J. Lipid Res.
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A more recent version of this article appeared on March 1, 2005

Papers In Press, published online ahead of print December 16, 2004
J. Lipid Res., doi:10.1194/jlr.M400374-JLR200
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Submitted on September 29, 2004
Revised on November 24, 2004
Accepted on December 9, 2004

Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the insect apolipoprotein B homologue, apolipophorin-II/I

Marcel M. W. Smolenaars, Marcelle A. M. Kasperaitis, Paul E. Richardson, Kees W. Rodenburg, and Dick J. Van der Horst

Biochemical Physiology, Faculty of Biology, and Institute of Biomembranes, Utrecht University, Utrecht 3584 CH

Corresponding Author: m.m.w.smolenaars{at}bio.uu.nl

The biosynthesis of neutral fat-transporting lipoproteins involves the lipidation of their non-exchangeable apolipoprotein. In contrast to its mammalian homologue apolipoprotein B, however, insect apolipophorin-II/I (apoLp-II/I) is cleaved post-translationally at a consensus substrate sequence for furin, resulting in the appearance of two apolipoproteins in insect lipoprotein. To characterize the cleavage process, a truncated cDNA encoding the N-terminal 38% of Locusta migratoria apoLp-II/I, including the cleavage site, was expressed in insect Sf9 cells. This resulted in the secretion of correctly processed apoLp-II and truncated apoLp-I. The cleavage could be impaired by the furin inhibitor decRVKRcmk as well as mutagenesis of the consensus substrate sequence for furin, as evidenced by the secretion of uncleaved apoLp-II/I-38. Treatment of L. migratoria fat body, the physiological site of lipoprotein biosynthesis, with decRVKRcmk, similarly resulted in the secretion of uncleaved apoLp-II/I, that was integrated in lipoprotein particles of buoyant density identical to wild-type high-density lipophorin (HDLp). These results show that apoLp-II/I is post-translationally cleaved by an insect furin, and that biosynthesis and secretion of HDLp can occur independent of this processing step. Structure modeling indicates that the cleavage of apoLp-II/I represents a molecular adaptation in homologous apolipoprotein structures. We propose that cleavage enables specific features of insect lipoproteins, such as low-density lipoprotein formation, endocytic recycling, or involvement in coagulation.


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