Fig 1: Sevoflurane increases the levels of CypD, but not ANT or VDAC, in hippocampus tissues of WT young mice. (A) Western blot shows that sevoflurane anesthesia (lanes 4–6) increases the levels of CypD, but not ANT or VDAC, other two components of mPTP, as compared to the control condition (lanes 1–3) in the hippocampus tissues of WT mice. There is no significant difference in the amounts of ß-actin in the hippocampus tissues between the mice in the control condition group and the mice in the sevoflurane anesthesia group. (B) Quantification of the Western blot shows that the sevoflurane anesthesia (black bar) increases CypD levels as compared to the control condition (white bar). (**P = 0.024, Student’s t test with post hoc Bonferroni adjustment, N = 6). (C) Sevoflurane anesthesia (row b) increases the levels of CypD compared to the control condition (row a) in the hippocampus tissues of WT mice. Column 1 is the CypD (red) staining, and column 2 is CypD merged with the DAPI (blue) nuclear staining. (D) Quantification of the image shows that sevoflurane anesthesia (black bar) increases CypD levels as compared to the control condition (white bar). (**P = 0.010, Student’s t test, N = 6).
Fig 2: Hypothesized pathway of CypD associated sevoflurane-induced cognitive impairment in young mice. Sevoflurane increases levels of CypD via reducing the binding of CypD with ANT. The increased CypD then causes mitochondrial dysfunctions and impairment of neurogenesis, eventually leading to cognitive impairment in young mice.
Fig 3: Muscle-specific changes in essential regulators of bioenergetics in D2.mdx mice. Protein content of adenine nucleotide translocase 1 (ANT 1) on the inner mitochondrial membrane (A), voltage-dependent anion carrier 2 (VDAC 2) on the outer mitochondrial membrane (B), mitochondrial creatine kinase (mtCK) found in the inner membrane space (C), and citrate synthase that catalyses the first reaction in the citric acid cycle (D). Protein content of electron transport chain components was also quantified in diaphragm (E), Quad (F), and WG (G). Results represent mean ± SEM; n = 8–12; * P < 0.05 compared with wild type (WT).
Fig 4: Effect of suppressing NFkB activation in response to cellular fuel overloading on mitochondrial morphology, mitochondrial proteins and gene expression. L6 myotubes were incubated with GLC (5 mM), PA (0.4 mM), 2DG (5 mM) and BI605906 (10 µM) for 16 h in the combinations indicated in the various experimental data panels prior to a analysis and quantification of mitochondrial morphology using Mitotracker green (Mitospy) by confocal microscopy (the scale bar represents 5 µm), b mitochondrial DNA copy number by qPCR, c citrate synthase (CS) activity and (d, e), analysis of mitochondria protein and mRNA abundance (UCP3, ANT1, PGC1a, SDHA, and COX4.1) which was normalised to GAPDH. All graphical bar data are presented as mean ± SEM from four separate experiments. Asterisks indicate a significant change (P < 0.05) to the GLC alone condition
Fig 5: Schematic representation of energy transfer between mitochondria and cytosol. The leading model for energy exchange involves a creatine-independent (-Cr) and creatine-dependent (+Cr) pathway. The left side depicts the -Cr pathway whereby ADP/ATP transfer occurs solely through diffusion across voltage-dependent anion carrier (VDAC) on the outer mitochondrial membrane and adenosine nucleotide translocase (ANT) on the inner mitochondrial membrane. The right side depicts the +Cr pathway where, in the presence of Cr, energy transfer is facilitated by mitochondrial creatine kinase (mtCK) through the transfer of the phosphate group from ATP to Cr, producing phosphocreatine (PCr) and ADP in the inner membrane space. The PCr is exported via VDAC into the cytosol while the ADP is directly recycled back via ANT into the mitochondrial matrix. Figure adapted from Aliev et al., 2011, