|
Originally published In Press as doi:10.1194/jlr.M500357-JLR200 on October 26, 2005
Journal of Lipid Research, Vol. 47, 154-171, January 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology
Absorption and lipoprotein transport of sphingomyelin
Åke Nilsson1 and
Rui-Dong Duan
Department of Medicine, University of Lund, University Hospital, S-22185 Lund, Sweden
Published, JLR Papers in Press, October 26, 2005.
1 To whom correspondence should be addressed. e-mail: ake.nilsson{at}med.lu.se
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 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.
Supplementary key words chylomicron very low density lipoprotein low density lipoprotein sphingomyelinase ceramidase phospholipid transfer protein Abbreviations: apoB, apolipoprotein B; BSSL, bile salt-stimulated lipase; CE, cholesteryl ester; CETP, cholesteryl ester transfer protein; ER, endoplasmic reticulum; IDL, intermediate density lipoprotein; LRP, low density lipoprotein receptor-related protein; PC, phosphatidylcholine; PE, phosphatidylethanolamine; PLTP, phospholipid transfer protein; SM, sphingomyelin; SMase, sphingomyelinase; SR-BI, scavenger receptor class B type I; TG, triglyceride

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
T.-S. Park, Y. Hu, H.-L. Noh, K. Drosatos, K. Okajima, J. Buchanan, J. Tuinei, S. Homma, X.-C. Jiang, E. D. Abel, et al.
Ceramide is a cardiotoxin in lipotoxic cardiomyopathy
J. Lipid Res.,
October 1, 2008;
49(10):
2101 - 2112.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. A. Siddiqi and C. M. Mansbach II
PKC{zeta}-mediated phosphorylation controls budding of the pre-chylomicron transport vesicle
J. Cell Sci.,
July 15, 2008;
121(14):
2327 - 2338.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. Kontush, P. Therond, A. Zerrad, M. Couturier, A. Negre-Salvayre, J. A. de Souza, S. Chantepie, and M. J. Chapman
Preferential Sphingosine-1-Phosphate Enrichment and Sphingomyelin Depletion Are Key Features of Small Dense HDL3 Particles: Relevance to Antiapoptotic and Antioxidative Activities
Arterioscler. Thromb. Vasc. Biol.,
August 1, 2007;
27(8):
1843 - 1849.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. Kohno, M. Momoi, M. L. Oo, J.-H. Paik, Y.-M. Lee, K. Venkataraman, Y. Ai, A. P. Ristimaki, H. Fyrst, H. Sano, et al.
Intracellular role for sphingosine kinase 1 in intestinal adenoma cell proliferation.
Mol. Cell. Biol.,
October 1, 2006;
26(19):
7211 - 7223.
[Abstract]
[Full Text]
[PDF]
|
 |
|
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|