J. Lipid Res.
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 28, 2007
J. Lipid Res., doi:10.1194/jlr.M700209-JLR200
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
M700209-JLR200v1
48/8/1832    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 Nieland, T. J. F.
Right arrow Articles by Krieger, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nieland, T. J. F.
Right arrow Articles by Krieger, M.
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 May 7, 2007
Accepted on May 28, 2007

Influence of HDL-cholesterol elevating drugs on the in vitro activity of the HDL receptor SR-BI

Thomas J. F. Nieland, Jared Shaw, Firoz A. Jaipuri, Zoltan Maliga, Jay L. Duffner, Angela N. Koehler, and Monty Krieger

Biology, Massachusetts Institute of Technology, Cambridge, MA 02139

Corresponding Author: krieger{at}mit.edu

Treatment of atherosclerotic disease often focuses on reducing plasma LDL-cholesterol or increasing plasma HDL-cholesterol. We examined in vitro the effects on HDL receptor (SR-BI) activity of three classes of clinical and experimental plasma HDL-cholesterol-raising compounds: niacin, fibrates and HDL376. Fenofibrate and HDL376 were potent (IC50 ~1 mu M), direct inhibitors of SR-BI-mediated lipid transport in cells and in liposomes reconstituted with purified SR-BI. Fenofibrate, a prodrug, was a more potent inhibitor of SR-BI than activator of PPARa, a target of its active fenofibric acid (FFA) derivative. Nevertheless, FFA, four other fibrates (clofibrate, gemfibrozil, ciprofibrate, benzafibrate) and niacin had little, if any, effect on SR-BI, suggesting that they don’t directly target SR-BI in vivo. However, similarities of HDL376 treatment and SR-BI gene knockout on HDL metabolism in vivo (increased HDL cholesterol and HDL particle sizes) and structure activity relationship analysis suggest SR-BI may be a target of HDL376 in vivo. HDL376 and other inhibitors may help elucidate SR-BI function in diverse mammalian models and determine the therapeutic potential of SR-BI-directed pharmaceuticals.


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
L.-H. Zhang, V. S. Kamanna, M. C. Zhang, and M. L. Kashyap
Niacin inhibits surface expression of ATP synthase {beta} chain in HepG2 cells: implications for raising HDL
J. Lipid Res., June 1, 2008; 49(6): 1195 - 1201.
[Abstract] [Full Text] [PDF]

Home page
 Chem SensesHome page
M. Forstner, T. Gohl, I. Gondesen, K. Raming, H. Breer, and J. Krieger
Differential Expression of SNMP-1 and SNMP-2 Proteins in Pheromone-Sensitive Hairs of Moths
Chem Senses, March 1, 2008; 33(3): 291 - 299.
[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.