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We have examined the effect of sodium butyrate on the levels of histone acetylation, the pattern of protein synthesis and the inducibility of heat shock polypeptides (hsps) in cultured trout fibroblasts. Maximal levels of histone acetylation are achieved upon treatment of these cells with 5 mM butyrate for 24 h. No significant changes in the pattern of protein synthesis, as detected by two-dimensional gel electrophoresis, are apparent under these conditions, although changes in the levels of three polypeptides are seen at shorter times of exposure to butyrate. Heat shock polypeptides are inducible at normal levels in butyrate-treated cells. This is in contrast to the ability of butyrate to inhibit the activation of steroid-inducible genes in some systems.
E A Burgess, and
R K Kothary, and
E P Candido
June 1978,
Biochemical and biophysical research communications,
E A Burgess, and
R K Kothary, and
E P Candido
September 1980,
Nucleic acids research,
E A Burgess, and
R K Kothary, and
E P Candido
May 1978,
Biochemical and biophysical research communications,
E A Burgess, and
R K Kothary, and
E P Candido
March 2010,
PloS one,
E A Burgess, and
R K Kothary, and
E P Candido
January 1985,
Nucleic acids research,
E A Burgess, and
R K Kothary, and
E P Candido
January 1982,
The EMBO journal,
E A Burgess, and
R K Kothary, and
E P Candido
July 2002,
Journal of clinical immunology,
E A Burgess, and
R K Kothary, and
E P Candido
December 2006,
The Journal of parasitology,
E A Burgess, and
R K Kothary, and
E P Candido
April 1985,
Journal of molecular biology,
E A Burgess, and
R K Kothary, and
E P Candido
June 2003,
Molecular cell,
