, OP; Delivoria-Papadopoulos, M;
Indirizzi:
Med Coll Penn & Hahnemann Univ, Dept Pediat, Philadelphia, PA 19129 USA Med Coll Penn & Hahnemann Univ Philadelphia PA USA 19129 ia, PA 19129 USA St Christophers Hosp Children, Philadelphia, PA 19133 USA St Christophers Hosp Children Philadelphia PA USA 19133 hia, PA 19133 USA
Titolo Testata:
NEUROCHEMICAL RESEARCH
fascicolo: 1, volume: 26, anno: 2001,
pagine: 1 - 9
SICI:
0364-3190(200101)26:1<1:POBABP>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROGRAMMED CELL-DEATH; GUINEA-PIG BRAIN; FOCAL CEREBRAL-ISCHEMIA; GERBIL HIPPOCAMPUS; DNA FRAGMENTATION; RAT-BRAIN; IN-VIVO; FOREBRAIN ISCHEMIA; TRANSIENT ISCHEMIA; GLOBAL-ISCHEMIA;
Keywords:
Bax; Bcl-2; phosphorylation; hypoxia; newborn brain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Ashraf, QM Med Coll Penn & Hahnemann Univ, Dept Pediat Neonatol, 3300 Henry Ave,7th Floor,Room 701, Philadelphia, PA 19129 USA Med Coll Penn & Hahnemann Univ 3300 Henry Ave,7th Floor,Room 701 Philadelphia PA USA 19129
Citazione:
Q.M. Ashraf et al., "Phosphorylation of Bcl-2 and Bax proteins during hypoxia in newborn piglets", NEUROCHEM R, 26(1), 2001, pp. 1-9

Abstract

Studies indicate that phosphorylated Bcl-2 cannot form a heterodimer with Bar and thus may lose its antiapoptotic potential. The present study tests:the hypothesis that graded hypoxia in cerebral tissue induces the phosphorylation of Bcl-2, thus altering the heterodimerization of Bcl-2 with Fax and subsequently leading to apoptosis. Anesthetized, ventilated newborn piglets were assigned to a normoxic and a graded hypoxic group. Cerebral cortical neuronal nuclei were isolated and immunoprecipitated; immune complexes were separated and reacted with Bcl-2 and Bar specific antibodies. The results show an increased level of serine/tyrosine phosphorylated Bcl-2 in nuclear membranes of hypoxic animals. The level of phosphorylated Bcl-2 protein increased linearly with decrease in tissue PCr. The level of phosphorylated Bar in the neuronal nuclear membranes was independent of cerebral tissue PCr. The data shows that during hypoxia, there is increased phosphorylation of Bcl-2, which may prevent its: heterodimerization with Bar and lead to increased proapoptotic activity due to excess Bar in the hypoxic brain. Further increased phosphorylation of Bcl-2 may alter the Bcl-2/Bax-dependent antioxidant, lipid peroxidation and pore forming activity, as well as the regulation of intranuclear Ca2+ and caspase activation pathways. We speculate that increased phosphorylation of Bcl-2 in neuronal nuclear membranes is a potential mechanism of programmed cell death activation in the hypoxic brain.

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Documento generato il 26/09/20 alle ore 05:41:24