Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens

Mullen, Lisa; Goldsworthy, G.J.

doi:10.1016/s0965-1748(03)00045-6

Cited by 75 publications

(47 citation statements)

References 33 publications

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“…Another aspect of the immune response, nodule formation, is also enhanced by co-injection of AKH-I with an immunogen such as LPS (Goldsworthy et al, 2003a). Intriguingly, the immunogen-induced changes in lipophorins and the exchangeable apoprotein, apolipophorin-III (apoLp-III) in the haemolymph of locusts shown previously (Mullen and Goldsworthy, 2003) are qualitatively identical to those brought about by AKH, including the mobilisation of diacylglycerol from the fat body, the appearance of low-density lipophorin (LDLp), and the virtual disappearance of free apoLp-III from the haemolymph. This provides strong circumstantial evidence to suggest that AKH could be released as part of the locust response to injected immunogens such as LPS or laminarin.…”

Section: Introductionmentioning

confidence: 76%

“…High and low density lipophorins and apoLp-III in the haemolymph were selectively precipitated using a method described previously (Goldsworthy et al, 1985;Mullen and Goldsworthy, 2003). Briefly, a 5 μL sample of fresh haemolymph was blown into 200 μL of heparin solution (0.375 % heparin sodium salt in 25 mM CaCl 2 , 3.8 mM NaCl) to precipitate the HDLp, followed by precipitation of LDLp in 5% EDTA from the supernatant.…”

Section: Isolation Of High Density Lipophorin (Hdlp) Low Density Lipmentioning

confidence: 99%

“…Total lipid (measured as vanillin-positive material) was measured as described previously (Mullen and Goldsworthy, 2003). Centrifuge pellets of HDLp and LDLp (from 5 μL of haemolymph) were solubilised in 1 mL of concentrated H 2 SO 4 .…”

Section: Measurement Of Lipid Concentration In Hdlp and Ldlp Pelletsmentioning

confidence: 99%

“…The protein concentration in the acetone-precipitated pellet (apoLp-III) was measured as described previously (Mullen and Goldsworthy, 2003) using a modification of an earlier method (Schacterle and Pollack, 1973). Briefly, precipitated protein was dissolved in 200 μL of 0.5 M NaOH, and 200 μL of copper reagent (10% NaHCO 3 , 0.1% (CHOH.COOK) 2 .½H 2 O), 0.05% CuSO 4 ) were added before the addition of Folin-Ciocalteu phenol reagent.…”

Section: Measurement Of Protein Concentrationmentioning

confidence: 99%

“…The most wellknown effects are lipid mobilisation and activation of glycogen phosphorylase in the fat body to provide energy for migratory flight (for review see Goldsworthy, 1990), although other actions include inhibition of the synthesis of protein, fatty acid and mRNA (Lee and Goldsworthy, 1995;Kodrik and Goldsworthy, 1994). Recently, however, it has been shown that in locusts injection of AKH can also influence immune responses (Goldsworthy et al, 2002a;Goldsworthy et al, 2003a;Goldsworthy et al, 2003b;Mullen and Goldsworthy, 2003). The orthopteran prophenoloxidase system is apparently located within haemocytes (Brehelin et al, 1989) and is activated by a serine protease cascade (Ashida, 1990) in response to recognition of non-self material within the haemocoel, and produces effector molecules such as cytotoxic quinones (for review see Ashida and Brey, 1998).…”

Section: Introductionmentioning

confidence: 99%

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Induced hyperlipaemia and immune challenge in locusts

Mullen

Lightfoot

Goldsworthy

2004

Journal of Insect Physiology

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Injections of immunogens, such as β-1,3-glucan or lipopolysaccharide (LPS), bring about a marked hyperlipaemia with associated changes in lipophorins and apolipophorin-III in the haemolymph of Locusta migratoria. These changes are similar to those observed after injection of adipokinetic hormone (AKH). The possibility that endogenous AKH is released as part of the response to these immunogens is investigated using passive immunisation against AKH-I, and measurement of AKH-I titre in the haemolymph after injection of immunogens. The data presented show that, despite the similarity of the changes brought about by the presence of immunogens in the haemolymph to those brought about by AKH, there is no release of endogenous AKH after injection of laminarin or LPS. A direct effect of the immunogens on release of neutral lipids by the fat body cannot be demonstrated in vitro, and the mechanism by which hyperlipaemia is induced during immune challenge remains uncertain.

