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Protein kinase C isoforms in murine erythroleukemia cells and their involvement in the differentiation process
Author(s) -
Patrone M.,
Pessino A.,
Passalacqua M.,
Sparatore B.,
Melloni E.,
Pontremoli S.
Publication year - 1994
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(94)00359-9
Subject(s) - protein kinase c , pkc alpha , isozyme , clone (java method) , gene isoform , alpha (finance) , cell , cellular differentiation , biology , cell type , cell culture , microbiology and biotechnology , in vitro , signal transduction , enzyme , chemistry , biochemistry , gene , genetics , medicine , construct validity , nursing , patient satisfaction
In addition to α, δ and ε‐protein kinase C, murine erythroleukemia cells contain ζ‐PKC and also a c‐PKC isoform, named α 1 , which shows cross‐reactivity with an anti‐α‐PKC antipeptide antibody. In a C44 MEL cell clone, characterized by a high rate of differentiation, both c‐PKC forms are expressed at a level higher than that of the N23 MEL cell clone which differentiates at a low rate and contains higher levels of ε‐PKC and particularly of the δ‐PKC isozyme. In the course of MEL cell differentiation, δ‐PKC in N23 cells and α 1 ‐PKC in C44 cells are rapidly down‐regulated and the overall process is almost completed before cell commitment. Of the other three PKC isozymes present in both clones, only α‐PKC is down‐regulated to a significant extent. It is proposed that modulation of the signal delivered by each PKC isozyme is one of the biochemical mechanisms involved in MEL cell differentiation.