Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca2+ concentrations in vitro
Phosphorylation inhibits the activity of μ-calpain at different incubation temperatures and Ca2+ concentrations in vitro
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DOI：
10.1016/j.foodchem.2017.02.003
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发表时间：
2017-08-01
期刊：
影响因子：
8.8
通讯作者：
Zhang, Dequan
中科院分区：
文献类型：
--
作者：
Du, Manting;Li, Xin;Zhang, Dequan
本研究旨在探讨磷酸化对mu-calpain活性及其对温度和Ca 2+敏感性的影响。对于温度敏感性分析，肌浆蛋白在4、25和37 ℃下用碱性磷酸酶（AP）和磷酸酶抑制剂（PI）处理。结果表明，AP组在孵育12 h后μ-calpain降解程度明显高于对照组。对于钙敏感性分析，将用AP和PI处理的样品在0.01、0.05、0.1和1 mM Ca 2+下孵育。结果表明，在0.01、0.05和0.1mM Ca ~（2+）时，AP组μ-calpain降解速率最大，PI组最小。随着浓度的增加，三组之间的差异减小。这些数据表明，磷酸化在调节μ-钙蛋白酶活性中起负面作用。本研究阐明了在体外和/或在死后肌肉中mu-钙蛋白酶激活的调节机制。(C)2017爱思唯尔有限公司版权所有
This study aimed to investigate the effects of phosphorylation on the activity of mu-calpain and its sensitivity to temperature and Ca2+. For temperature sensitivity analysis, sarcoplasmic protein was treated with alkaline phosphatase (AP) and phosphatase inhibitor (PI) at 4, 25 and 37 degrees C. The results showed that the degradation degree of mu-calpain in the AP group was significantly higher after incubation for 12 h. For calcium sensitivity analysis, samples treated with AP and PI were incubated at 0.01, 0.05, 0.1 and 1 mM Ca2+. The results showed that the degradation rate of mu-calpain was maximum in the AP group and minimum in the PI group at 0.01, 0.05 and 0.1 mM Ca2+. The differences between the three groups reduced as concentration increased. These data demonstrate that phosphorylation plays a negative role in regulating mu-calpain activity. This study clarifies the regulatory mechanism of mu-calpain activation in vitro and/or in postmortem muscle. (C) 2017 Elsevier Ltd. All rights reserved.