首页> 外文期刊>Biochimica et biophysica acta. Gene structure and expression >Up-regulation of fatty acid-binding proteins during hibernation in the little brown bat, Myotis lucifugus
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Up-regulation of fatty acid-binding proteins during hibernation in the little brown bat, Myotis lucifugus

机译:小棕蝙蝠冬眠时冬眠期间脂肪酸结合蛋白的上调

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摘要

Hibernating animals rely primarily on lipids throughout winter as their primary fuel source, thus it is hypothesized that an increase in genes and proteins relating to lipid transport will increase accordingly. The cloning and expression of heart type fatty acid-binding protein (h-fabp) from a mammalian hibernator, the little brown bat Myotis lucifugus, is presented. Northern blot analysis revealed that transcript levels of h-fabp were significantly higher during hibernation in brown adipose tissue and skeletal muscle compared with levels in euthermic bats. Similarly, heterologous probing with rat adipose type a-fabp found 3.9-fold higher levels of a-fabp transcripts in brown adipose from hibernating animals. Levels of A- and H-FABP protein were quantified in tissues of euthermic versus hibernating animals by Western blotting. A-FABP was 4-fold higher in brown adipose of hibernating, compared with euthermic bats, whereas H-FABP was significantly higher in hibernator brown adipose, heart and skeletal muscle. The present work implicates FABPs as important elements related to the hibernating state in mammals; alterations in gene and protein expression along with amino acid substitutions are shown. These likely contribute to optimizing the function of FABPs at the low body temperatures (near 0 ℃) experienced in the hibernating state.
机译:整个冬季,冬眠的动物主要依靠脂质作为其主要燃料来源,因此可以推测,与脂质运输有关的基因和蛋白质的增加将相应增加。介绍了从哺乳动物冬眠者小棕蝙蝠Myotis lucifugus克隆并表达心脏型脂肪酸结合蛋白(h-fabp)。 Northern印迹分析表明,与正常蝙蝠相比,在棕色脂肪组织和骨骼肌中,冬眠期间h-fabp的转录水平明显更高。同样,用大鼠脂肪型a-fabp进行异源探测发现,来自冬眠动物的棕色脂肪中a-fabp转录水平高3.9倍。通过Western印迹法定量对处于温和与冬眠状态的动物组织中的A-和H-FABP蛋白水平。与正常蝙蝠相比,冬眠棕色脂肪中的A-FABP高4倍,而冬眠棕色脂肪,心脏和骨骼肌中的H-FABP显着更高。目前的工作暗示FABPs是与哺乳动物冬眠状态有关的重要因素。显示了基因和蛋白质表达的改变以及氨基酸取代。这些可能有助于优化FABP在冬眠状态下的低体温(接近0℃)下的功能。

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