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J. Biol. Chem., Vol. 277, Issue 19, 16470-16477, May 10, 2002
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From the Departments of Although a critical role of
microsomal transfer protein (MTP) has been recognized in the assembly
of nascent apolipoprotein B (apoB)-containing lipoproteins, it remains
unclear where and how MTP transfers lipids in the secretory
pathway during the maturational process of apoB lipidation. The aims of
this study were to determine whether MTP functions in the secretory
pathway as well as in the endoplasmic reticulum and whether its
large 97-kDa subunit interacts with the small 58-kDa protein disulfide
isomerase (PDI) subunit and apoB, particularly in the Golgi apparatus.
Using a high resolution immunogold approach combined with specific
polyclonal antibodies, the large and small subunits of MTP were
observed over the rough endoplasmic reticulum and the Golgi. Double
immunocytochemical detection unraveled the colocalization of MTP and
PDI as well as MTP and apoB in these same subcellular compartments. To
confirm the spatial contact of these proteins, Golgi fractions were
isolated, homogenized, and incubated with an anti-MTP large subunit
antibody. Immunoprecipitates were applied on SDS-PAGE and then
transferred on to nitrocellulose. Immunoblotting the membrane with PDI
and apoB antibodies confirmed the colocalization of these proteins with
MTP. Furthermore, MTP activity assay disclosed a substantial triglyceride transfer in the Golgi fractions. The occurrence of membrane-associated apoB in the Golgi, coupled with its interaction with active MTP, suggests an important role for the Golgi in the biogenesis of apoB-containing lipoproteins.
Localization of Microsomal Triglyceride Transfer Protein in
the Golgi
POSSIBLE ROLE IN THE ASSEMBLY OF CHYLOMICRONS*
§,,
,,,, Nutrition,
¶ Biochemistry, Pediatrics, and
§§ Pathology and Cell Biology, Hôpital
Sainte-Justine and University of Montreal, Montreal, Quebec H3T 1C5,
Canada, Group on the Functional Development and Physiopathology
of the Digestive Tract, Canadian Institute of Health Research and
Department of Cellular Biology, Faculty of Medicine, Université
de Sherbrooke, Sherbrooke, Quebec J1H 5N4, Canada, and the
** Department of Medicine, Hammersmith Hospital,
London W12 0NN, United Kingdom
*
This was supported by research grants from the Canadian
Institutes of Health Research (MT-10583) and the Canadian Heart
Association, as well as research scholarship awards from the
Fonds de la Recherche en Santé du Québec (to E. L.
and E. S.).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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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