HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sparrow, C. P. Articles by Detmers, P. A. Search for Related Content PubMed PubMed Citation Articles by Sparrow, C. P. Articles by Detmers, P. A. Social Bookmarking                      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

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

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

This article has been cited by other articles:

				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]

				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]

				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]

				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]

				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]

				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]

				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]

				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]

				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]

				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]