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J. Biol. Chem., Vol. 277, Issue 33, 30325-30336, August 16, 2002
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From the We studied the transport of the fluorescent
cholesterol analog dehydroergosterol (DHE) in polarized HepG2 human
hepatoma cells. DHE delivered via methyl-
Rapid Nonvesicular Transport of Sterol between the Plasma
Membrane Domains of Polarized Hepatic Cells*
§,, and
Department of Biochemistry, Weill Medical
College of Cornell University, New York, New York 10021 and
Humboldt-Universität zu Berlin,
Mathematisch-Naturwissenschaftliche Fakultät I, Institut
für Biologie/Biophysik, Invalidenstrasse 43, D-10115 Berlin, Germany
-cyclodextrin was delivered
to both the apical and basolateral membranes and became concentrated in the apical membrane within 1 min. Intracellular DHE was targeted mainly
to vesicles of the subapical compartment or apical recycling compartment (SAC/ARC), where it colocalized with fluorescent
transferrin and fluorescent analogs of phosphatidylcholine and
sphingomyelin. In contrast, transport of DHE from the plasma membrane
to the trans-Golgi network was found to be very low. Vesicles
containing DHE traversed the cells in both directions, but vesicular
export of DHE from the SAC/ARC to the plasma membrane domains was low. Disruption of the microtubule cytoskeleton disturbed vesicular transport of DHE but not its enrichment in the apical (canalicular) membrane. Transport of DHE to the canalicular membrane after
photobleaching was very rapid (t1/2 = 1.6 min) and was largely ATP-independent in contrast to enrichment of DHE in the
SAC/ARC. Release of DHE from the canalicular membrane was also
ATP-independent but slower than the enrichment of sterol in the biliary
canaliculus (t1/2 = 5.4 min). Canalicular DHE could
completely redistribute to the basolateral plasma membrane but could
not transfer from one cell to the other cell of an HepG2 couplet. We
conclude that sterol shuttles rapidly among the plasma membrane domains
and other membrane organelles and that this nonvesicular pathway
includes fast transbilayer migration.
*
This work was supported in part by Deutsche
Forschungsgemeinschaft Grant GK 268 (to A. H.), National Institutes of
Health Grant DK27083, and the Ara Parseghian Medical Research
Foundation grant (to F. R. M.).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
Biochemistry, Rm. E-215, Weill Medical College of Cornell University, 1300 York Ave., New York, NY 10021. Fax: 212-746-8875;
E-mail:frmaxfie@med.cornell.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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