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Papers In Press, published online ahead of print December 16, 2003
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Department of Biochemistry, Weill Medical College, Cornell University, New York, NY 10021
Corresponding Author: frmaxfie{at}med.cornell.edu
We analyzed the intracellular transport of high density lipoproteins (HDL) and its associated free sterol in polarized human hepatoma HepG2 cells. Using pulse-chase protocols, we demonstrated that HDL labeled with Alexa488 at the apoprotein (Alexa488-HDL) was internalized by a scavenger receptor SR-BI dependent process at the basolateral membrane and became enriched in a subapical/apical recycling compartment. Most Alexa488-HDL was rapidly recycled to the basolateral cell surface and released from cells. Within 30 min chase at 37°C, about 3% of the initial cell-associated Alexa488-HDL accumulated in the biliary canaliculus (BC) formed at the apical pole of polarized HepG2 cells. Even less Alexa488-HDL was transported to late endosomes or lysosomes. The fluorescent cholesterol analog dehydroergosterol (DHE) incorporated into Alexa488-HDL was delivered to the BC within a few minutes, independent of the labeled apoprotein. This transport did not require metabolic energy and could be blocked by antibodies against SR-BI. The fraction of cell-associated DHE transported to the BC was comparable when cells were incubated with either Alexa488-HDL containing DHE or with DHE bound to methyl-b-cyclodextrin. We conclude that rapid, nonvesicular transport of sterol to the BC and efficient recycling of HDL particles underlies the selective sorting of sterol from HDL in hepatocytes.
Revised on December 16, 2003
Accepted on December 2, 2003
Different transport routes for high density lipoprotein (HDL) and its associated free sterol in polarized hepatic cells
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