2014
DOI: 10.1016/j.ibmb.2014.06.002
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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)

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Cited by 20 publications
(15 citation statements)
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“…3 ). Although previously thought to only have a role in the mitochondria, ATPases are present in the plasma membrane of the insect midgut and salivary glands and have been shown to have a role in lipid transport 35 , 36 .…”
Section: Resultsmentioning
confidence: 99%
“…3 ). Although previously thought to only have a role in the mitochondria, ATPases are present in the plasma membrane of the insect midgut and salivary glands and have been shown to have a role in lipid transport 35 , 36 .…”
Section: Resultsmentioning
confidence: 99%
“…Apolipophorin has a long half-life, calculated to exceed one day in some species [ 6 ], and each particle participates in multiple cycles of lipid loading and unloading in tissues without apparent degradation of the Apolipophorin moiety [ 7 ]. Biochemical and kinetic studies indicated that the interaction of lipophorin with cells is mediated through specific receptors [ 8 11 ]. At the molecular level, the best characterized are the lipophorin receptors of the Low Density Lipoprotein Receptor (LDLR) family, which were initially identified by their capacity to induce lipophorin endocytosis when overexpressed in a cell culture system [ 12 ].…”
Section: Introductionmentioning
confidence: 99%
“…The mechanism of Stunted release remains to be clarified. The beta subunit of the ectopic form of F 1 F 0 -ATP synthase is a receptor for lipoproteins (18)(19)(20)(21), which serve as cargos for proteins and peptides. In addition, Drosophila lipid transfer particle-containing lipoproteins were shown to act on the larval brain to control systemic insulin signaling in response to nutrition (23).…”
mentioning
confidence: 99%