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J. Biol. Chem., Vol. 278, Issue 9, 7459-7468, February 28, 2003
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From the Department of Physiology and Biophysics, Center for
Advanced Biomedical Research, Boston University School of Medicine,
Boston, Massachusetts 02118
We have previously demonstrated that endoplasmic
reticulum (ER)-resident molecular chaperones interact with
apolipoprotein B-100 (apoB) during its maturation. The initial stages
of apoB folding occur while it is bound to the ER membrane, where it
becomes partially lipidated to form a primordial intermediate. We
determined whether this intermediate is dependent on the assistance of
molecular chaperones for its subsequent folding steps. To that end,
microsomes were prepared from HepG2 cells and luminal contents were
subjected to KBr density gradient centrifugation. Immunoprecipitation
of apoB followed by Western blotting showed that the luminal pool floated at a density of 1.12 g/ml and, like the membrane-bound pool,
was associated with GRP94, ERp72, BiP, calreticulin, and cyclophilin B. Except for calreticulin, chaperone/apoB ratio in the lumen was
severalfold higher than that in the membrane, suggesting a role for
these chaperones both in facilitating the release of the primordial
intermediate into the ER lumen and in providing stability. Subcellular
fractionation on sucrose gradients showed that apoB in the Golgi was
associated with the same array of chaperones as the pool of apoB
recovered from heavy microsomes containing the ER, except that
chaperone/apoB ratio was lower. KBr density gradient fractionation
showed that the major pool of luminal apoB in the Golgi was recovered
from 1.02 < d < 1.08 g/ml, whereas apoB in ER
was recovered primarily from 1.08 < d < 1.2 g/ml. Both fractions were associated with the same spectrum of
chaperones. Together with the finding that GRP94 was found associated
with sialylated apoB, we conclude that correct folding of apoB is
dependent on the assistance of molecular chaperone, which play
multiple roles in its maturation throughout the secretory pathway
including distal compartments such as the trans-Golgi network.
Nascent Lipidated Apolipoprotein B Is Transported to the Golgi as
an Incompletely Folded Intermediate as Probed by Its Association with
Network of Endoplasmic Reticulum Molecular Chaperones, GRP94, ERp72,
BiP, Calreticulin, and Cyclophilin B*
*
This work was supported by National Institutes of Health
Grants HL-58833 and HL-26335.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 all correspondence should be addressed: Dept. of
Physiology and Biophysics, Center for Advanced Biomedical Research, Boston University School of Medicine, 715 Albany St., Boston, MA 02118. Tel.: 617-638-4012; Fax: 617-638-4041; E-mail:
haya@bu.edu.
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