J. Lipid Res.
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A more recent version of this article appeared on September 1, 2007

Papers In Press, published online ahead of print June 13, 2007
J. Lipid Res., doi:10.1194/jlr.M600434-JLR200
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Submitted on September 29, 2006
Revised on May 29, 2007
Accepted on June 13, 2007

Insect lipoprotein biogenesis depends on an amphipathic beta cluster in apolipophorin-II/I and is stimulated by microsomal triglyceride transfer protein

Marcel M.W. Smolenaars, Antoine De Morrée, Jana Kerver, Dick J. Van der Horst, and Kees W. Rodenburg

Endocrinology and Metabolism, Utrecht University, Utrecht, Utrecht NL 3584 CH

Corresponding Author: c.w.rodenburg{at}uu.nl

Lipoproteins transport lipids in the circulation of an evolutionary wide diversity of animals. The pathway for lipoprotein biogenesis has been uncovered to a large extent in mammals only, where apolipoprotein B (apoB) acquires lipids via the assistance of microsomal triglyceride transfer protein (MTP) and binds them by means of amphipathic protein structures. To investigate whether this is a common mechanism for lipoprotein biogenesis in animals, we studied the structural elements involved in the assembly of the insect lipoprotein, lipophorin. LOCATE sequence analysis predicted that the insect lipoprotein precursor apolipophorin-II/I (apoLp-II/I) contains clusters of amphipathic -helices and -strands, organized along the protein as N-1--2-C, reminiscent of a truncated form of apoB. Recombinant expression of a series of C-terminal truncation variants of Locusta migratoria apoLp-II/I in an insect cell (Sf9) expression system revealed that formation of a buoyant high-density lipoprotein requires the amphipathic  cluster. Co-expression of apoLp-II/I with the MTP homolog of Drosophila melanogaster impacted insect lipoprotein biogenesis quantitatively as well as qualitatively, as the secretion of apoLp-II/I proteins was increased several-fold while the buoyant density of the secreted lipoprotein decreased concomitantly, indicative of augmented lipidation. Based on the above findings we propose that, despite specific modifications, the assembly of lipoproteins involves MTP as well as amphipathic structures in the apolipoprotein carrier, both in mammals and insects. Thus, lipoprotein biogenesis in animals appears to rely on structural elements that are of early metazoan origin.


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