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J. Biol. Chem., Vol. 278, Issue 22, 20367-20373, May 30, 2003

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A Drosophila Microsomal Triglyceride Transfer Protein Homolog Promotes the Assembly and Secretion of Human Apolipoprotein B

IMPLICATIONS FOR HUMAN AND INSECT LIPID TRANSPORT AND METABOLISM^*

Jeremy A. Sellers  , Li Hou , Humra Athar ¶, M. Mahmood Hussain ¶ and Gregory S. Shelness  ||

From the Department of Pathology, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157-1040 and the ^¶Department of Anatomy and Cell Biology and Pediatrics, Downstate Medical Center, State University of New York, Brooklyn, New York 11203

The assembly and secretion of triglyceride-rich lipoproteins in vertebrates requires apolipoprotein B (apoB) and the endoplasmic reticulum-localized cofactor, microsomal triglyceride transfer protein (MTP). Invertebrates, particularly insects, transport the majority of their neutral and polar lipids in lipophorins; however, the assembly of lipophorin precursor particles was presumed to be MTP-independent. A Drosophila melanogaster expressed gene sequence (CG9342), displaying 23% identity with human MTP, was recently identified. When coexpressed in COS cells, CG9342 promoted the assembly and secretion of apoB34 and apoB41 (N-terminal 34 and 41% of human apoB). The apoB34-containing particles assembled by human MTP and CG9342 displayed similar peak densities of 1.169 g/ml and similar lipid compositions. However, CG9342 displayed differential sensitivities to two inhibitors of human MTP and low vesicle-based lipid transfer activity, in vitro. In addition, important predicted structural distinctions exist between the human and Drosophila proteins suggesting overlapping but not identical functional roles. We conclude that CG9342 and human MTP are orthologs that share only a subset of functions, consistent with known differences in intracellular and extracellular aspects of vertebrate and invertebrate lipid transport and metabolism.

Received for publication, January 9, 2003 , and in revised form, March 23, 2003.

^* This work was supported in part by National Institutes of Health (NIH) Grants HL49373 (to G. S. S.) and DK46900 and HL64272 (to M. M. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported as a Predoctoral Fellow by NIH Training Grant HL07867.

^|| To whom correspondence should be addressed. Tel.: 336-716-3282; Fax: 336-716-6279; E-mail: gshelnes{at}wfubmc.edu.

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