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J. Biol. Chem., Vol. 277, Issue 19, 16470-16477, May 10, 2002

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Localization of Microsomal Triglyceride Transfer Protein in the Golgi
POSSIBLE ROLE IN THE ASSEMBLY OF CHYLOMICRONS^*

Emile Levy^§, Simona Stan, Edgard Delvin^¶, Daniel Ménard, Carol Shoulders^**, Carole Garofalo, Isabelle Slight, Ernest Seidman, Gaétan Mayer^§§, and Moïse Bendayan^§§

From the Departments of  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

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.

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