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closeButyrate as a Histone Deacetylase Inhibitor (iHDAC)
Posted by DerekS on 15 Aug 2013 at 22:36 GMT
In the discussion section the authors remark that "The decreased oxidation rate of butyrate may result in increased intra-cellular butyrate concentrations in tumor cells, hence causing increased histone deacetylation and subsequently decreased proliferation." This is only partially correct, however, as lower levels of butyrate oxidation can lead to increased intracellular concentrations. The statement is incorrect in that elevated butyrate concentrations will lead to a decrease in histone deacetylation, not an increase. In other words, increases in intracellular concentrations of butyrate lead to HDAC inhibition and likely maintain levels of acetylated histones. Furthermore, butyrate has also been shown to provide the carbon substrate necessary for histone acetyl transferase activity (HAT) which would logically increase the levels of histone acetylation.
Sources:
"Inhibition of Histone Deacetylase Activity by Butyrate"
James R. Davie. J. Nutr. July 1, 2003 vol. 133 no. 7 2485S-2493S
"Butyrate suppresses Cox-2 activation in colon cancer cells through HDAC inhibition"
Xin Tong, Lei Yin, Charles Giardina. Biochemical and Biophysical Research Communications Volume 317, Issue 2, 30 April 2004, Pages 463–471
"The Warburg Effect Dictates the Mechanism of Butyrate-Mediated Histone Acetylation and Cell Proliferation" Dallas R. Donohoe, Leonard B. Collins, Aminah Wali, Rebecca Bigler, Wei Sun, Scott J. Bultman.
Molecular Cell Volume 48, Issue 4, 30 November 2012, Pages 612–626