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Originally published In Press as doi:10.1074/jbc.M011291200 on April 20, 2001

J. Biol. Chem., Vol. 276, Issue 28, 26164-26170, July 13, 2001
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Caveolin-1 and Caveolin-2 Expression in Mouse Macrophages
HIGH DENSITY LIPOPROTEIN 3-STIMULATED SECRETION AND A LACK OF SIGNIFICANT SUBCELLULAR CO-LOCALIZATION*

Peter Gargalovic and Ladislav DoryDagger

From the Department of Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, Texas 76107

Evidence for caveolin expression in macrophages is scarce and conflicting. We therefore examined caveolin-1 and caveolin-2 expression in resident and thioglycollate-elicited mouse peritoneal macrophages (tg-MPM) and in the J774 mouse macrophage cell line by RT-PCR, ribonuclease protection assay, immunoblotting, and immunofluorescence. We found that relative to 3T3 cells, resident MPM and tg-MPM express low amounts of caveolin-1 (45 and 15% of those in 3T3 fibroblasts, respectively), while J774.A1 cells do not express any. Caveolin-2, on the other hand, is expressed in all cells examined, with highest expression in tg-MPM and the lowest in J774 cells. The relative levels of caveolin expression in the various cells correspond well with their respective mRNA levels, as measured by ribonuclease protection assay. Caveolin-1, present primarily on the cell surface, does not co-localize significantly with caveolin-2, which is present primarily in the Golgi compartment in all macrophages studied. Loading of tg-MPM with cholesterol or variations in unesterified cholesterol content appear to have little effect on the level of caveolin-1 or -2 expression or their distribution. Stimulation of cholesterol efflux by HDL3 leads to caveolin-1 and caveolin-2 secretion to the cell culture medium, a process not detected in the absence of HDL3. The lack of significant co-localization of the two caveolin isoforms in primary macrophages and their secretion in the presence of HDL3 provides an interesting and physiologically relevant model system to study additional aspects of caveolin function.


* This work was supported, in part, by National Institutes of Health Grant HL 45513 (to L. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Molecular Biology and Immunology, University of North Texas Health Science Center, 3500 Camp Bowie Blvd., Fort Worth, TX 76107. Tel.: 817-735-0180; Fax: 817-735-2118; E-mail: ldory@hsc.unt.edu.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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