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A more recent version of this article appeared on September 1, 2002
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Submitted on January 15, 2002
Revised on May 10, 2002
Accepted on June 13, 2002
1 Department of Molecular Medicine, National Public Health Institute, Biomedicum Helsinki, Haartmaninkatu 8, 00251 Helsinki, Finland
2 Department of Cell Biology, University Medical Center Utrecht and Center for Biomedical Genetics, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands
3 Institute of Biomedicine, PL 63, 00014 University of Helsinki, Finland
* Corresponding author. E-mail address: elina.ikonen{at}ktl.fi.
To analyze the contribution of vesicular trafficking pathways in cellular cholesterol transport we examined the effects of selected endosomal Rab proteins on cholesterol distribution by filipin staining. Transient overexpression of Rab11 resulted in prominent accumulation of free cholesterol in Rab11 positive organelles that sequestered transferrin receptors and internalized transferrin. Sphingolipids were selectively redistributed as pyrene-sphingomyelin and sulfatide co-sequestered with Rab11 positive endosomes while globotriaosyl ceramide and GM2 ganglioside did not. Rab11 overexpression did not perturb the transport of DiI-labeled LDL to late endosomes or the NPC1-induced late endosomal cholesterol clearance in Niemann-Pick type C patient cells. However, Rab11 overexpression inhibited cellular cholesterol esterification in a LDL-independent manner. This effect could be overcome by introducing cholesterol to the plasma membrane by using cyclodextrin as a carrier. These results suggest that in Rab11 overexpressing cells, deposition of cholesterol in recycling endosomes results in its impaired esterification, presumably due to defective recycling of cholesterol to the plasma membrane. The findings point to the importance of the recycling endosomes in regulating cholesterol and sphingolipid trafficking and cellular cholesterol homeostasis.
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