Biochemical and cellular characterization of lipophorin–midgut interaction in the hematophagous Panstrongylus megistus (Hemiptera: Reduviidae)

Fruttero, Leonardo L.; Rubiolo, Edilberto R.; Canavoso, Lilián Etelvina

doi:10.1016/j.ibmb.2009.01.009

Cited by 16 publications

(29 citation statements)

References 44 publications

(76 reference statements)

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“…Unless otherwise stated, insects that consumed a blood meal of approximately twofold their body weight (240 ± 15 mg) were selected for the experiments (Canavoso et al, 2004a;Fruttero et al, 2009). …”

Section: Insectsmentioning

confidence: 99%

“…Lipophorin was isolated from the hemolymph of fifth instar nymphs by KBr gradient ultracentrifugation followed by fractionation on Sepharose 6B as described elsewhere (Fruttero et al, 2009).…”

Section: Lipophorin Purification and Fluorescent Labelingmentioning

confidence: 99%

“…For the in vivo functional experiments, lipophorin was labeled in its phospholipid moiety with the non-exchangeable fluorophore DiI (Lp-DiI) (Via and Smith, 1986) as described previously (Fruttero et al, 2009). Lipophorin was also labeled on its exchangeable lipid fraction with the fluorescent palmitic acid analog Bodipy FL C16 (Lp-Bodipy-FA) (Martin-Nizard et al, 1987;Fruttero et al, 2011).…”

Section: Lipophorin Purification and Fluorescent Labelingmentioning

confidence: 99%

“…After blood feeding, phosphatidate phosphohydrolase and triacylglycerol lipase play a key role in regulating intracellular diacylglycerol synthesis in the midgut as well as its export to the hemolymph via lipophorin (Canavoso et al, 2004a). The biochemical and cellular characterization of lipophorin-midgut interaction in P. megistus was reported and the lack of an endocytic pathway for lipophorin in this tissue was also demonstrated (Fruttero et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

“…Despite the fact that the interaction of lipophorin with specific binding sites at the membrane of the cells has been characterized in several species (Van Antwerpen et al, 1988;Tsuchida and Wells, 1990;Bauerfeind and Komnick, 1992;Dantuma et al, 1996;Grillo et al, 2003;Lee et al, 2003;Fruttero et al, 2009), the identification of lipophorin docking receptors has been poorly successful. Recently, it has been reported that Cameo2 and SCRB15, two protein members of the CD36 family, may function as non-internalizing lipophorin receptors and/or transmembrane transporters facilitating the selective uptake of carotenoids in the silk gland of Bombyx mori (Sakudoh et al, 2010(Sakudoh et al, , 2013.…”

Section: Introductionmentioning

confidence: 99%

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β-chain of ATP synthase as a lipophorin binding protein and its role in lipid transfer in the midgut of Panstrongylus megistus (Hemiptera: Reduviidae)

Fruttero

Demartini

Rubiolo

et al. 2014

Insect Biochemistry and Molecular Biology

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Section: Insectsmentioning

confidence: 99%

Section: Lipophorin Purification and Fluorescent Labelingmentioning

confidence: 99%

Section: Lipophorin Purification and Fluorescent Labelingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

β-chain of ATP synthase as a lipophorin binding protein and its role in lipid transfer in the midgut of Panstrongylus megistus (Hemiptera: Reduviidae)

Fruttero

Demartini

Rubiolo

et al. 2014

Insect Biochemistry and Molecular Biology

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Rhodnius prolixus LIPOPHORIN: LIPID COMPOSITION AND EFFECT OF HIGH TEMPERATURE ON PHYSIOLOGICAL ROLE

