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RAPID ALTERATIONS IN PROTEIN KINASE C ACTIVITY AND INTRACELLULAR DISTRIBUTION DURING PHORBOL ESTER-INDUCED HL-60 CELL MICROPHAGE-LIKE DIFFERENTIATION
作者姓名:邵国英  刘城高  Samuel Waxman
作者单位:Department of Biochemistry,SSMU,Shanghai,Division of Medical Oncology,Mount Sinai School of Medicine of the City University of New York,New York,Division of Medical Oncology,Mount Sinai School of Medicine of the City University of New York,New York
摘    要:Alterations of protein kinase c activity were studied in the human leukemic cell line, HL-60, during induction of macropahge-like differentiation by tetradecenoyl phorbol 13-acetate (TPA). TPA added to intact HL-60 cells caused a concentration-dependent decrease in the total detergent-solubilized protein kinase C activity within an hour. This decrease in protein kinase c acticity in extracts of the cells did not appear to be due to an inhibitor of the kinase induced by TPA. DEAE-cellulose chromatography showed that the total decrease was caused by a decrease in the level of protein kinase C activity in the cytosol, since a higher peak of activity eluted at NaCl concentration greater than 0.125 M was found in the particulate preparation. Trifluoperazine, an inhibitor of protein kinase C activity in cell extracts, was however found to raise the protein kinase C activity when added to intact HL-60 cells. Nevertheless, trifluoperazine, when added in combination with TPA, did not overcome the TPA-induced decrease in protein kinase C activity.


RAPID ALTERATIONS IN PROTEIN KINASE C ACTIVITY AND INTRACELLULAR DISTRIBUTION DURING PHORBOL ESTER-INDUCED HL-60 CELL MICROPHAGE-LIKE DIFFERENTIATION
Shao Guoying.RAPID ALTERATIONS IN PROTEIN KINASE C ACTIVITY AND INTRACELLULAR DISTRIBUTION DURING PHORBOL ESTER-INDUCED HL-60 CELL MICROPHAGE-LIKE DIFFERENTIATION[J].Journal of Shanghai Second Medical University(Foreign Language Edition),1988(1).
Authors:Shao Guoying
Institution:Shao Guoying Department of Biochemistry,SSMU,Shanghai Liu Chenkao Samuel Waxman Division of Medical Oncoiogy,Mount Sinal School of Medicine of the City University of New York,New York
Abstract:Alterations of protein kinase c activity were studied in the human leukemic cell line, HL-60, during induction of macropahge-like differentiation by tetradecenoyl phorbol 13-acetate (TPA). TPA added to intact HL-60 cells caused a concentration-dependent decrease in the total detergent-solubilized protein kinase C activity within an hour. This decrease in protein kinase c acticity in extracts of the cells did not appear to be due to an inhibitor of the kinase induced by TPA. DEAE-cellulose chromatography showed that the total decrease was caused by a decrease in the level of protein kinase C activity in the cytosol, since a higher peak of activity eluted at NaCl concentration greater than 0.125 M was found in the particulate preparation. Trifluoperazine, an inhibitor of protein kinase C activity in cell extracts, was however found to raise the protein kinase C activity when added to intact HL-60 cells. Nevertheless, trifluoperazine, when added in combination with TPA, did not overcome the TPA-induced decrease in protein kinase C activity.
Keywords:protein kinase C HL-60 cell trifluoperazine macrophage-like differentiation tetradecanoyl phorbol 13-acetate
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