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(Received for publication, May 9, 1996, and in revised form, June 5, 1996)
From the The sterol binding agent
2-hydroxypropyl-
Volume 271, Number 35,
Issue of August 30, 1996
pp. 21604-21613
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Lipid Cell Biology Section, Laboratory of
Cell Biochemistry and Biology, NIDDK, the ¶ Developmental and
Metabolic Neurology Branch, NINDS, National Institutes of Health,
Bethesda, Maryland 20892, the 
Gerontology Research Center,
NIA, National Institutes of Health, Baltimore, Maryland 21224, and
the '' Marine Biological Laboratory, Woods Hole,
Massachusetts 02543
-cyclodextrin is shown to be a convenient and useful
experimental tool to probe intracellular pathways of cholesterol
transport. Biochemical and cytochemical studies reveal that
cyclodextrin specifically removes plasma membrane cholesterol.
Depletion of plasma membrane sphingomyelin greatly accelerated
cyclodextrin-mediated cholesterol removal. Cholesterol arriving at the
plasma membrane from lysosomes and the endoplasmic reticulum was also
removed by cyclodextrin. Cellular cholesterol esterification linked to
the mobilization of cholesterol from lysosomes was strongly attenuated
by cyclodextrin, suggesting that the major portion of endocytosed
cholesterol is delivered from lysosomes to the endoplasmic reticulum
via the plasma membrane. Evidence for translocation of lysosomal
cholesterol to the endoplasmic reticulum by a plasma
membrane-independent pathway is provided by the finding that
cyclodextrin loses its ability to suppress esterification when plasma
membrane sphingomyelin is depleted. The Golgi apparatus appears to play
an active role in directing the relocation of lysosomal cholesterol to
the plasma membrane since brefeldin A also abrogated
cyclodextrin-mediated suppression of cholesterol esterification. Using
cyclodextrin we further show that attenuated esterification of
lysosomal cholesterol in Niemann-Pick C cells reflects defective
translocation of cholesterol to the plasma membrane that may be linked
to abnormal Golgi trafficking.
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G. H. Hans |
