J. Lipid Res.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Sparrow, C. P.
Right arrow Articles by Detmers, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sparrow, C. P.
Right arrow Articles by Detmers, P. A.
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. 40, 1747-1757, October 1999
Copyright © 1999 by Lipid Research, Inc.


Original Article

A fluorescent cholesterol analog traces cholesterol absorption in hamsters and is esterified in vivo and in vitro

Carl P. Sparrowa, Sushma Patela, Joanne Baffica, Yu-Sheng Chaoa, Melba Hernandeza, My-Hanh Lama, Judy Montenegroa, Samuel D. Wrighta, and Patricia A. Detmersa
a Department of Lipid Biochemistry, Merck Research Laboratories, Building 80W, 126 E. Lincoln Avenue, Rahway, NJ 07065

Correspondence to: Carl P. Sparrow

The fluorescent cholesterol analog 22-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-23,24-bisnor-5-cholen-3ß-ol (fluoresterol) was characterized as a tool for exploring the biochemistry and cell biology of intestinal cholesterol absorption. Hamsters absorbed fluoresterol in a concentration- and time-dependent manner, with an efficiency of about 15;–30% that of cholesterol. Fluoresterol absorption was blocked by compounds known to inhibit cholesterol absorption, implying that fluoresterol interacts with those elements of the normal pathway for cholesterol absorption on which the inhibitors act. Confocal microscopy of small intestinal tissue demonstrated that fluoresterol was taken up by absorptive epithelial cells and packaged into lipoprotein particles, suggesting a normal route of intracellular trafficking. Uptake of fluoresterol was confirmed by biochemical analysis of intestinal tissue, and a comparison of [3H]cholesterol and fluoresterol content in the mucosa suggested that fluoresterol moved through the enterocytes more rapidly than did cholesterol. This interpretation was supported by measurements of fluoresterol esterification in the mucosa. Four hours after hamsters were given fluoresterol and [3H]cholesterol orally, 44% of the fluoresterol in the intestinal mucosa was esterified, compared to 8% of the [3H]cholesterol. Caco-2 cells took up 2- to 5-fold more [3H]cholesterol than fluoresterol from bile acid micelles, and esterified 21;–24% of the fluoresterol but only 1;–4% of the [3H]cholesterol.

Thus fluoresterol apparently interacts with the proteins required for cholesterol uptake, trafficking, and processing in the small intestine.—Sparrow, C. P., S. Patel, J. Baffic, Y-S. Chao, M. Hernandez, M-H. Lam, J. Montenegro, S. D. Wright, and P. A. Detmers. A fluorescent cholesterol analog traces cholesterol absorption in hamsters and is esterified in vivo and in vitro. J. Lipid Res. 1999. 40: 1747;–1757.

Supplementary key words: small intestine, cholesterol trafficking, endoplasmic reticulum, ACAT, esterification, Caco-2


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
Mol. Biol. CellHome page
S. Reiner, D. Micolod, G. Zellnig, and R. Schneiter
A Genomewide Screen Reveals a Role of Mitochondria in Anaerobic Uptake of Sterols in Yeast
Mol. Biol. Cell, January 1, 2006; 17(1): 90 - 103.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
W. Kramer, F. Girbig, D. Corsiero, A. Pfenninger, W. Frick, G. Jahne, M. Rhein, W. Wendler, F. Lottspeich, E. O. Hochleitner, et al.
Aminopeptidase N (CD13) Is a Molecular Target of the Cholesterol Absorption Inhibitor Ezetimibe in the Enterocyte Brush Border Membrane
J. Biol. Chem., January 14, 2005; 280(2): 1306 - 1320.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
W. Stockinger, A. B. Castoreno, Y. Wang, J. C. Pagnon, and A. Nohturfft
Real-time analysis of endosomal lipid transport by live cell scintillation proximity assay
J. Lipid Res., November 1, 2004; 45(11): 2151 - 2158.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
A. T. Lada, M. Davis, C. Kent, J. Chapman, H. Tomoda, S. Omura, and L. L. Rudel
Identification of ACAT1- and ACAT2-specific inhibitors using a novel, cell-based fluorescence assay: individual ACAT uniqueness
J. Lipid Res., February 1, 2004; 45(2): 378 - 386.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
G. Dagher, N. Donne, C. Klein, P. Ferre, and I. Dugail
HDL-mediated cholesterol uptake and targeting to lipid droplets in adipocytes
J. Lipid Res., October 1, 2003; 44(10): 1811 - 1820.
[Abstract] [Full Text] [PDF]


Home page
Exp. Biol. Med.Home page
F. Schroeder, A. M. Gallegos, B. P. Atshaves, S. M. Storey, A. L. McIntosh, A. D. Petrescu, H. Huang, O. Starodub, H. Chao, H. Yang, et al.
Recent Advances in Membrane Microdomains: Rafts, Caveolae, and Intracellular Cholesterol Trafficking
Experimental Biology and Medicine, November 1, 2001; 226(10): 873 - 890.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
F. J. Field, E. Born, S. Murthy, and S. N. Mathur
Gene expression of sterol regulatory element-binding proteins in hamster small intestine
J. Lipid Res., January 1, 2001; 42(1): 1 - 8.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
A. Frolov, A. Petrescu, B. P. Atshaves, P. T. C. So, E. Gratton, G. Serrero, and F. Schroeder
High Density Lipoprotein-mediated Cholesterol Uptake and Targeting to Lipid Droplets in Intact L-cell Fibroblasts. A SINGLE- AND MULTIPHOTON FLUORESCENCE APPROACH
J. Biol. Chem., April 21, 2000; 275(17): 12769 - 12780.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. P. Atshaves, O. Starodub, A. McIntosh, A. Petrescu, J. B. Roths, A. B. Kier, and F. Schroeder
Sterol Carrier Protein-2 Alters High Density Lipoprotein-mediated Cholesterol Efflux
J. Biol. Chem., November 17, 2000; 275(47): 36852 - 36861.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
B. P. Atshaves, S. M. Storey, A. L. McIntosh, A. D. Petrescu, O. I. Lyuksyutova, A. S. Greenberg, and F. Schroeder
Sterol Carrier Protein-2 Expression Modulates Protein and Lipid Composition of Lipid Droplets
J. Biol. Chem., June 29, 2001; 276(27): 25324 - 25335.
[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 © 1999 by the American Society for Biochemistry and Molecular Biology.