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Short‐chain fatty acids reduce expression of specific protein kinase C isoforms in human colonic epithelial cells
Author(s) -
Rickard Kurt L.,
Gibson Peter R.,
Wilson Nicholas J.,
Mariadason John M.,
Phillips Wayne A.
Publication year - 2000
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/(sici)1097-4652(200002)182:2<222::aid-jcp11>3.0.co;2-b
Subject(s) - protein kinase c , butyrate , gene isoform , western blot , trichostatin a , microbiology and biotechnology , pkc alpha , caco 2 , biology , chemistry , kinase , histone deacetylase , histone , biochemistry , cell , gene , fermentation
LIM1215 colon cancer cells were used as a model of human colonic epithelium to examine the effects of butyrate on protein kinase C (PKC) activity and isoform expression. On Western blot analysis, LIM1215 cells express the PKC isoforms α, β, ε, ζ, and λ, but not γ, θ, or μ. Treatment with 2 mM butyrate for 48 h reduced cellular PKC activity up to 50% and specifically reduced the expression of PKCα and PKCε. Similar results were obtained using Caco‐2 colon cancer cells. These effects were neither a consequence of the induction of differentiation itself nor the result of direct or indirect activation of PKC. Although dependent on gene transcription and protein synthesis, the effect was not due to a reduction in the synthesis of PKC protein. Butyrate's effect was independent of its β‐oxidation but was mimicked, at least in part, by trichostatin A, an inhibitor of histone deacetylase. J. Cell. Physiol. 182:222–231, 2000. © 2000 Wiley‐Liss, Inc.