The process of lipid storage in insect oocytes: The involvement of β-chain of ATP synthase in lipophorin-mediated lipid transfer in the chagas’ disease vector Panstrongylus megistus (Hemiptera: Reduviidae)

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• 作者：Leonardo L. Fruttero^a ; ¹ ; Jimena Leyria^a ; ² ; Fabiá ; n O. Ramos^a ; ³ ; Raú ; l Stariolo^b ; Beatriz P. Settembrini^c ; ^d ; ⁴ ; Liliá ; n E. Canavoso^a ; ⁴ ; ^{lcanavo@fcq.unc.edu.ar}
• 关键词：β-ATPase ; β-chain of the ATP synthase complex ; Bodipy FL C16 ; 4 ; 4-difluoro-5 ; 7-dimethyl-4-bora-3a ; 4a-diaza-s-indacene-3-hexadecanoic acid ; Cameo2 ; C locus associated membrane protein homologous to a mammalian HDL receptor-2 ; CD36 ; cluster of differentiation 36 ; DAG ; diacylglycerol ; DAGTP ; diacylglycerol transport protein ; DIC ; differential interference contrast ; DiI ; 1 ; 10-dioctadecyl-3 ; 3 ; 30 ; 30-tetramethylindocarbocyanine ; DTSSP ; 3 ; 3&prime ; -dithiobis(sulfosuccinimidyl propionate) ; HDL ; high-densi
• 刊名：Journal of Insect Physiology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：96
• 期：Complete
• 页码：82-92
• 全文大小：2026 K
• 卷排序：96

文摘

β-ATPase was immunodetected in the microsomal fraction of the ovarian tissue. Lipophorin and β-ATPase partially co-localized in the membrane of the oocytes. β-ATPase blocking impaired the transfer of fatty acids from lipophorin to the oocytes. β-ATPase blocking did not affect lipophorin internalization in the oocytes. β-ATPase plays a role as a docking lipophorin receptor at the ovary.