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A more recent version of this article appeared on January 1, 2005

Papers In Press, published online ahead of print November 1, 2004
J. Lipid Res., doi:10.1194/jlr.M400247-JLR200
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Submitted on June 28, 2004
Revised on September 22, 2004
Accepted on October 22, 2004

Potential role of ABCA7 in cellular lipid efflux to apoA-I

Patrick Linsel-Nitschke, Andreas W. Jehle, Jing Shan, Guoqing Cao, Desa Bacic, Debin Lan, Nan Wang, and Alan R. Tall

Medicine Dept., Columbia University, New York, NY 10032

Corresponding Author: pl2031{at}columbia.edu

ABCA7 is homologous to ABCA1 and has recently been shown in cell culture to bind apoA-I and promote efflux of phospholipids. However, it is not known if ABCA7 promotes lipid efflux in vivo. When expressed in human embryonic kidney (HEK) 293 cells, both human and mouse ABCA7 promoted phospholipid efflux to apoA-I, but no detectable cholesterol efflux. However, genetic knock-down of ABCA7 in mouse peritoneal macrophages did not affect phospholipid or cholesterol efflux to apoA-I. Moreover, in ABCA1-/- macrophages there was no detectable apoA-I stimulated phospholipid efflux, inconsistent with a residual role of ABCA7. In contrast to plasma membrane localization of ABCA7 in transfected embryonic kidney cells, immunofluorescence-microscopy of endogenous ABCA7 in macrophages showed a predominantly intracellular localization of the protein. Strikingly, immunofluorescence studies of adult mouse kidney revealed an apical brush border membrane localization of ABCA7 in the proximal tubule, suggesting that ABCA7 may come in contact with apoA-I in the glomerular filtrate. Although ABCA7 does not contribute to apolipoprotein-mediated lipid efflux in resting macrophages, its cell surface location in the kidney suggests it could serve such a role in tissue microenvironments.


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