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


     

A more recent version of this article appeared on August 1, 2007

Papers In Press, published online ahead of print May 24, 2007
J. Lipid Res., doi:10.1194/jlr.M700103-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
M700103-JLR200v1
48/8/1754    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Ahnstrom, J.
Right arrow Articles by Dahlback, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ahnstrom, J.
Right arrow Articles by Dahlback, B.
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?

Submitted on February 28, 2007
Revised on May 23, 2007
Accepted on May 24, 2007

Hydrophobic ligand-binding properties of the human lipocalin apolipoprotein M

Josefin Ahnstrom, Kirsten Faber, Olof Axler, and Bjorn Dahlback

Laboratory Medicine, Clinical Chemistry, Malmö University Hospital, Malmo 20502

Corresponding Author: bjorn.dahlback{at}med.lu.se

Apolipoprotein M (apoM) is a plasma protein mainly associated with HDL. ApoM is suggested to be important for the formation of pre-ß HDL, but its mechanism of action is unknown. Homology modeling has suggested apoM to be a lipocalin. Lipocalins share a structurally conserved ß-barrel, which in many lipocalins bind hydrophobic ligands. The aim of the present study was to test the ability of apoM to bind different hydrophobic substances. ApoM was produced both in E. coli and in HEK 293 cells. Characterization of both variants with electrophoretic and immunological methods suggested apoM from E.coli to be correctly folded. Intrinsic tryptophan fluorescence of both apoM variants revealed that retinol, all-trans retinoic acid and 9-cis retinoic acid bound (Kd 2-3 µM), whereas other tested substances e.g. cholesterol, vitamin K and arachidonic acid did not. The intrinsic fluorescence of two apoM mutants carrying single tryptophans was quenched by retinol and retinoic acid to the same extent as wildtype apoM, indicating that the environment of both tryptophans was affected by the binding. In conclusion, the binding of retinol and retinoic acid supports the hypothesis that apoM is a lipocalin. The physiological relevance of this binding is yet to be elucidated.


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
J. Ahnstrom, O. Axler, M. Jauhiainen, V. Salomaa, A. S. Havulinna, C. Ehnholm, R. Frikke-Schmidt, A. Tybjaerg-Hansen, and B. Dahlback
Levels of apolipoprotein M are not associated with the risk of coronary heart disease in two independent case-control studies
J. Lipid Res., September 1, 2008; 49(9): 1912 - 1917.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Christoffersen, J. Ahnstrom, O. Axler, E. I. Christensen, B. Dahlback, and L. B. Nielsen
The Signal Peptide Anchors Apolipoprotein M in Plasma Lipoproteins and Prevents Rapid Clearance of Apolipoprotein M from Plasma
J. Biol. Chem., July 4, 2008; 283(27): 18765 - 18772.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Christoffersen, M. Jauhiainen, M. Moser, B. Porse, C. Ehnholm, M. Boesl, B. Dahlback, and L. B. Nielsen
Effect of Apolipoprotein M on High Density Lipoprotein Metabolism and Atherosclerosis in Low Density Lipoprotein Receptor Knock-out Mice
J. Biol. Chem., January 25, 2008; 283(4): 1839 - 1847.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
O. Axler, J. Ahnstrom, and B. Dahlback
An ELISA for apolipoprotein M reveals a strong correlation to total cholesterol in human plasma
J. Lipid Res., August 1, 2007; 48(8): 1772 - 1780.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.