安普克
AMP脱氨酶
腺苷
蛋白激酶A
化学
核苷酸酶
AMP活化蛋白激酶
骨骼肌
一磷酸腺苷
生物
生物化学
内分泌学
激酶
细胞生物学
腺苷脱氨酶
作者
Samanta Kviklyte,Didier Vertommen,Xavier Yerna,Harriet Andersén,Xiufeng Xu,Philippe Gailly,Mohammad Bohlooly‐Y,Jan Oscarsson,Mark H. Rider
出处
期刊:American Journal of Physiology-endocrinology and Metabolism
[American Physiological Society]
日期:2017-07-01
卷期号:313 (1): E48-E62
被引量:22
标识
DOI:10.1152/ajpendo.00304.2016
摘要
AMP-activated protein kinase (AMPK) plays a key role in energy homeostasis and is activated in response to contraction-induced ATP depletion in skeletal muscle via a rise in intracellular AMP/ADP concentrations. AMP can be deaminated by AMP-deaminase (AMPD) to IMP, which is hydrolyzed to inosine by cytosolic 5′-nucleotidase II (NT5C2). AMP can also be hydrolyzed to adenosine by cytosolic 5′-nucleotidase 1A (NT5C1A). Previous gene silencing and overexpression studies indicated control of AMPK activation by NT5C enzymes. In the present study using gene knockout mouse models, we investigated the effects of NT5C1A and NT5C2 deletion on intracellular adenine nucleotide levels and AMPK activation in electrically stimulated skeletal muscles. Surprisingly, NT5C enzyme knockout did not lead to enhanced AMP or ADP concentrations in response to contraction, with no potentiation of increases in AMPK activity in extensor digitorum longus (EDL) and soleus mouse muscles. Moreover, dual blockade of AMP metabolism in EDL using an AMPD inhibitor combined with NT5C1A deletion did not enhance rises in AMP and ADP or increased AMPK activation by electrical stimulation. The results on muscles from the NT5C knockout mice contradict previous findings where AMP levels and AMPK activity were shown to be modulated by NT5C enzymes.
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