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Section: Introductionmentioning

confidence: 76%

Section: Isolation Of High Density Lipophorin (Hdlp) Low Density Lipmentioning

confidence: 99%

Section: Measurement Of Lipid Concentration In Hdlp and Ldlp Pelletsmentioning

confidence: 99%

Section: Measurement Of Protein Concentrationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Induced hyperlipaemia and immune challenge in locusts

Mullen

Lightfoot

Goldsworthy

2004

Journal of Insect Physiology

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Molecular characterization and gene expression of apolipophorin III from the ghost moth, Thitarodes pui (Lepidoptera, Hepialidae)

Sun¹,

Yu²,

Wu³

et al. 2011

Arch Insect Biochem Physiol

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Apolipophorin III (apoLp-III) functions in lipid transport and immune activation in insects. We cloned a cDNA encoding putative apoLp-III from larvae of Thitarodes pui, a host species of Ophiocordyceps sinensis, with great economic importance in the Tibetan Plateau. Excluding a putative signal peptide of the first 20 amino acid residues, the 171-residue mature apoLp-III has a calculated molecular mass of 18,606 Da. T. pui apoLp-III shares little sequence homologies (<36%) with other apoLp-IIIs. Phylogenetic analysis reveals that T. pui apoLp-III belongs to a distinct, early diverging lineage of lepidopteran apoLp-IIIs. Homology modeling of T. pui apoLp-III shows a bundle of five amphipathic α-helices, including a short helix 3'. T. pui apoLp-III was constitutively expressed in larval fat body at lower levels than pupal and adult fat body. Significant induction of apoLp-III expression, associated with strongest nodulation response, was observed in both sixth and eighth instar larvae challenged with Beauveria bassiana conidia at 1 hr after inoculation, compared with saline-injected controls. The inoculation experiment as well as previous field studies revealed the relative susceptibility of the sixth instar to the entomopathogenic fungus. ApoLp-III transcripts in the infected sixth and eighth instars were found to be induced highest 2- and 14.7-fold, respectively, during the first 12 hr. In late-stage infection, the infected susceptible sixth instar showed decrease in apoLp-III expression followed by production of B. bassiana hyphal bodies, whereas the infected eighth instar showed longer lasting increase in the expression. These results suggest that apoLp-III might contribute to T. pui immune response against fungal pathogens.

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MOLECULAR CHARACTERIZATION OF AN APOLIPOPHORIN‐III GENE FROM THE CHINESE OAK SILKWORM, Antheraea pernyi (LEPIDOPTERA: SATURNIIDAE)

Liu

Lin

Yang

et al. 2014

Arch Insect Biochem Physiol

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Apolipophorin-III (ApoLp-III) acts in lipid transport, lipoprotein metabolism, and innate immunity in insects. In this study, an ApoLp-III gene of Antheraea pernyi pupae (Ap-ApoLp-III) was isolated and characterized. The full-length cDNA of Ap-ApoLp-III is 687 bp, including a 5'-untranslated region (UTR) of 40 bp, 3'-UTR of 86 bp and an open reading frame of 561 bp encoding a polypeptide of 186 amino acids that contains an Apolipophorin-III precursor domain (PF07464). The deduced Ap-apoLp-III protein sequence has 68, 59, and 23% identity with its orthologs of Manduca sexta, Bombyx mori, and Aedes aegypti, respectively. Phylogenetic analysis showed that the Ap-apoLp-III was close to that of Bombycoidea. qPCR analysis revealed that Ap-ApoLp-III expressed during the four developmental stages and in integument, fat body, and ovaries. After six types of microorganism infections, expression levels of the Ap-ApoLp-III gene were upregulated significantly at different time points compared with control. RNA interference (RNAi) of Ap-ApoLp-III showed that the expression of Ap-ApoLp-III was significantly downregulated using qPCR after injection of E. coli. We infer that the Ap-ApoLp-III gene acts in the innate immunity of A. pernyi.

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Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens

Cited by 75 publications

References 33 publications

Induced hyperlipaemia and immune challenge in locusts

Induced hyperlipaemia and immune challenge in locusts

Molecular characterization and gene expression of apolipophorin III from the ghost moth, Thitarodes pui (Lepidoptera, Hepialidae)

MOLECULAR CHARACTERIZATION OF AN APOLIPOPHORIN‐III GENE FROM THE CHINESE OAK SILKWORM, Antheraea pernyi (LEPIDOPTERA: SATURNIIDAE)

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