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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
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
Dory
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.
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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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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