title: Demonstration of a double-stranded DNA-stimulated protein kinase (DNA-PK) inhibitory activity in human HL-60 leukemia cells.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla 10595.
authors.forename: S
authors.initials: S
authors.lastname: An
authors.forename: Y
authors.initials: Y
authors.lastname: Chen
authors.forename: W
authors.initials: W
authors.lastname: Wu
authors.forename: J M
authors.initials: JM
authors.lastname: Wu
mesh_terms: 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
chemical_list: 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