Lipid Transport

Horst, Dick J. Van der

doi:10.1016/b0-44-451924-6/00055-7

Cited by 15 publications

(17 citation statements)

References 138 publications

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“…Their crucial role in the mobilization of lipids is well known (e.g. review articles - Canavoso et al, 2001;Gäde & Goldsworthy, 2003;Van der Horst & Ryan, 2005), but they are also involved in a number of accompanying processes (Kodrík, 2008). Currently, almost 50 different AKHs have been characterized and their physiological effects investigated in insects belonging to various insect orders (Gäde et al, 1997;Gäde, 2009).…”

Section: Introductionmentioning

confidence: 99%

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Analysis of the lipids mobilized by adipokinetic hormones in the firebug Pyrrhocoris apterus (Heteroptera: Pyrrhocoridae)

Bártů¹,

Tomčala²,

Socha³

et al. 2010

Eur. J. Entomol.

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Abstract. Effects of two adipokinetic hormones (Pyrap-AKH and Peram-CAH-II) on the presence of diacylglycerol (DG) molecular species and their fatty acid (FA) constituents in the haemolymph of the firebug Pyrrhocoris apterus were investigated using liquid chromatography (HPLC) and electrospray ionization mass spectrometry (ESI-MS). The results show that DGs with characteristic FAs are preferentially mobilized from the fat body (FB) by the action of both the AKHs produced by P. apterus. Both the macropterous and brachypterous morphs have similar DG and FA profiles. A difference in the action of the Pyrap-AKH and the Peram-CAH-II, however, results in distinct differences in the distribution of FAs in the macropterous morph. It seems that C16 to a slight extent and unsaturated C18 FAs mainly play a dominant role in the AKH based action, in particular linoleic acid (18:2), which represents 50-60% of the total DG mobilized. The metabolically active C16 and C18 FAs are preferentially absorbed from the linden seeds and accumulated in the FB. The relationships between AKH action and FA distribution in DGs in P. apterus, compared to other insect species are summarized and discussed in detail.

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Section: Introductionmentioning

confidence: 99%

“…The LDLp transports the DGs to target tissues (mostly muscles) where the DGs are hydrolyzed by lipophorin lipase to free FAs and glycerol. Then, the apoLp-III dissociates from LDLp and is converted to HDLp, which returns to the FB to transport the next DG molecule (Canavoso et al, 2001; Van der Horst & Ryan, 2005).…”

Section: Introductionmentioning

confidence: 99%

Analysis of the lipids mobilized by adipokinetic hormones in the firebug Pyrrhocoris apterus (Heteroptera: Pyrrhocoridae)

Bártů¹,

Tomčala²,

Socha³

et al. 2010

Eur. J. Entomol.

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“…In contrast to apoB, apoLp-II/I is cleaved during lipoprotein biosynthesis, resulting in the presence of two apolipoproteins in the secreted insect lipoprotein, apoLp-I and apoLp-II (8)(9)(10)(11)(12); for reviews, see Refs. [13][14][15][16][17]. Cleavage of apoLp-II/I is not essential for lipophorin biogenesis, as uncleaved apoLp-II/I is also able to form a lipoprotein (11).…”

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confidence: 99%

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

Smolenaars

Morrée

Kerver

et al. 2007

Journal of Lipid Research

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Lipoproteins transport lipids in the circulation of an evolutionally wide diversity of animals. The pathway for lipoprotein biogenesis has been revealed to a large extent in mammals only, in which 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 a-helices and b-strands, organized along the protein as N-a 1 -b-a 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 the formation of a buoyant high density lipoprotein requires the amphipathic b cluster. Coexpression of apoLp-II/I with the MTP homolog of Drosophila melanogaster affected insect lipoprotein biogenesis quantitatively as well as qualitatively, as the secretion of apoLp-II/I proteins was increased severalfold and the buoyant density of the secreted lipoprotein decreased concomitantly, indicative of augmented lipidation. Based on these 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. Lipoproteins function in the transport of lipids in the circulation of vertebrates as well as invertebrates. In mammals, the biosynthesis of these macromolecular proteinlipid complexes occurring in liver and intestine involves the intracellular transfer and subsequent stabilization of lipids onto a single protein component, the nonexchangeable apolipoprotein B (apoB) (for reviews, see Refs. 1-7).The major lipoprotein of insects, lipophorin, is stabilized by apolipopoteins derived from apolipophorin II/I (apoLp-II/I), a homolog of apoB (8). In contrast to apoB, apoLp-II/I is cleaved during lipoprotein biosynthesis, resulting in the presence of two apolipoproteins in the secreted insect lipoprotein, apoLp-I and apoLp-II (8-12; for reviews, see Refs. 13-17). Cleavage of apoLp-II/I is not essential for lipophorin biogenesis, as uncleaved apoLp-II/I is also able to form a lipoprotein (11). Lipophorin is produced in cells of the fat body, an organ that combines the functions of liver and adipose tissues in vertebrates. Lipophorin is secreted with a buoyant density in the high density or very high density lipoprotein range, dependent on the species (18)(19)(20)(21)(22). Accordingly, lipophorin contains far fewer associated lipids than apoB lipoproteins that are secreted as very low density lipoproteins or chylomicrons. Moreover, the...

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“…Lp functions as a reusable lipid shuttle that operates without internalization of the protein portion of the Lp. The transfer of lipids is facilitated by a lipid transfer particle (4)(5)(6). However, it has been shown that high density lipophorin (HDLp) binds to lipophorin receptor (LpR) on the cell surface and is sequestered via receptor-mediated endocytosis (7).…”

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confidence: 99%

Lipophorin receptor of Bombyx mori: cDNA cloning, genomic structure, alternative splicing, and isolation of a new isoform

Gopalapillai¹,

Kadono-Okuda

Tsuchida

et al. 2006

Journal of Lipid Research

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Lipid Transport

Cited by 15 publications

References 138 publications

Analysis of the lipids mobilized by adipokinetic hormones in the firebug Pyrrhocoris apterus (Heteroptera: Pyrrhocoridae)

Analysis of the lipids mobilized by adipokinetic hormones in the firebug Pyrrhocoris apterus (Heteroptera: Pyrrhocoridae)

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

Lipophorin receptor of Bombyx mori: cDNA cloning, genomic structure, alternative splicing, and isolation of a new isoform

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