Mdm-2 and Ubiquitin-Independent p53 Proteasomal Degradation Regulated by NQO1

The tumor suppressor p53 is a labile protein whose level is known to be regulated by the Mdm-2-ubiquitin-proteasome degradation pathway. We have found another pathway for p53 proteasomal degradation regulated by NAD(P)H quinone oxidoreductase 1 (NQO1). Inhibition of NQO1 activity by dicoumarol induc...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2002-10, Vol.99 (20), p.13125-13130
Hauptverfasser:	Asher, Gad, Lotem, Joseph, Sachs, Leo, Kahana, Chaim, Shaul, Yosef
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoptosis Biological Sciences Cell Line Cell lines COS Cells Cultured cells Cysteine Endopeptidases - metabolism DNA-Binding Proteins - metabolism Gene Expression Regulation Genes, Tumor Suppressor HCT116 cells Humans Immunoblotting Medical research Mice Mice, Inbred BALB C Multienzyme Complexes - metabolism Mutation NAD(P)H Dehydrogenase (Quinone) NADPH Dehydrogenase Nuclear Proteins - metabolism Oncogenes Plasmids - metabolism Polymorphism, Genetic Proteasome Endopeptidase Complex Protein Binding Proteins Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-mdm2 Quinone Reductases - chemistry Quinone Reductases - genetics Quinone Reductases - metabolism Reticulocytes Reticulocytes - metabolism Temperature Time Factors Transfection Tumor Cells, Cultured Tumor Protein p73 Tumor Suppressor Protein p14ARF - metabolism Tumor Suppressor Protein p53 - metabolism Tumor Suppressor Proteins Tumors Ubiquitin - metabolism Ubiquitins
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