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(Received for publication, March 18, 1997, and in revised form, June 19, 1997)
From the Two ALLN
(N-acetyl-leucyl-leucyl-norleucinal)-sensitive endoplasmic
reticulum (ER)-localized proteases (ER-60 and ER-72) were recently
purified from rat liver. We used an antibody to rat ER-60 to
investigate the possible role of this protease in apolipoprotein B
(apoB) degradation. First, immunoprecipitation and immunoblotting experiments with the anti-rat ER-60 antibody suggested that HepG2 cells
contain a homologue of ER-60 with an approximate molecular mass of
58-60 kDa. The ER-60 homologue was mostly associated with the luminal
contents of HepG2 microsomes. Evidence from co-immunoprecipitation and
cross-linking experiments appear to suggest that the ER-60 homologue in
HepG2 cells is associated with apoB intracellularly. A small pool of
apoB was recovered when HepG2 lysates were subjected to
immunoprecipitation with anti-rat ER-60 antibody followed by a second
immunoprecipitation with anti-apoB antibody. Furthermore, cross-linking
of permeabilized cells with dithiobis(succinimidylpropionate) further
demonstrated association of apoB with the ER-60 homologue in HepG2
cells. Three polypeptides with molecular masses of 78, 66, and 50 kDa
were consistently found to be associated with apoB as well as the
58-kDa ER-60 homologue. The 78-kDa protein associated with both apoB
and ER-60 appeared to represent immunoglobulin heavy chain-binding
protein (BiP) based on immunoprecipitation with a monoclonal antibody.
Cross-linking and immunoblotting experiments suggested the association
of the 78-kDa BiP with both the 58-kDa ER-60 homologue as well as the
550-kDa apoB.
In summary, the data suggests that HepG2 cells contain a 58-kDa protein
which is homologous to the rat liver ER-60 in size, antigenecity, and
intracellular localization. The ER-60 homologue in HepG2 cells appears
to be closely associated with apoB, as well as other proteins possibly
representing ER chaperones such as BiP. We hypothesize that the ER-60
homologue may be involved in the degradation of apoB in the ER lumen of
HepG2 cells.
Volume 272, Number 36,
Issue of September 5, 1997
pp. 22489-22494
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Department of Chemistry and Biochemistry,
University of Windsor, Windsor, Ontario, N9B 3P4 Canada and the
¶ Research Institute for Food Science, Kyoto University, Uji,
Kyoto 611, Japan
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