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Titolo:
LAMIN-B PHOSPHORYLATION BY PROTEIN-KINASE-C-ALPHA AND PROTEOLYSIS DURING APOPTOSIS IN HUMAN LEUKEMIA HL60 CELLS
Autore:
SHIMIZU T; CAO CX; SHAO RG; POMMIER Y;
Indirizzi:
NCI,MOL PHARMACOL LAB,DIV BASIC SCI,NIH,BLDG 37,RM 5D02 BETHESDA MD 20892 NCI,MOL PHARMACOL LAB,DIV BASIC SCI,NIH BETHESDA MD 20892
Titolo Testata:
The Journal of biological chemistry
fascicolo: 15, volume: 273, anno: 1998,
pagine: 8669 - 8674
SICI:
0021-9258(1998)273:15<8669:LPBPAP>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
TOPOISOMERASE-II INHIBITORS; ISOLATED THYMOCYTE NUCLEI; DNA FRAGMENTATION; HL-60 CELLS; POLY(ADP-RIBOSE) POLYMERASE; ICE/CED-3 PROTEASE; ACTIVATION; DEGRADATION; INDUCTION; DEATH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
T. Shimizu et al., "LAMIN-B PHOSPHORYLATION BY PROTEIN-KINASE-C-ALPHA AND PROTEOLYSIS DURING APOPTOSIS IN HUMAN LEUKEMIA HL60 CELLS", The Journal of biological chemistry, 273(15), 1998, pp. 8669-8674

Abstract

Protein phosphorylation plays an important role in signal transduction, but its involvement in apoptosis still remains unclear. In this report, the p53-null human leukemia HL60 cells were used to investigate phosphorylation and degradation of lamin B during apoptosis. We found that lamin B was phosphorylated within I h after addition of the DNA topoisomerase I inhibitor, camptothecin, and that lamin B phosphorylation preceded lamin B degradation and DNA fragmentation. Using a cell-free system we also found that cytosol from camptothecin-treated cells induced lamin B phosphorylation and degradation in isolated nuclei from untreated HL60 cells. Lamin B phosphorylation was prevented by the protein kinase C (PKC) inhibitor 7-hydroxystaurosporine (UCN-01) but not by the Cdc2 inhibitor, flavopiridol. Phosphorylation of lamin B was inhibited by immunodepletion of PKC alpha from activated cytosol and wasrestored by addition of purified PKC alpha. PKC alpha activity also increased rapidly as lamin B was phosphorylated after initiation of theapoptotic response in HL60 cells. These data suggest that lamin B is phosphorylated by PKC alpha and proteolyzed before DNA fragmentation in HL60 cells undergoing apoptosis.

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Documento generato il 20/09/20 alle ore 08:00:13