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Identification of multiple PKC isoforms in Swiss 3T3 cells: Differential down‐regulation by phorbol ester
Author(s) -
Olivier Andrée R.,
Parker Peter J.
Publication year - 1992
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041520204
Subject(s) - protein kinase c , gene isoform , tetradecanoylphorbol acetate , phorbol ester , 12 o tetradecanoylphorbol 13 acetate , phorbol , chemistry , microbiology and biotechnology , biology , biochemistry , kinase , gene
Abstract The expression of members of the Ca 2+ and phospholipid‐dependent protein kinase (PKC) family were studied in murine Swiss 3T3 cells. In addition to PKC‐α, the presence of immunoreactive PKC‐δ, ‐ε, and ζ was detected. Treatment with 500 nM 12‐0‐tetradecanoylphorbol‐13‐acetate (TPA) led to the down‐regulation of α, δ, and ε isoforms, but not that of ζ. Higher concentrations of TPA similarly had no effect on the level of PKC‐ζ. In contrast to PKC‐α, the membrane localization of PKC‐δ, ‐ε, and ‐ζ was not enhanced by extraction in Ca 2+ ‐containing buffers, whereas acute TPA treatment increased membrane association of PKC‐α, ‐δ, and ‐ε but not that of PKC‐ζ. © 1992 Wiley‐Liss, Inc.