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J. Biol. Chem., Vol. 276, Issue 27, 24891-24900, July 6, 2001
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From the Apoprotein B (apoB) is the major protein of
liver-derived atherogenic lipoproteins. The net production of
apoB can be regulated by presecretory degradation mediated by the
ubiquitin-proteasome pathway and cytosolic hsp70. To further explore
the mechanisms of apoB degradation, we have established a cell-free
system in which degradation can be faithfully recapitulated. Human
apoB48 synthesized in vitro was translocated into
microsomes, glycosylated, and ubiquitinylated. Subsequent incubation
with rat hepatic cytosol led to proteasome-mediated degradation. To
explore whether hsp90 is required for apoB degradation, geldanamycin
(GA) was added during the degradation assay. GA increased the recovery
of microsomal apoB48 ~3-fold and disrupted the interaction between
hsp90 and apoB48. Confirming the hsp90 effect in the cell-free system,
we also found that transfection of hsp90 cDNA into rat hepatoma
cells enhanced apoB48 degradation. Finally, apoB48 degradation was
reconstituted in vitro using cytosol prepared from wild
type yeast. Notably, degradation was attenuated when apoB48-containing
microsomes were incubated with cytosol supplemented with GA or with
cytosol prepared from yeast strains with mutations in the homologues of
mammalian hsp70 and hsp90. Overall, our data suggest that hsp90
facilitates the interaction between endoplasmic reticulum-associated
apoB and components of the proteasomal pathway, perhaps in cooperation with hsp70.
Apoprotein B Degradation Is Promoted by the Molecular Chaperones
hsp90 and hsp70*
,
Departments of Medicine and
Biochemistry/Molecular Biology and The Cardiovascular Institute, Mount
Sinai School of Medicine, New York, New York 10029, the
§ Department of Biochemistry and Molecular Biology, Mount
Sinai School of Medicine, New York, New York 10029, and the
¶ Department of Biological Sciences, University of Pittsburgh,
Pittsburgh, Pennsylvania 15260
*
This work was supported by National Institutes of Health
Grant HL58541 (to E. A. F.), National Science Foundation Grant
MCB-9722889 (to J. L. B.), a grant from the Irma T. Hirschl Trust (to
A. J. C.), and a grant from the Zena and Michael A. Wiener
Cardiovascular Institute, Mount Sinai School of Medicine (to
E. A. F.).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: Box 1269, Mount
Sinai School of Medicine, 1 Gustave Levy Pl., New York, NY 10029. Tel.:
212-241-7152; Fax: 212-828-4178; E-mail: edward.fisher@mssm.edu.
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