Effect of Phosphorylation on the Degradation of Myofibrillar Proteins by μ-Calpain

doi:10.7506/spkx1002-6630-201715001

Abstract

Abstract: Objective: The objective of this study was to investigate the effect of phosphorylation on the degradation of myofibrillar proteins by μ-calpain. Methods: Protein kinase A (PKA) and alkaline phosphatase (AP) were used to catalyze the phosphorylation and dephosphorylation of myofibrillar proteins of mutton longissimus dorsi muscle, followed by hydrolysis by μ-calpain. The levels of protein phosphorylation and degradation were measured by SDS-PAGE, Pro-Q Diamond fluorescent staining, and Western blotting, respectively. Results: The phosphorylation level of myofibrillar proteins in the PKA group was significantly higher than that of the control group (P < 0.05), while the phosphorylation level of myofibrillar proteins in the AP group was significantly lower than that of the control group (P < 0.05). The autolysis and activity of μ-calpain were suppressed by PKA treatment, thereby leading to prolonged hydrolysis of myofibrillar proteins by μ-calpain. Phosphorylation enhanced the degradation of myosin heavy chain and troponin T, while dephosphorylation enhanced the degradation of actin and desmin. Conclusion: Phosphorylation affected both myofibrillar proteins and μ-calpain activity and therefore the degradation of myofibrillar proteins by μ-calpain.

Key words: phosphorylation, myofibrillar proteins, μ-calpain, degradation, protein kinase A, alkaline phosphatase

CLC Number:

TS251.1

LI Zheng, LI Xin, DU Manting, LI Meng, ZHANG Dequan. Effect of Phosphorylation on the Degradation of Myofibrillar Proteins by μ-Calpain[J]. FOOD SCIENCE, 2017, 38(15): 1-6.

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Effect of Phosphorylation on the Degradation of Myofibrillar Proteins by μ-Calpain

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