Premium
Protein kinase C α, δ, ϵ and ζ in C 6 glioma cells
Author(s) -
Chen Ching-Chow
Publication year - 1993
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(93)80506-p
Subject(s) - protein kinase c , pkc alpha , cytosol , isozyme , chromosomal translocation , microbiology and biotechnology , gene isoform , western blot , cell culture , biology , chemistry , biochemistry , enzyme , signal transduction , gene , genetics
Both the cytosol and membrane in C 6 glioma cells express abundance of PKCα, δ, ζ and trace amount of PKCϵ by Western blot analysis with isozyme‐specific antibodies. These characteristics make this cell line a good model to study the properties of different classes of PKC isoforms in one cell type. Exposure of the cells to 100 nM TPA for 10 min resulted in the translocation of conventional PKCα (cPKCα) and new PKCδ(nPKCδ) and ‐ϵ from the cytosolic to the membrane fraction, while left atypical PKCζ (aPKCζ) unaffected. The extent of translocation of cPKCα induced by TPA was more prominent than that of nPKCδ and nPKCϵ. α‐TPA, the inactive phorbol ester, did not induce translocation of these isozymes. After treatment of the cells with 1 μM TPA for 17 h, cPKCα, nPKGδ and nPKCϵ were almost completely down‐regulated, whereas aPKCζ was still unaffected. The natural activators of this cell line, endothelin‐1 and ATP also translocated cPKCa and nPKCδ. However, the extent of translocation induced by these two agonists was much less than that of TPA.