Demonstration of a double-stranded DNA-stimulated protein kinase (DNA-PK) inhibitory activity in human HL-60 leukemia cells.
A 41,000 protein, p41, was highly purified from human promyelocytic HL-60 cells by chromatography on GTP-agarose columns. The purified p41 inhibited phosphorylation of endogenous substrates present in partially purified DNA-PK from HL-60 or HeLa cells, as well as phosphorylation of recombinant protein tau mediated by the purified HeLa DNA-PK. The ability of p41 to inhibit DNA-PK was largely abolished by heating at 95 degrees C for 30 min.
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Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla 10595.
Chen
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Wu
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Wu
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JM
D002846:Chromatography, Affinity; D004247:DNA / Q000502:physiology*; D051747:DNA-Activated Protein Kinase; D004268:DNA-Binding Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D006367:HeLa Cells; D006801:Humans; D009687:Nuclear Proteins; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors*; D011506:Proteins / Q000302:isolation & purification / Q000502:physiology*; D014407:Tumor Cells, Cultured
D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D011506:Proteins; D004247:DNA; D051747:DNA-Activated Protein Kinase; C497263:PRKDC protein, human; D017346:Protein Serine-Threonine Kinases