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Absorption and lipoprotein transport of sphingomyelin

Nilsson, Åke LU and Duan, Rui-Dong LU (2006) In Journal of Lipid Research 47(1). p.154-171
Abstract
Dietary sphingomyelin (SM) is hydrolyzed by intestinal alkaline sphingomyelinase and neutral ceramidase to sphingosine, which is absorbed and converted to palmitic acid and acylated into chylomicron triglycerides (TGs). SM digestion is slow and is affected by luminal factors such as bile salt, cholesterol, and other lipids. In the gut, SM and its metabolites may influence TG hydrolysis, cholesterol absorption, lipoprotein formation, and mucosal growth. SM accounts for similar to 20% of the phospholipids in human plasma lipoproteins, of which two-thirds are in LDL and VLDL. It is secreted in chylomicrons and VLDL and transferred into HDL via the ABCA1 transporter. Plasma SM increases after periods of large lipid loads, during suckling, and... (More)
Dietary sphingomyelin (SM) is hydrolyzed by intestinal alkaline sphingomyelinase and neutral ceramidase to sphingosine, which is absorbed and converted to palmitic acid and acylated into chylomicron triglycerides (TGs). SM digestion is slow and is affected by luminal factors such as bile salt, cholesterol, and other lipids. In the gut, SM and its metabolites may influence TG hydrolysis, cholesterol absorption, lipoprotein formation, and mucosal growth. SM accounts for similar to 20% of the phospholipids in human plasma lipoproteins, of which two-thirds are in LDL and VLDL. It is secreted in chylomicrons and VLDL and transferred into HDL via the ABCA1 transporter. Plasma SM increases after periods of large lipid loads, during suckling, and in type II hypercholesterolemia, cholesterol-fed animals, and apolipoprotein E-deficient mice. SM is thus an important amphiphilic component when plasma lipoprotein pools expand in response to large lipid loads or metabolic abnormalities. It inhibits lipoprotein lipase and LCAT as well as the interaction of lipoproteins with receptors and counteracts LDL oxidation. The turnover of plasma SM is greater than can be accounted for by the turnover of LDL and HDL particles. Some SM must be degraded via receptor-mediated catabolism of chylomicron and VLDL remnants and by scavenger receptor class B type I receptor-mediated transfer into cells. (Less)
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author
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
ceramidase, sphingomyelinase, low density lipoprotein, chylomicron, very low density lipoprotein, phospholipid transfer protein
in
Journal of Lipid Research
volume
47
issue
1
pages
154 - 171
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:16251722
  • wos:000234291300016
  • scopus:30844463225
ISSN
1539-7262
DOI
10.1194/jlr.M500357-JLR200
language
English
LU publication?
yes
id
cb223cae-11dd-441f-aad2-daee33fd32f1 (old id 421505)
date added to LUP
2016-04-01 12:36:14
date last changed
2020-12-01 02:26:56
@article{cb223cae-11dd-441f-aad2-daee33fd32f1,
  abstract     = {Dietary sphingomyelin (SM) is hydrolyzed by intestinal alkaline sphingomyelinase and neutral ceramidase to sphingosine, which is absorbed and converted to palmitic acid and acylated into chylomicron triglycerides (TGs). SM digestion is slow and is affected by luminal factors such as bile salt, cholesterol, and other lipids. In the gut, SM and its metabolites may influence TG hydrolysis, cholesterol absorption, lipoprotein formation, and mucosal growth. SM accounts for similar to 20% of the phospholipids in human plasma lipoproteins, of which two-thirds are in LDL and VLDL. It is secreted in chylomicrons and VLDL and transferred into HDL via the ABCA1 transporter. Plasma SM increases after periods of large lipid loads, during suckling, and in type II hypercholesterolemia, cholesterol-fed animals, and apolipoprotein E-deficient mice. SM is thus an important amphiphilic component when plasma lipoprotein pools expand in response to large lipid loads or metabolic abnormalities. It inhibits lipoprotein lipase and LCAT as well as the interaction of lipoproteins with receptors and counteracts LDL oxidation. The turnover of plasma SM is greater than can be accounted for by the turnover of LDL and HDL particles. Some SM must be degraded via receptor-mediated catabolism of chylomicron and VLDL remnants and by scavenger receptor class B type I receptor-mediated transfer into cells.},
  author       = {Nilsson, Åke and Duan, Rui-Dong},
  issn         = {1539-7262},
  language     = {eng},
  number       = {1},
  pages        = {154--171},
  publisher    = {American Society for Biochemistry and Molecular Biology},
  series       = {Journal of Lipid Research},
  title        = {Absorption and lipoprotein transport of sphingomyelin},
  url          = {http://dx.doi.org/10.1194/jlr.M500357-JLR200},
  doi          = {10.1194/jlr.M500357-JLR200},
  volume       = {47},
  year         = {2006},
}