Lipid Transport

Horst, Dick J. Van der

doi:10.1016/b978-0-12-384747-8.10009-1

Cited by 12 publications

(13 citation statements)

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“…Unsurprisingly total TAG levels were (a) the most abundant class of the lipids analysed and (b) underwent the most pronounced decline in flown moths (1.8‐fold reduction from 739.6 to 410.5 nmol/g fresh weight, p = .006; Figure 3a). Sustained flight activity in insects is powered primarily by the mobilization of TAG in the insect fat body into diacylglycerol (DAG), which is then shuttled in the haemolymph to the flight muscle (Van der Horst & Ryan, 2012). The role of phospholipid metabolism in insects is far less well understood although in this experiment we show a consistent depletion in each phospholipid class following flight (Figure 3b; see Figure for individual lipid species and Table for test statistics).…”

Section: Resultsmentioning

confidence: 99%

“…This requires an enormous amount of fuel consumption, metabolism and intracellular transport to the flight muscles. Given the well‐established hydrophobic binding capacity of OBPs and their over‐expression in H. armigera , it is possible that this group of proteins act as lipid transport carriers in H. armigera —the main flight fuel of migratory insects (Van der Horst & Ryan, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Odorant binding proteins promote flight activity in the migratory insect, Helicoverpa armigera

et al. 2020

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Odorant binding proteins promote flight activity in the migratory insect, Helicoverpa armigera

et al. 2020

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“…DAG, which is transported by lipophorin from the fat body to the milk gland, is the main lipid moiety provided for milk fat synthesis (15, 76, 101, 105). FFAs in the hemolymph are directly absorbed by the milk gland through passive diffusion and/or an uncharacterized protein-mediated mechanism (75, 121, 133). Lipids are likely directly incorporated into the milk to act as the milk fat source.…”

Section: Tsetse Lactation and Underlying Mechanismsmentioning

confidence: 99%

Adenotrophic Viviparity in Tsetse Flies: Potential for Population Control and as an Insect Model for Lactation

Benoit

Attardo

Baumann

et al. 2015

Annu. Rev. Entomol.

105

102

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Tsetse flies (Glossina spp.), vectors of African trypanosomes, are distinguished by their specialized reproductive biology, defined by adenotrophic viviparity (maternal nourishment of progeny by glandular secretions followed by live birth). This trait has evolved infrequently among insects and requires unique reproductive mechanisms. A key event in Glossina reproduction involves the transition between periods of lactation and nonlactation (dry periods). Increased lipolysis, nutrient transfer to the milk gland, and milk-specific protein production characterize lactation, which terminates at the birth of the progeny and is followed by a period of involution. The dry stage coincides with embryogenesis of the progeny, during which lipid reserves accumulate in preparation for the next round of lactation. The obligate bacterial symbiont Wigglesworthia glossinidia is critical to tsetse reproduction and likely provides B vitamins required for metabolic processes underlying lactation and/or progeny development. Here we describe findings that utilized transcriptomics, physiological assays, and RNA interference–based functional analysis to understand different components of adenotrophic viviparity in tsetse flies.

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“…Apolipophorin-III (ApoLp-III) is an amphipathic insect hemolymph protein that binds hydrophobically to lipoprotein surfaces and allows lipid transport in aqueous media (Van der Horst et al, 1993; Blacklock and Ryan, 1994). Homologous to a mammalian lipoprotein Apolipoprotein E, the insect ApoLp-III facilitates the transport of diacylglycerol (DAG) from fat body to flight muscles under the influence of adipokinetic hormones (Feingold et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Apolipophorin-III Acts as a Positive Regulator of Plasmodium Development in Anopheles stephensi

et al. 2017

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Apolipophorin III (ApoLp-III) is a well-known hemolymph protein having a functional role in lipid transport and immune responses of insects. Here we report the molecular and functional characterization of Anopheles stephensi Apolipophorin-III (AsApoLp-III) gene. This gene consists of 679 nucleotides arranged into two exons of 45 and 540 bp that give an ORF encoding 194 amino acid residues. Excluding a putative signal peptide of the first 19 amino acid residues, the 175-residues in mature AsApoLp-III protein has a calculated molecular mass of 22 kDa. Phylogenetic analysis revealed the divergence of mosquitoes (Order Diptera) ApoLp-III from their counterparts in moths (Order: Lepidoptera). Also, it revealed a close relatedness of AsApoLp-III to ApoLp-III of An. gambiae. AsApoLp-III mRNA expression is strongly induced in Plasmodium berghei infected mosquito midguts suggesting its crucial role in parasite development. AsApoLp-III silencing decreased P. berghei oocysts numbers by 7.7 fold against controls. These effects might be due to the interruption of AsApoLp-III mediated lipid delivery to the developing oocysts. In addition, nitric oxide synthase (NOS), an antiplasmodial gene, is also highly induced in AsApoLp-III silenced midguts suggesting that this gene acts like an agonist and protects Plasmodium against the mosquito immunity.

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Lipid Transport

Cited by 12 publications

References 252 publications

Odorant binding proteins promote flight activity in the migratory insect, Helicoverpa armigera

Odorant binding proteins promote flight activity in the migratory insect, Helicoverpa armigera

Adenotrophic Viviparity in Tsetse Flies: Potential for Population Control and as an Insect Model for Lactation

Apolipophorin-III Acts as a Positive Regulator of Plasmodium Development in Anopheles stephensi

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