Nuclear Translocation of the Catalytic Component of DNA-dependent Protein Kinase upon Growth Stimulation in Normal Human T Lymphocytes.

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  • Nagasawa Masayuki
    Department of Pediatrics, School of Medicine, Tokyo Medical and Dental University
  • Watanabe Fumiaki
    Department of Pathological Biochemistry, Medical Research Institute, Tokyo Medical and Dental University
  • Suwa Akira
    Division of Rheumatic Diseases, Tokyo Metropolitan Ohtsuka Hospital
  • Yamamoto Kohtaro
    Department of Virology and Immunology, Medical Research Institute, Tokyo Medical and Dental University
  • Tsukada Kinji
    Department of Pathological Biochemistry, Medical Research Institute, Tokyo Medical and Dental University
  • Teraoka Hirobumi
    Department of Pathological Biochemistry, Medical Research Institute, Tokyo Medical and Dental University

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  • Nuclear Translocation of the Catalytic

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DNA-dependent protein kinase (DNA-PK), consisting of the 470-kDa catalytic component (DNA-PKcs) and the DNA-binding regulatory component Ku protein (p70/p80), catalyzes phosphorylation of a variety of DNA replication/transcription/repair factors in the presence of double-stranded DNA. In the resting states of human peripheral blood mononuclear cells, DNA-PK activity and the protein level of DNA-PKcs were very low in the nuclear extracts, but they were high in the whole cell extracts. Depending upon proliferation of the T lymphocytes, DNA-PK activity and the protein level of DNA-PKcs in the nuclear extracts greatly increased. Immunocytochemical analysis suggested translocation of DNA-PKcs from the cytoplasm to the nucleus upon growth stimulation in the T lymphocytes.

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