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首页> 外文期刊>The Journal of Physiology >Differential effect of bicycling exercise intensity on activity and phosphorylation of atypical protein kinase C and extracellular signal-regulated protein kinase in skeletal muscle.
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Differential effect of bicycling exercise intensity on activity and phosphorylation of atypical protein kinase C and extracellular signal-regulated protein kinase in skeletal muscle.

机译：骑自行车运动强度对骨骼肌中非典型蛋白激酶C和细胞外信号调节蛋白激酶活性和磷酸化的差异影响。

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摘要

Atypical protein kinase C (aPKC) and extracellular signal-regulated kinase (ERK) are emerging as important signalling molecules in the regulation of metabolism and gene expression in skeletal muscle. Exercise is known to increase activity of aPKC and ERK in skeletal muscle but the effect of exercise intensity hereon has not been studied. Furthermore, the relationship between activity and phosphorylation of the two enzymes during exercise is unknown. Nine healthy young men exercised for 30 min on a bicycle ergometer on two occasions. One occasion consisted of three consecutive 10 min bouts of 35, 60 and 85% of peak pulmonary oxygen uptake V(O(2 peak)) and the second of one 30 min bout at 35% of V(O(2 peak)). Both trials also included 30 min recovery. Muscle biopsies were obtained from the vastus lateralis muscle before and after each exercise bout. Exercise increased muscle aPKC activity at 35% V(O(2 peak)), whereupon no further increase was observed at higher exercise intensities. Activation of aPKC was not accompanied by increased phosphorylation of aPKC Thr(410/403). ERK1/2 activity increased in a similar pattern to aPKC, reaching maximal activity at 35% V(O(2 peak)), whereas ERK1 Thr(202)/Tyr(204) and ERK2 Thr(183)/Tyr(185) phosphorylation increased with increasing exercise intensity. Thus, aPKC and ERK1/2 activity in muscle during exercise did not correspond to phosphorylation of sites on aPKC or ERK1/2, respectively, which are considered important for their activation. It is concluded that assessment of aPKC and ERK1/2 activity in muscle using phosphospecific antibodies did not reflect direct activity measurements on immunoprecipitated enzyme in vitro. Thus, estimation of enzyme activity during exercise by use of phosphospecific antibodies should not be performed uncritically. In addition, increase in muscle activity of aPKC or ERK1/2 during exercise is not closely related to energy demands of the muscle but may serve other regulatory or permissive functions in muscle.
机译：非典型蛋白激酶C（aPKC）和细胞外信号调节激酶（ERK）在骨骼肌代谢和基因表达的调节中正作为重要的信号分子出现。已知运动可增加骨骼肌中aPKC和ERK的活性，但尚未研究运动强度对其的影响。此外，运动期间两种酶的活性与磷酸化之间的关系是未知的。九名健康的年轻人两次在自行车测功机上锻炼了30分钟。一种情况包括连续三个10分钟的发作，分别为35、60和85％的峰值肺氧摄取V（O（2峰值）），第二次是30分钟的发作，以35％的V（O（2峰值））。两项试验还包括30分钟的恢复时间。每次运动前后从外侧股外侧肌获得肌肉活检。运动在35％V（O（2峰值））下增加了肌肉aPKC活性，因此在较高的运动强度下未观察到进一步的增加。 aPKC的激活并不伴随着aPKC Thr（410/403）磷酸化的增加。 ERK1 / 2活性以与aPKC相似的方式增加，在35％V（O（2峰值））处达到最大活性，而ERK1 Thr（202）/ Tyr（204）和ERK2 Thr（183）/ Tyr（185）磷酸化随着运动强度的增加而增加。因此，运动期间肌肉中的aPKC和ERK1 / 2活性分别不对应于aPKC或ERK1 / 2上的位点的磷酸化，这被认为对其激活很重要。结论是，使用磷酸特异性抗体评估肌肉中aPKC和ERK1 / 2的活性不能反映体外免疫沉淀酶的直接活性测量结果。因此，不应通过使用磷酸特异性抗体来估计运动过程中的酶活性。此外，运动过程中aPKC或ERK1 / 2的肌肉活动增加与肌肉的能量需求并不紧密相关，但可能在肌肉中起到其他调节或允许功能。

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