J. Lipid Res.
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A more recent version of this article appeared on September 1, 2005

Papers In Press, published online ahead of print June 16, 2005
J. Lipid Res., doi:10.1194/jlr.M500118-JLR200
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Submitted on March 30, 2005
Revised on May 10, 2005
Accepted on June 6, 2005

Acid sphingomyelinase expression is stimulated by butyrate but not functionally involved in cell proliferation and apoptosis in HT29 and HepG2 cells

Jun Wu, Yajun Cheng, Bo AG Jonsson, Ake Nilsson, and Rui-Dong Duan

Department of Biomedical Center, B11, Lund University, Lund S-221 84

Corresponding Author: rui-dong.duan{at}med.lu.se

Butyric acid and sphingomyelin are two molecules affecting colonic tumorigenesis. The present study examines the potential link between butyrate stimulation and sphingomyelin metabolism in colonic and hepatic cancer cell lines. HT29 and HepG2 cells were incubated with butyrate and other short chain fatty acids. The sphingomyelinase (SMase) activities were determined. The contents of phospholipids were analyzed by TLC and that of ceramide was quantified by liquid chromatography tandem mass spectrometry. Butyrate increased acid but not neutral or alkaline SMase activity in HT29 and Hep G2 cells in a dose-dependent manner. The threshold concentration was 2.5 mM and 0.125 mM for HT29 and HepG2 cells, respectively. The effects occurred after 16 hour incubation, and were associated with reduced sphingomyelin and phosphatidylcholine contents and an increase in ceramide level. Northern blotting showed increased acid SMase mRNA levels in these cells after butyrate stimulation. Propionate was less potent and acetate had no effect. No similar changes of acid phosphatase could be identified after butyrate stimulation. At concentrations that increased acid SMase expression, butyrate inhibited cell proliferation, activated caspase 3 and induced apoptosis. However, the antiproliferative and apoptotic effects of butyrate preceded the changes of acid SMase, and were not affected by knocking down acid SMase expression by siRNA. In addition, butyrate-induced acid SMase expression was not affected by blocking the caspase pathway. In conclusion, butyrate regulates sphingomyelin metabolism by stimulating acid SMase expression in colon and liver cancer cells, but the increased acid SMase is not a critical mechanism for the anticancer effects of butyrate in these cells.


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