Abstract
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.
MeSH terms
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Amino Acid Sequence
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Biological Transport / physiology
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Blotting, Western
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Cell Division / drug effects
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Cell Division / physiology
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Cell Extracts
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Cell Nucleus / metabolism*
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Cells, Cultured
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Cytoplasm / metabolism
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DNA-Activated Protein Kinase
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DNA-Binding Proteins*
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Fluorescent Antibody Technique
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Humans
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Immunoblotting
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Molecular Sequence Data
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Nuclear Proteins
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Phytohemagglutinins / pharmacology
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Precipitin Tests
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Protein Serine-Threonine Kinases / analysis
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Protein Serine-Threonine Kinases / isolation & purification
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Protein Serine-Threonine Kinases / metabolism*
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T-Lymphocytes / cytology*
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T-Lymphocytes / enzymology*
Substances
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Cell Extracts
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DNA-Binding Proteins
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Nuclear Proteins
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Phytohemagglutinins
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DNA-Activated Protein Kinase
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PRKDC protein, human
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Protein Serine-Threonine Kinases