ArticleFood science of animal resources2026
Effect of the combined action of myofibrillar protein phosphorylation and S-nitrosylation on the degradation of myofibrillar proteins by µ-calpain.
Article in Food science of animal resources, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Abstract
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.
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