腺苷一磷酸（AMP）会降低骨骼肌线粒体的效率。
AMP decreases the efficiency of skeletal-muscle mitochondria.
作者信息
Cadenas S, Buckingham J A, St-Pierre J, Dickinson K, Jones R B, Brand M D
机构信息
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
出版信息
Biochem J. 2000 Oct 15;351 Pt 2(Pt 2):307-11.
Mitochondrial proton leak in rat muscle is responsible for approx. 15% of the standard metabolic rate, so its modulation could be important in regulating metabolic efficiency. We report in the present paper that physiological concentrations of AMP (K(0.5)=80 microM) increase the resting respiration rate and double the proton conductance of rat skeletal-muscle mitochondria. This effect is specific for AMP. AMP also doubles proton conductance in skeletal-muscle mitochondria from an ectotherm (the frog Rana temporaria), suggesting that AMP activation is not primarily for thermogenesis. AMP activation in rat muscle mitochondria is unchanged when uncoupling protein-3 is doubled by starvation, indicating that this protein is not involved in the AMP effect. AMP activation is, however, abolished by inhibitors and substrates of the adenine nucleotide translocase (ANT), suggesting that this carrier (possibly the ANT1 isoform) mediates AMP activation. AMP activation of ANT could be important for physiological regulation of metabolic rate.
大鼠肌肉中的线粒体质子泄漏约占标准代谢率的15%，因此对其进行调节可能对调控代谢效率具有重要意义。我们在本文中报告，生理浓度的AMP（K(0.5)=80微摩尔）可提高静息呼吸速率，并使大鼠骨骼肌线粒体的质子传导率加倍。这种效应是AMP特有的。AMP还能使变温动物（青蛙林蛙）骨骼肌线粒体的质子传导率加倍，这表明AMP激活并非主要用于产热。当通过饥饿使解偶联蛋白-3加倍时，大鼠肌肉线粒体中的AMP激活作用不变，这表明该蛋白不参与AMP效应。然而，腺嘌呤核苷酸转位酶（ANT）的抑制剂和底物可消除AMP激活作用，这表明该载体（可能是ANT1同工型）介导了AMP激活。ANT的AMP激活作用可能对代谢率的生理调节具有重要意义。
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