Calpastatin inhibits the activity of phosphorylated mu-calpain in vitro

文献类型： 外文期刊

第一作者： Du, Manting

作者： Du, Manting;Li, Xin;Li, Zheng;Ren, Chi;Zhang, Dequan;Du, Manting;Shen, Qingwu

作者机构：

关键词： Calpastatin; mu-Calpain; Phosphorylation; Protein kinase A; Alkaline phosphatase

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN： 0308-8146

年卷期： 2019 年 274 卷

页码：

收录情况： SCI

摘要： The objective of this study was to investigate the effect of phosphorylation on the sensitivity of mu-calpain to the inhibition induced by calpastatin. Purified mu-calpain was incubated with alkaline phosphatase (AP) or protein kinase A (PKA) to modulate the phosphorylation level of mu-calpain. Accurately 25, 50, 100 and 150 units of AP/PKA-treated mu-calpain were mixed with the same amounts of heat stable proteins and incubated at 4 degrees C. In the calpastatin-free system, AP and PKA-treated mu-calpain had higher proteolytic activity compared to the control. Intact AP-treated mu-calpain degraded fastest in the 50, 100 and 150 unit mu-calpain incubation systems. However, the degradation rate of mu-calpain in control and PKA group was non-significant in 100 and 150 unit mu-calpain systems. Our results demonstrated that, compared to dephosphorylated and control mu-calpain, calpastatin presents greater inhibition to PKA phosphorylated mu-calpain. This study increases understanding of the mechanism of mu-calpain activity regulated by phosphorylation.

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