1. Exploring the Effects of S-Nitrosylation on Caspase-3 Modification and Myofibril Degradation of Beef In Vitro.
- Author
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Hou Q, Ma C, Liu R, Kang Z, and Zhang W
- Subjects
- Animals, Cattle, S-Nitrosoglutathione chemistry, S-Nitrosoglutathione metabolism, S-Nitrosoglutathione pharmacology, Tandem Mass Spectrometry, Cysteine metabolism, Cysteine chemistry, Proteolysis drug effects, Muscle, Skeletal chemistry, Muscle, Skeletal metabolism, Muscle, Skeletal drug effects, Muscle, Skeletal enzymology, Nitric Oxide metabolism, Troponin T metabolism, Troponin T chemistry, Muscle Proteins metabolism, Muscle Proteins chemistry, Myofibrils chemistry, Myofibrils metabolism, Caspase 3 metabolism, Caspase 3 chemistry, Caspase 3 genetics
- Abstract
This study aimed to explore the effects of S-nitrosylation on caspase-3 modification and its subsequent effects on beef myofibril degradation in vitro. Recombinant caspase-3 was reacted with different concentrations of S-nitrosoglutathione (GSNO, nitric oxide donor) at 37 °C for 30 min and subsequently incubated with purified myofibrillar protein from bovine semimembranosus muscle. Results indicated that the activity of caspase-3 was significantly reduced after GSNO treatments ( P < 0.05) and showed a dose-dependent inhibitory effect, which was attributed to the increased S-nitrosylation extent of caspase-3. LC-MS/MS analysis revealed that caspase-3 was S-nitrosylated at cysteine sites 116, 170, 184, 220, and 264. Moreover, the degradation of desmin and troponin-T was notably suppressed by S-nitrosylated caspase-3 ( P < 0.05). To conclude, protein S-nitrosylation could modify the cysteine residues of caspase-3, which accounts for the reduced caspase-3 activity and further represses its proteolytic ability on beef myofibrillar protein.
- Published
- 2024
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