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Evidence of the role of protein kinase C during aclacinomycin inductionof erythroid differentiation in K562 cells
Author(s) -
Reynald Gillet,
Emmanuelle Devemy,
Claude Dupont,
Claudine Billat,
Pierre Jeannesson,
Chantal Trentesaux
Publication year - 1999
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/s0014-5793(99)00838-8
Subject(s) - protein kinase c , bisindolylmaleimide , k562 cells , cytosol , microbiology and biotechnology , western blot , kinase , chromosomal translocation , chemistry , biology , cell , biochemistry , gene , enzyme
At subtoxic concentrations, aclacinomycin is effective in controlling erythroid differentiation of K562, a human erythroleukemic cell line. To better understand early events implicated in this process, we have used bisindolylmaleimide (GF109203X), an inhibitor with a high selectivity for protein kinase C (PKC). Our data show that GF109203X inhibits aclacinomycin effects on K562, evidenced by a strong reduction of hemoglobinized cells and a marked decrease of mRNA rates of erythroid genes. To establish firmly PKC involvement, we also verified that aclacinomycin stimulates its rapid translocation, from the cytosolic to the membrane compartment. By Western blot analysis, we also show that after short induction times, PKCalpha was the most implicated.