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Editorial
. 2011 Sep 16;109(7):716-9.
doi: 10.1161/CIRCRESAHA.111.253864.

Cardiac Resynchronization Therapy and Reverse Molecular Remodeling: Importance of Mitochondrial Redox Signaling

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Editorial

Cardiac Resynchronization Therapy and Reverse Molecular Remodeling: Importance of Mitochondrial Redox Signaling

Jay L Zweier et al. Circ Res. .
Free PMC article

Figures

Figure 1
Figure 1. Oxidative modification of protein thiols
Under oxidative stress, protein thiols are subject to either reversible or irreversible oxidative modification. Reversible modifications, S-nitrosation, S-glutathionylation, disulfide bond, and cysteine sulphenic acid formation, play important roles in cellular redox regulation. When cellular reducing status returns to normal, these are reversed. For irreversible modification, protein thiols are oxidized to sulphinic and sulphonic acid leading to loss of protein function and protein degradation which can trigger cellular apoptosis or necrosis.
Figure 2
Figure 2. Oxidative posttranslational modification of ATP synthase in DHF and effect of CRT
In DHF, Cys244 and Cys294 of the α-subunit are S-glutathionylated (2), or inter-disulfide bonding occurs between Cys294 of α-subunits as well as between Cys294 and Cys103 of the γ–subunit (3). S-glutathionylation and inter-disulfide formation of ATP synthase inhibits its ATP synthesis leading to mitochondrial energy starvation and dysfunction. CRT increases S-nitrosation of ATP synthase at Cys103 of γ-subunit and Cys294 of α-subunit (4), along with ATPase activity.

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