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AMP decreases the efficiency of skeletal-muscle mitochondria

被引：48
作者：
Cadenas, S
Buckingham, JA
St-Pierre, J
Dickinson, K
Jones, RB
Brand, MD
机构：
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England
[2] MRC, Dunn Human Nutr Unit, Cambridge CB2 2XY, England
[3] BASF Pharma, Nottingham NG1 1GF, England
[4] Univ Cambridge, Dept Zool, Cambridge CB2 3EJ, England
来源：
BIOCHEMICAL JOURNAL | 2000年 / 351卷
关键词：
adenine nucleotide translocase; nucleotides; proton leak; uncoupling; uncoupling proteins;
D O I：
10.1042/0264-6021:3510307
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 muM) 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.
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页码：307 / 311
页数：5
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