Majerowicz

Cezimbra

Auger

et al. 2013

Arch Insect Biochem Physiol

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Lipophorin is a major lipoprotein that transports lipids in insects. In Rhodnius prolixus, it transports lipids from midgut and fat body to the oocytes. Analysis by thin-layer chromatography and densitometry identified the major lipid classes present in the lipoprotein as diacylglycerol, hydrocarbons, cholesterol, and phospholipids (PLs), mainly phosphatidylethanolamine and phosphatidylcholine. The effect of preincubation at elevated temperatures on lipophorin capacity to deliver or receive lipids was studied. Transfer of PLs to the ovaries was only inhibited after preincubation of lipophorin at temperatures higher than 55 °C. When it was pretreated at 75 °C, maximal inhibition of phospholipid transfer was observed after 3-min heating and no difference was observed after longer times, up to 60 min. The same activity was also obtained when lipophorin was heated for 20 min at 75 °C at protein concentrations from 0.2 to 10 mg/ml. After preincubation at 55 °C, the same rate of lipophorin loading with PLs at the fat body was still present, and 30% of the activity was observed at 75 °C. The effect of temperature on lipophorin was also analyzed by turbidity and intrinsic fluorescence determinations. Turbidity of a lipophorin solution started to increase after preincubations at temperatures higher than 65 °C. Emission fluorescence spectra were obtained for lipophorin, and the spectral area decreased after preincubations at 85 °C or above. These data indicated no difference in the spectral center of mass at any tested temperature. Altogether, these results demonstrate that lipophorin from R. prolixus is very resistant to high temperatures.

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OVARIAN NUTRITIONAL RESOURCES DURING THE REPRODUCTIVE CYCLE OF THE HEMATOPHAGOUSDIPETALOGASTER MAXIMA(HEMIPTERA: REDUVIIDAE): FOCUS ON LIPID METABOLISM

Leyria

Fruttero

Aguirre

et al. 2014

Arch Insect Biochem Physiol

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In this study, we have analyzed the changes of the ovarian nutritional resources in Dipetalogaster maxima at representative days of the reproductive cycle: previtellogenesis, vitellogenesis, as well as fasting-induced early and late atresia. As expected, the amounts of ovarian lipids, proteins, and glycogen increased significantly from previtellogenesis to vitellogenesis and then, diminished during atresia. However, lipids and protein stores found at the atretic stages were higher in comparison to those registered at previtellogenesis. Specific lipid staining of ovarian tissue sections evidenced remarkable changes in the shape, size, and distribution of lipid droplets throughout the reproductive cycle. The role of lipophorin (Lp) as a yolk protein precursor was analyzed by co-injecting Lp-OG (where OG is Oregon Green) and Lp-DiI (where DiI is 1,10-dioctadecyl-3,3,30,30-tetramethylindocarbocyanine) to follow the entire particle, demonstrating that both probes colocalized mainly in the yolk bodies of vitellogenic oocytes. Immunofluorescence assays also showed that Lp was associated to yolk bodies, supporting its endocytic pathway during vitellogenesis. The involvement of Lp in lipid delivery to oocytes was investigated in vivo by co-injecting fluorescent probes to follow the fate of the entire particle (Lp-DiI) and its lipid cargo (Lp-Bodipy-FA). Lp-DiI was readily incorporated by vitellogenic oocytes and no lipoprotein uptake was observed in terminal follicles of ovaries at atretic stages. Bodipy-FA was promptly transferred to vitellogenic oocytes and, to a much lesser extent, to previtellogenic follicles and to oocytes of ovarian tissue at atretic stages. Colocalization of Lp-DiI and Lp-Bodipy-FA inside yolk bodies indicated the relevance of Lp in the buildup of lipid and protein oocyte stores during vitellogenesis.

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Biochemical and cellular characterization of lipophorin–midgut interaction in the hematophagous Panstrongylus megistus (Hemiptera: Reduviidae)

Cited by 16 publications

References 44 publications

β-chain of ATP synthase as a lipophorin binding protein and its role in lipid transfer in the midgut of Panstrongylus megistus (Hemiptera: Reduviidae)

β-chain of ATP synthase as a lipophorin binding protein and its role in lipid transfer in the midgut of Panstrongylus megistus (Hemiptera: Reduviidae)

Rhodnius prolixus LIPOPHORIN: LIPID COMPOSITION AND EFFECT OF HIGH TEMPERATURE ON PHYSIOLOGICAL ROLE

OVARIAN NUTRITIONAL RESOURCES DURING THE REPRODUCTIVE CYCLE OF THE HEMATOPHAGOUSDIPETALOGASTER MAXIMA(HEMIPTERA: REDUVIIDAE): FOCUS ON LIPID METABOLISM

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