J. Lipid Res. Did you know there is a large type edition? Click here.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1194/jlr.M500357-JLR200 on October 26, 2005

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
M500357-JLR200v1
47/1/154    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Nilsson, A.
Right arrow Articles by Duan, R.-D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nilsson, A.
Right arrow Articles by Duan, R.-D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Lipid Res.Home page
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]

Home page
 J. Cell Sci.Home page
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]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
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]

Home page
 Mol. Cell. Biol.Home page
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]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.