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Alkaline sphingomyelinase: An old enzyme with novel implications.

Duan, Rui-Dong LU (2006) In Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids 1761(3). p.281-291
Abstract
Alkaline sphingomyelinase (alk-SMase) is present in the intestinal tract and additionally human bile. It hydrolyses sphingomyelin in both intestinal lumen and the mucosal membrane in a specific bile salt dependent manner. The enzyme was discovered 36 years ago but got real attention only in the last decade, when sphingomyelin metabolism was realized to be a source of multiple lipid messengers, and when dietary sphingomyelin was found to inhibit colonic tumorigenesis in animals. The enzyme shares no structural similarity with other SMases and belongs to the nucleotide pyrophosphatase/phosphodiesterase family. The enzyme is of specific properties, such as bile salt dependency, trypsin resistance, high stability, and tissue specific... (More)
Alkaline sphingomyelinase (alk-SMase) is present in the intestinal tract and additionally human bile. It hydrolyses sphingomyelin in both intestinal lumen and the mucosal membrane in a specific bile salt dependent manner. The enzyme was discovered 36 years ago but got real attention only in the last decade, when sphingomyelin metabolism was realized to be a source of multiple lipid messengers, and when dietary sphingomyelin was found to inhibit colonic tumorigenesis in animals. The enzyme shares no structural similarity with other SMases and belongs to the nucleotide pyrophosphatase/phosphodiesterase family. The enzyme is of specific properties, such as bile salt dependency, trypsin resistance, high stability, and tissue specific expression. In the colon, the enzyme may play antiproliferative and antiinflammatory roles through generating ceramide, reducing the formation of lysophosphatidic acid, and inactivating platelet-activating factor. The enzyme is down regulated in human long-standing ulcerative colitis and colonic adenocarcinoma, and mutation of the enzyme has been found in colon cancer cells. In the small intestine, alk-SMase is the key enzyme for sphingomyelin digestion. The hydrolysis of sphingomyelin may affect the cholesterol uptake and have impact on sphingomyelin levels in plasma lipoproteins. The review summarizes the new information of alk-SMase from biochemical, cell and molecular biological studies in the last decade and evaluates its potential implications in development of colon cancer, inflammatory bowel diseases, and atherosclerosis. (c) 2006 Elsevier B.V. All rights reserved. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
nucleotide pyrophosphatase phosphodiesterase, colon cancer, alkaline sphingomyelinase, inflammatory bowel disease, platelet activating factor, sphingomyelin digestion, atherosclerosis, lysophosphatidic acid, liver, intestine
in
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
volume
1761
issue
3
pages
281 - 291
publisher
Elsevier
external identifiers
  • pmid:16631405
  • wos:000238116300001
  • scopus:33646146401
ISSN
1388-1981
DOI
10.1016/j.bbalip.2006.03.007
language
English
LU publication?
yes
id
f3fc6024-a3e2-46c2-9e8a-4b9376484272 (old id 155795)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16631405&dopt=Abstract
date added to LUP
2016-04-01 16:21:02
date last changed
2021-09-15 05:49:08
@article{f3fc6024-a3e2-46c2-9e8a-4b9376484272,
  abstract     = {Alkaline sphingomyelinase (alk-SMase) is present in the intestinal tract and additionally human bile. It hydrolyses sphingomyelin in both intestinal lumen and the mucosal membrane in a specific bile salt dependent manner. The enzyme was discovered 36 years ago but got real attention only in the last decade, when sphingomyelin metabolism was realized to be a source of multiple lipid messengers, and when dietary sphingomyelin was found to inhibit colonic tumorigenesis in animals. The enzyme shares no structural similarity with other SMases and belongs to the nucleotide pyrophosphatase/phosphodiesterase family. The enzyme is of specific properties, such as bile salt dependency, trypsin resistance, high stability, and tissue specific expression. In the colon, the enzyme may play antiproliferative and antiinflammatory roles through generating ceramide, reducing the formation of lysophosphatidic acid, and inactivating platelet-activating factor. The enzyme is down regulated in human long-standing ulcerative colitis and colonic adenocarcinoma, and mutation of the enzyme has been found in colon cancer cells. In the small intestine, alk-SMase is the key enzyme for sphingomyelin digestion. The hydrolysis of sphingomyelin may affect the cholesterol uptake and have impact on sphingomyelin levels in plasma lipoproteins. The review summarizes the new information of alk-SMase from biochemical, cell and molecular biological studies in the last decade and evaluates its potential implications in development of colon cancer, inflammatory bowel diseases, and atherosclerosis. (c) 2006 Elsevier B.V. All rights reserved.},
  author       = {Duan, Rui-Dong},
  issn         = {1388-1981},
  language     = {eng},
  number       = {3},
  pages        = {281--291},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids},
  title        = {Alkaline sphingomyelinase: An old enzyme with novel implications.},
  url          = {https://lup.lub.lu.se/search/files/4645712/625426.pdf},
  doi          = {10.1016/j.bbalip.2006.03.007},
  volume       = {1761},
  year         = {2006},
}