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J. Biol. Chem., Vol. 276, Issue 42, 39476-39483, October 19, 2001
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From the A human genetic disorder, Tangier disease, has
been linked recently to mutations in ATP-binding cassette protein A1
(ABCA1). In addition to its function in apoprotein
A-I-mediated lipid removal, ABCA1 was also shown to be a
phosphatidylserine (PS) translocase that facilitates PS exofacial
flipping. This PS translocation is crucial for the plasma membrane to
produce protrusions enabling the engulfment of apoptotic cells. In this
report, we show that ABCA1 also plays a role in endocytosis.
Receptor-mediated endocytosis, probed by both transferrin and low
density lipoprotein, is up-regulated by more than 50% in homozygous
Tangier fibroblasts in comparison with controls. Fluid-phase uptake is
increased similarly. We also demonstrate that bulk membrane flow,
including lipid endocytosis and exocytosis, is accelerated greatly in
Tangier cells. Moreover, endocytosis is similarly enhanced in normal
fibroblasts when ABCA1 function is inhibited by glyburide, whereas
glyburide has no effect on endocytosis in Tangier cells. In addition,
we demonstrate a decreased annexin V binding in Tangier fibroblasts as
compared with controls, supporting the notion that PS transmembrane
distribution is indeed defective in the presence of ABCA1 mutations.
Furthermore, adding a PS analog to the exofacial leaflet of the plasma
membrane normalizes endocytosis in Tangier cells. Taken together, these data demonstrate that ABCA1 plays an important role in endocytosis. We
speculate that this is related to the PS translocase function of
ABCA1. A loss of functional ABCA1, as in the case of Tangier cells, enhances membrane inward bending and facilitates endocytosis.
Endocytosis Is Enhanced in Tangier Fibroblasts
POSSIBLE ROLE OF ATP-BINDING CASSETTE PROTEIN A1 IN ENDOSOMAL
VESICULAR TRANSPORT*
§,§
Lipoprotein and Atherosclerosis Group,
University of Ottawa Heart Institute, 40 Ruskin Street, Ottawa, Ontario
K1Y 4W7, Canada and the ¶ Division of Cardiology,
McGill University Health Center, Montreal, Quebec H3A 1A1,
Canada
*
This work was supported by a Canadian Institutes of Health
Research (CIHR) Group Grant in Atherosclerosis (44360) (to
R. M.) and CIHR/Wyeth-Ayerst Chair in Cardiovascular Disease (to
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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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