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Journal of Lipid Research, Vol 33, 1517-1526, Copyright © 1992 by Lipid Research, Inc.
Hepatic apolipoprotein J is secreted as a lipoprotein
BF Burkey, WD Stuart and JA Harmony
Developmental Biology Program, University of Cincinnati, College of Medicine, OH 45267-0575.
Apolipoprotein J (apoJ) is a unique glycoprotein thought to be involved in
a variety of physiological processes, including lipid transport, regulation
of complement function, sperm maturation, programmed cell death, and
membrane recycling. In the plasma, apoJ is associated with apoA-I in high
and very high density lipoproteins. In this report we demonstrate that
HepG2 human hepatocellular carcinoma cells secrete apoJ in association with
a significant amount of lipid, providing unequivocal evidence that apoJ can
transport lipids. The HepG2 cell line has provided important clues about
the structural organization of nascent lipoprotein particles. HepG2 cell
apoJ-containing lipoproteins are dense and heterogenous in size, ranging
from 100 to 910 kDa. Plasma and HepG2 cell apoJ-lipoproteins differ in size
distribution. Both have alpha 2 electrophoretic mobility, although their
average mobilities differ within the alpha 2 region. In contrast to plasma
apoJ-HDL which contain little triglyceride and which can associate with
apoA-I, HepG2 cell apoJ-lipoproteins are rich in triglyceride and lack
apoA-I. By implication, nascent apoJ-lipoproteins undergo plasma remodeling
that results in triglyceride depletion and apoA-I association. We propose
that the metabolic consequences of this remodeling play an important role
in lipid homeostasis in localized tissue environments, particularly where
organs are isolated from the blood by cellular barriers such as in testis
and brain. In such tissues, apoJ is expressed constitutively in high level
compared to other lipid transport proteins.

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Copyright © 1992 by the American Society for Biochemistry and Molecular Biology.
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