Acid sphingomyelinase is induced by butyrate but does not initiate the anticancer effect of butyrate in HT29 and HepG2 cells
(2005) In Journal of Lipid Research 46(9). p.1944-1952- Abstract
- Butyric acid and sphingomyelin (SM) affect colonic tumorigenesis. We examined the potential link between butyrate stimulation and SM metabolism in colonic and hepatic cancer cell lines. After incubating HT29 and HepG2 cells with butyrate and other short-chain fatty acids, we found that butyrate increased acid but not neutral or alkaline sphingomyelinase (SMase) activity by 10- to 20-fold. The effects occurred after 16 h of incubation and were associated with reduced SM and phosphatidylcholine contents and increased ceramide levels. 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... (More)
- Butyric acid and sphingomyelin (SM) affect colonic tumorigenesis. We examined the potential link between butyrate stimulation and SM metabolism in colonic and hepatic cancer cell lines. After incubating HT29 and HepG2 cells with butyrate and other short-chain fatty acids, we found that butyrate increased acid but not neutral or alkaline sphingomyelinase (SMase) activity by 10- to 20-fold. The effects occurred after 16 h of incubation and were associated with reduced SM and phosphatidylcholine contents and increased ceramide levels. 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. 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 small, interfering RNA. In addition, butyrate-induced acid SMase expression was not affected by blocking the caspase pathway. In conclusion, butyrate regulates SM metabolism by stimulating acid SMase expression in colon and liver cancer cells, but the increased acid SMase is not a critical mechanism for initiating the anticancer effects of butyrate. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/223694
- author
- Wu, Jun LU ; Cheng, Yajun LU ; Jönsson, Bo A LU ; Nilsson, Åke LU and Duan, Rui-Dong LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- apoptosis, sphingomyelin, liver, short-chain fatty acid, colon, caspase, small, interfering RNA
- in
- Journal of Lipid Research
- volume
- 46
- issue
- 9
- pages
- 1944 - 1952
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:15961787
- wos:000231244200016
- scopus:24344503325
- ISSN
- 1539-7262
- DOI
- 10.1194/jlr.M500118-JLR200
- language
- English
- LU publication?
- yes
- id
- ca7fae47-f4b0-4590-9a0b-1b0e4be7dc51 (old id 223694)
- date added to LUP
- 2016-04-01 12:34:59
- date last changed
- 2024-01-09 01:35:36
@article{ca7fae47-f4b0-4590-9a0b-1b0e4be7dc51, abstract = {{Butyric acid and sphingomyelin (SM) affect colonic tumorigenesis. We examined the potential link between butyrate stimulation and SM metabolism in colonic and hepatic cancer cell lines. After incubating HT29 and HepG2 cells with butyrate and other short-chain fatty acids, we found that butyrate increased acid but not neutral or alkaline sphingomyelinase (SMase) activity by 10- to 20-fold. The effects occurred after 16 h of incubation and were associated with reduced SM and phosphatidylcholine contents and increased ceramide levels. 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. 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 small, interfering RNA. In addition, butyrate-induced acid SMase expression was not affected by blocking the caspase pathway. In conclusion, butyrate regulates SM metabolism by stimulating acid SMase expression in colon and liver cancer cells, but the increased acid SMase is not a critical mechanism for initiating the anticancer effects of butyrate.}}, author = {{Wu, Jun and Cheng, Yajun and Jönsson, Bo A and Nilsson, Åke and Duan, Rui-Dong}}, issn = {{1539-7262}}, keywords = {{apoptosis; sphingomyelin; liver; short-chain fatty acid; colon; caspase; small; interfering RNA}}, language = {{eng}}, number = {{9}}, pages = {{1944--1952}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Lipid Research}}, title = {{Acid sphingomyelinase is induced by butyrate but does not initiate the anticancer effect of butyrate in HT29 and HepG2 cells}}, url = {{http://dx.doi.org/10.1194/jlr.M500118-JLR200}}, doi = {{10.1194/jlr.M500118-JLR200}}, volume = {{46}}, year = {{2005}}, }