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J. Biol. Chem., Vol. 278, Issue 12, 10119-10127, March 21, 2003
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From the The pathways of hepatic intra- and
peri-cellular lipidation of apolipoprotein A-I (apoA-I) were studied by
infecting primary mouse hepatocytes from either apoA-I-deficient or
ABCA1-deficient mice with a recombinant adenovirus expressing the human
apoA-I (hapoA-I) cDNA (endo apoA-I) or incubating the hepatocytes
with exogenously added hapoA-I (exo apoA-I) and examining the
hapoA-I-containing lipoproteins formed. The cells, maintained in
serum-free medium, were labeled with
[3H]choline, and the cell medium was
separated by fast protein liquid chromatography or
immunoprecipitated to quantify labeled choline phospholipids
specifically associated with hapoA-I. With the apoA-I-deficient hepatocytes, the high density lipoprotein fraction formed with endo
apoA-I contained proportionally more phospholipids than that formed
with exo apoA-I. However, the lipoprotein size and electrophoretic mobility and phospholipid profiles were similar for exo apoA-I and endo
apoA-I. Taken together, these data demonstrate that a significant
proportion of hapoA-I is secreted from hepatocytes in a
phospholipidated state but that hapoA-I is also phospholipidated peri-cellularly. With primary hepatocytes from ABCA1-deficient mice,
the expression and net secretion of adenoviral-generated endogenous
apoA-I was unchanged compared with control mice, but 3H-phospholipids associated with endo apoA-I and exo apoA-I
decreased by 63 and 25%, respectively. The lipoprotein size and
electrophoretic migration and their phospholipid profiles remained
unchanged. In conclusion, we demonstrated that intracellular and
peri-cellular lipidation of apoA-I represent distinct and additive
pathways that may be regulated independently. Hepatocyte
expression of ABCA1 is central to the lipidation of newly synthesized
apoA-I but also contributes to the lipidation of exogenous apoA-I.
However, a significant basal level of phospholipidation occurs in the
absence of ABCA1.
The Lipidation by Hepatocytes of Human Apolipoprotein A-I Occurs
by Both ABCA1-dependent and -independent Pathways*
§¶,§
**,,,,, and
Lipoprotein and Atherosclerosis Research
Group, Departments of Pathology & Laboratory Medicine and Biochemistry,
Microbiology, and Immunology, University of Ottawa Heart Institute,
Ottawa, Ontario K1Y 4W7, Canada and the Centre d'Immunologie
INSERM-CNRS de Marseille Luminy, 13288 Marseille, France
*
This work was supported in part by a group grant from the
Canadian Institutes of Health Research.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.
To whom correspondence should be addressed: Lipoprotein and
Atherosclerosis Research Group, University of Ottawa Heart Inst., Rm.
H460, 40 Ruskin St., Ottawa, Ontario K1Y 4W7, Canada. Tel.: 613-761-5255; Fax: 613-761-5281; E-mail: ymarcel@ottawaheart.ca.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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