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(Received for publication, June 28, 1996, and in revised form, August 23, 1996)
From the Department of Cell Biology and Neuroscience, University of
Texas Southwestern Medical Center, Dallas, Texas 75235-9039
Caveolin is a 22-kDa membrane protein found
associated with a coat material decorating the inner membrane surface
of caveolae. A remarkable feature of this protein is its ability to
migrate from caveolae directly to the endoplasmic reticulum (ER) when membrane cholesterol is oxidized. We now present evidence caveolin is
involved in transporting newly synthesized cholesterol from the ER
directly to caveolae. MA104 cells and normal human fibroblasts transported new cholesterol to caveolae with a half-time of ~10 min.
The cholesterol then rapidly flowed from caveolae to non-caveolae membrane. Cholesterol moved out of caveolae even when the supply of
fresh cholesterol from the ER was interrupted. Treatment of cells with
10 µg/ml progesterone blocked cholesterol movement from ER to
caveolae. Simultaneously, caveolin accumulated in the lumen of the ER,
suggesting cholesterol transport is linked to caveolin movement.
Caveolae fractions from cells expressing caveolin were enriched in
cholesterol 3-4-fold, while the same fractions from cells lacking
caveolin were not enriched. Cholesterol transport to the cell surface
was nearly 4 times more rapid in cells expressing caveolin than in
matched cells lacking caveolin.
Volume 271, Number 46,
Issue of November 15, 1996
pp. 29427-29435
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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