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Rapid down‐regulation of protein kinase C and membrane association in phorbol ester‐treated leukemia cells
Author(s) -
Wickremasinghe R.Gitendra,
Piga Andrea,
Campana Dario,
Yaxley John C.,
Hoffbrand A.Victor
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80425-7
Subject(s) - protein kinase c , chronic lymphocytic leukemia , protein kinase a , cytosol , prkcq , leukemia , phorbol ester , kinase , biochemistry , chemistry , enzyme , tetradecanoylphorbol acetate , microbiology and biotechnology , biology , immunology
Peripheral blood lymphocytes from patients with chronic lymphocytic leukemia (CLL) acquire after several days of exposure to 12‐ O ‐tetradecanoylphobol‐13‐acetate (TPA) several morphological, immunological and histochemical features of hairy cell leukemia. We have investigated the short term effects of TPA treatment on protein kinase C and its subcellular distribution. Within minutes of addition of TPA to CLL cells 20% of the cytosolic protein kinase C had associated with the particulate fraction. The remaining 80% of protein kinase C activity was down‐regulated. The association with the membrane dramatically increased the resistance of the enzyme to inhibition by the non‐ionic detergent, Triton X‐100. These results suggest that activation of protein kinase C causes multiple biological changes in CLL cells.