Function and immuno-localization of aquaporins in the Antarctic midge Belgica antarctica.

Function and immuno-localization of aquaporins in the Antarctic midge Belgica antarctica.
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DOI:
10.1016/j.jinsphys.2011.02.006
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发表时间:
2011-08
影响因子:
2.2
通讯作者:
Lee RE Jr
Lee RE Jr
中科院分区:
农林科学3区
文献类型:
--
作者:
Yi SX;Benoit JB;Elnitsky MA;Kaufmann N;Brodsky JL;Zeidel ML;Denlinger DL;Lee RE Jr

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水通道蛋白(Aquaporin,AQP)在跨细胞膜的水分运动中起着关键作用。在前人关于昆虫低温保护功能的报道的基础上,本研究考察了水通道蛋白在脱水、复水和冷冻反应中的作用,以及它们在南极吸虫贝尔吉卡南极洲(双翅目,摇蚊科)特定组织中的分布。当用氯化汞阻断水通道蛋白时,组织对高渗刺激的耐受性增加,而在低渗溶液中对过度水化的敏感性降低。阻断水通道蛋白降低了中肠和马氏管组织的耐寒能力,但脂肪体的细胞活力只有很小的变化。免疫定位显示,大多数幼虫组织中存在一种滴状蛋白(果蝇水孔蛋白)、AQP2和AQP3(水甘油孔蛋白)样蛋白。在成虫的肠道中也存在类似水滴和AQP2的蛋白,但在我们研究的任何组织中都没有检测到类似AQP4的蛋白。Western blotting表明,幼虫对脱水、复水和冷冻的反应增加了AQP2样蛋白的水平,而在成虫中,脱水提高了AQP2和AQP3样蛋白的水平。这些结果表明,水通道蛋白/水甘油孔蛋白在南极假单胞菌的水关系和耐寒性中起着至关重要的作用。
Aquaporin (AQP) water channel proteins play key roles in water movement across cell membranes. Extending previous reports of cryoprotective functions in insects, this study examines roles of AQPs in response to dehydration, rehydration, and freezing, and their distribution in specific tissues of the Antarctic midge, Belgica antarctica (Diptera, Chironomidae). When AQPs were blocked using mercuric chloride, tissue dehydration tolerance increased in response to hypertonic challenge, and susceptibility to overhydration decreased in a hypotonic solution. Blocking AQPs decreased the ability of tissues from the midgut and Malpighian tubules to tolerate freezing, but only minimal changes were noted in cellular viability of the fat body. Immuno-localization revealed that a DRIP-like protein (a Drosophila aquaporin), AQP2- and AQP3 (aquaglyceroporin)-like proteins were present in most larval tissues. DRIP- and AQP2-like proteins were also present in the gut of adult midges, but AQP4-like protein was not detectable in any tissues we examined. Western blotting indicated that larval AQP2-like protein levels were increased in response to dehydration, rehydration and freezing, whereas, in adults DRIP-, AQP2-, and AQP3-like proteins were elevated by dehydration. These results imply a vital role for aquaporin/aquaglyceroporins in water relations and freezing tolerance in B. antarctica.
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