The effect of autophagy activation on apoptosis and myofibrillar structural proteins during the post-mortem storage of Esox lucius
文献类型： 外文期刊
作者： Fan, Xuemei 1 ; Liu, Yibo 1 ; Guo, Xin 1 ; Wei, Yabo 1 ; Liu, Pingping 1 ; Li, Hui 1 ; Chen, Xin 1 ; Deng, Xiaorong 1 ; Lei, Yongdong 2 ; Zhang, Jian 1 ;
作者机构： 1.Shihezi Univ, Sch Food Sci & Technol, Shihezi 832000, Xinjiang, Peoples R China
2.Shihezi Univ, Sch Food Sci & Technol, Key Lab Characterist Agr Prod Proc & Qual Control, Minist Agr & Rural Affairs, Shihezi 832000, Xinjiang, Peoples R China
3.Shihezi Univ, Sch Food Sci & Technol, Key Lab Food Nutr & Safety Control, Xinjiang Prod & Construct Corps, Shihezi 832003, Xinjiang, Peoples R China
4.Xinjiang Acad Agr & Reclamat Sci, Food Qual Supervis & Testing Ctr, Minist Agr, Shihezi 832003, Xinjiang, Peoples R China
关键词： Autophagy; Mitochondrial apoptosis; Myofibrillar structural proteins; 3-MA; Esox Lucius
期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）
ISSN： 0308-8146
年卷期： 2025 年 491 卷
页码：
收录情况： SCI
摘要： This study surveyed the regulatory role of autophagy in mitochondrial apoptosis and myofibrillar structural proteins degradation in postmortem fish muscle. Using 3-methyladenine (3-MA), a model of autophagy inhibition was established. Results showed that 3-MA significantly suppressed autophagy by downregulating Beclin-1 expression (by 24.19 % at 120 h) and the LC3-II/LC3-I ratio, upregulating p62 expression, and inhibiting autophagosome formation. This inhibition stabilized mitochondrial membrane potential (Delta Psi m) and attenuated apoptotic signaling by reducing the Bax/Bcl-2 ratio, cytochrome c release(by 37.83 % at 120 h), and caspase-3/9 activity. Consequently, it slowed the degradation of troponin-T in the early stage and titin, actin, and desmin (reduced by 16.37 % at 120 h) in the later stage, preserving myofibril integrity, reducing myofibril fragmentation index (MFI) and increasing shear force, and improving muscle texture. These results demonstrated that autophagy contributes to the degradation of myofibrillar structural proteins by facilitating mitochondrial apoptosis
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