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Titolo:
ACTIVATION OF PKC-ALPHA DOWNSTREAM FROM CASPASES DURING APOPTOSIS INDUCED BY 7-HYDROXYSTAUROSPORINE OR THE TOPOISOMERASE INHIBITORS, CAMPTOTHECIN AND ETOPOSIDE, IN HUMAN MYELOID-LEUKEMIA HL60 CELLS
Autore:
SHAO RG; CAO CX; POMMIER Y;
Indirizzi:
NCI,MOL PHARMACOL LAB,DIV BASIC SCI,NIH,BLDG 37,RM 5C25 BETHESDA MD 20892 NCI,MOL PHARMACOL LAB,DIV BASIC SCI,NIH BETHESDA MD 20892
Titolo Testata:
The Journal of biological chemistry
fascicolo: 50, volume: 272, anno: 1997,
pagine: 31321 - 31325
SICI:
0021-9258(1997)272:50<31321:AOPDFC>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; DNA FRAGMENTATION; HL-60 CELLS; THYMOCYTE APOPTOSIS; SELECTIVE INHIBITOR; ANTITUMOR-ACTIVITY; ICE-LIKE; IN-VIVO; INDUCTION; UCN-01;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
R.G. Shao et al., "ACTIVATION OF PKC-ALPHA DOWNSTREAM FROM CASPASES DURING APOPTOSIS INDUCED BY 7-HYDROXYSTAUROSPORINE OR THE TOPOISOMERASE INHIBITORS, CAMPTOTHECIN AND ETOPOSIDE, IN HUMAN MYELOID-LEUKEMIA HL60 CELLS", The Journal of biological chemistry, 272(50), 1997, pp. 31321-31325

Abstract

We previously demonstrated that the anticancer agent and protein kinase C (PKC) inhibitor 7-hydroxy-staurosporine (UCN-01) induces apoptosis independently of p53 and protein synthesis in HL60 cells, We now report the associated changes of PKC isoforms, PKC alpha, beta I, beta II, delta, and zeta activities were measured after immunoprecipitation of cytosols from UCN-01-treated HL60 cells. UCN-01 had no effect on PKCzeta and inhibited kinase activity of PKC beta I, beta II, and delta. PKC alpha activity was initially inhibited at 1 h, and subsequently increased as cells underwent apoptosis 3 h after the beginning of UCN-01 treatment, Camptothecin (CPT) and etoposide (VP-16) also markedly enhanced PKC alpha activity during apoptosis in HL60 cells. However, CPTdid not affect PKC beta I, beta II and zeta, and activated PKC delta,PKC alpha activation was not due to increased protein levels or proteolytic cleavage but was associated with PKC alpha autophosphorylation in vitro and increased phosphorylation in vivo, We also found that notonly PKC delta but also PKC beta I was proteolytically activated in HL60 cells during apoptosis. The PKC alpha activation and hyperphosphorylation were abrogated by carbonyl-Val-Ala-Asp(O-methyl)-fluoro-methylketone (z-VAD-fmk) under conditions that abrogated apoptosis, z-VAD-fmk also prevented PKC delta and beta I proteolytic activation, Togetherthese findings suggest that caspases regulate PKC activity during apoptosis in HL60 cells, At least two modes of activation were observed: hyperphosphorylation for PKC alpha and proteolytic activation for PKC delta and beta I.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 22:38:15