Phosphorylation of Calpastatin Negatively Regulates the Activity of Calpain

文献类型： 外文期刊

第一作者： Bai, Yuqiang

作者： Bai, Yuqiang;Hou, Chengli;Huang, Caiyan;Fang, Fei;Dong, Yu;Li, Xin;Zhang, Dequan

作者机构：

关键词： tenderization; structural stability; serine

期刊名称：LIFE-BASEL （ 影响因子：3.2； 五年影响因子：3.2 ）

ISSN：

年卷期： 2023 年 13 卷 3 期

页码：

收录情况： SCI

摘要： Tenderness is an important characteristic of meat quality. Calpastatin and calpain play important roles in meat tenderization. However, it is not clear how phosphorylation affects the regulation of calpastatin on mu-calpain and, consequently, meat tenderness. Calpastatin with high and low phosphorylation levels were obtained in vitro corresponding to the treatments by protein kinase A (PKA) and alkaline phosphatase. Then, calpain was incubated with calpastatin with different phosphorylation levels, and the effect of calpastatin on calpain activity under different phosphorylation levels was analyzed. The results showed that PKA promoted the phosphorylation of calpastatin, and a high phosphorylation level was maintained during incubation. The degradation rate of mu-calpain in AP group was higher than that in the other groups, meaning there was lower inhibition of calpastatin on calpain activity. The degradation of calpastatin was lower and its structure was more stable after phosphorylation. One more serine 133 site of calpastatin was identified in PKA group compared with the other groups. Phosphorylation at serine 133 of calpastatin enhanced its inhibition on calpain activity by maintaining its structural stability, thus inhibiting the tenderization of meat.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序