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Carnitine is a Pivotal Contributor for Butyrate Oxidation in Colon Cancer Cells
Author(s) -
Han Anna,
Donohoe Dallas
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.394.6
Subject(s) - butyrate , carnitine , acetylation , chemistry , biochemistry , beta oxidation , sodium butyrate , metabolism , cancer research , microbiology and biotechnology , biology , fermentation , gene
Butyrate, derived from colonic microbial fermentation of dietary fiber, is the primary energy substrate of the colonocyte. Butyrate also regulates gene expression in the colonocyte via inhibition of histone deacetylases (HDACs). The main objective of this study was to identify mechanisms that influence butyrate oxidation in cancerous colonocyte (HCT116). We hypothesized that carnitine, which is used to mainly shuttle LCFAs into the mitochondria via CPT1, would be required to achieve full butyrate oxidation in the cancerous colonocyte. The Seahorse XF24 Analyzer was used to measure butyrate oxidation in HCT116 cells with and without carnitine. The oxidation of butyrate in HCT 116 cells incubated with carnitine was significantly higher than those without carnitine (p<0.05). Next, we predicted that if carnitine increased butyrate oxidation, it would lower intracellular butyrate, suppress HDAC inhibition, and diminish butyrate induced histone acetylation. This was indeed the case as the relative H3 acetylation induced by butyrate is significantly decreased in HCT116 cells treated with carnitine (p<0.05).. Furthermore, we found that only butyrate oxidation was shown to be carnitine dependent when compared to other SCFAs (p<0.05). This suggests that carnitine is an important contributor toward butyrate oxidation and butyrate‐induced histone acetylation in colorectal cancer cells.