内分泌学
内科学
磷酸化
胰岛素
丝氨酸
葡萄糖摄取
化学
医学
生物化学
作者
Haiyan Wang,Seong Eun Kwak,Amy Zheng,Edward B. Arias,Xiufang Pan,Dongsheng Duan,Gregory D. Cartee
出处
期刊:American Journal of Physiology-endocrinology and Metabolism
[American Physiological Society]
日期:2024-04-24
卷期号:326 (6): E807-E818
被引量:1
标识
DOI:10.1152/ajpendo.00010.2024
摘要
The current study evaluated the role of Akt substrate of 160 kDa (AS160) phosphorylation on Ser704 in increased insulin-stimulated glucose uptake by skeletal muscle after exercise. Adeno-associated virus vectors were engineered to express either wild-type-AS160 or AS160 mutated so that it could not be phosphorylated on Ser704 in paired muscles from AS160-knockout rats. The results demonstrated that AS160 phosphorylation on Ser704 was not essential for exercise-induced elevation in insulin-stimulated glucose uptake by rats of either sex.
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