Flt3 Activation Mitigates Mitochondrial Fragmentation and Heart Dysfunction through Rebalanced L-OPA1 Processing by Hindering the Interaction between Acetylated p53 and PHB2 in Cardiac Remodeling

نویسندگان

چکیده

Recent studies have shown that FMS-like receptor tyrosine kinase 3 (Flt3) has a beneficial effect on cardiac maladaptive remodeling. However, the role and mechanism of Flt3 in mitochondrial dynamic imbalance under stress remains poorly understood. This study aims to investigate how regulates p53-mediated optic atrophy 1 (OPA1) processing fragmentation improve Mitochondrial cardiomyocytes was induced by isoprenaline (ISO) H2O2 challenge, respectively, vitro. Cardiac remodeling mice established ligating left anterior descending coronary artery or chronic ISO vivo. Our results demonstrated protein expression acetylated-p53 (ac-p53) mitochondria significantly increased cell conditions, facilitating dissociation PHB2-OPA1 complex binding prohibitin 2 (PHB2), molecular chaperone stabilizes OPA1 mitochondria. led degradation long isoform (L-OPA1) facilitates fusion resultant network fragmentation. abolished p53 K371R mutant failed bind PHB2 impeded formation ac-p53-PHB2 complex. The activation reduced ac-p53 via SIRT1, thereby hindering potentiating stability ultimately inhibits L-OPA1 leads balancing dynamics. These findings highlight novel which mitigates dysfunction through reduction dampening interaction between

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ژورنال

عنوان ژورنال: Antioxidants

سال: 2023

ISSN: ['2076-3921']

DOI: https://doi.org/10.3390/antiox12091657