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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M300276-JLR200 on July 1, 2003

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Journal of Lipid Research, Vol. 44, 1841-1849, October 2003
Copyright © 2003 by American Society for Biochemistry and Molecular Biology

Subcellular localization of microsomal triglyceride transfer protein

Larry L. Swift1,*, Mei-Ying Zhu*, Bharati Kakkad{dagger}, Aneta Jovanovska*, M. Diana Neely*, Klara Valyi-Nagy*, Richard L. Roberts*, David E. Ong{dagger} and W. Gray Jerome*

* Departments of Pathology, Vanderbilt University School of Medicine, C-3321 Medical Center North, Nashville, TN 37232-2561
{dagger} Biochemistry, Vanderbilt University School of Medicine, C-3321 Medical Center North, Nashville, TN 37232-2561

1 To whom correspondence should be addressed. e-mail: larry.swift{at}vanderbilt.edu

Microsomal triglyceride transfer protein (MTP) is essential for the assembly of apolipoprotein B-containing lipoproteins. Within the endoplasmic reticulum, it transfers lipid from the membrane to the forming lipoprotein. Recent evidence suggests that it may also function within the Golgi apparatus. To address this hypothesis, we developed a polyclonal antibody to MTP and used it in a series of studies on mouse liver and McArdle-RH7777 (McA) cells. Western blot analysis demonstrated the presence of MTP within mouse hepatic-Golgi apparatus-rich fractions. In addition, in vitro lipid transfer assays demonstrated the presence of triglyceride transfer activity within the Golgi fractions. Immunohistochemical studies with mouse liver demonstrated the presence of MTP within all hepatocytes, but not in nonparenchymal cells. The subcellular location of MTP in McA cells was investigated using confocal microscopy. MTP colocalized with the trans-Golgi network (TGN) 38 and Golgi SNARE (soluble N-ethylmalemide-sensitive factor attachment protein receptor) of 28 kDa (GS28), markers for the trans- and cis-Golgi apparatus, respectively. Morphometric analyses indicated that ~17% of the MTP signal colocalized with the TGN38, while 33% of the trans-Golgi marker colocalized with the MTP. Approximately 17% of the MTP signal colocalized with the GS28, whereas 53% of the cis-Golgi marker colocalized with the MTP.

The results provide unequivocal evidence for the location of MTP within the Golgi apparatus, and further highlight the importance of this organelle in the assembly of lipoproteins.

Abbreviations: ER, endoplasmic reticulum; McA, McArdle-RH7777; MTP, microsomal triglyceride transfer protein; PDI, protein disulfide isomerase

Supplementary key words Golgi apparatus • very low density lipoprotein • intracellular transport


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