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<p>This study investigated the responsiveness of interactively phosphorylated and S-nitrosylated myofibrillar proteins (MPs) to µ-calpain for elucidating the interactive effect of phosphorylation and S-nitrosylation on MPs degradation. MP were treated with protein kinase A (PKA), S-nitrosoglutathione (SNG) and PKA + SNG, respectively, to regulate its modification levels, and then incubated with µ-calpain for 40&#xa0;min. The results showed that phosphorylation level of MPs significantly raised in PKA and PKA + SNG group (<i>p</i> &lt; 0.05), but presented insignificantly differences between these two groups (<i>p</i> ≥ 0.05). S-nitrosylation level of MPs was significantly higher in PKA + SNG group than that in other groups (<i>p</i> &lt; 0.05). MPs co-modified by phosphorylation and S-nitrosylation significantly promoted the degradation of actin (<i>p</i> &lt; 0.05), but inhibited the degradation of desmin. Besides, both co-modification or single modification of MPs showed little influence on the degradation of myosin heavy chain by µ-calpain. The crosstalk of phosphorylation and S-nitrosylation of MPs plays different roles in regulating the degradation of different types of MPs via µ-calpain.</p>

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Effect of the combined action of myofibrillar protein phosphorylation and S-nitrosylation on the degradation of myofibrillar proteins by µ-calpain

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年2月11日

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  • Manting Du,
  • Fangge Hao,
  • Mengli Gao,
  • Ke Li,
  • Junguang Li,
  • Lichuang Cao,
  • Yanhong Bai

摘要

This study investigated the responsiveness of interactively phosphorylated and S-nitrosylated myofibrillar proteins (MPs) to µ-calpain for elucidating the interactive effect of phosphorylation and S-nitrosylation on MPs degradation. MP were treated with protein kinase A (PKA), S-nitrosoglutathione (SNG) and PKA + SNG, respectively, to regulate its modification levels, and then incubated with µ-calpain for 40 min. The results showed that phosphorylation level of MPs significantly raised in PKA and PKA + SNG group (p < 0.05), but presented insignificantly differences between these two groups (p ≥ 0.05). S-nitrosylation level of MPs was significantly higher in PKA + SNG group than that in other groups (p < 0.05). MPs co-modified by phosphorylation and S-nitrosylation significantly promoted the degradation of actin (p < 0.05), but inhibited the degradation of desmin. Besides, both co-modification or single modification of MPs showed little influence on the degradation of myosin heavy chain by µ-calpain. The crosstalk of phosphorylation and S-nitrosylation of MPs plays different roles in regulating the degradation of different types of MPs via µ-calpain.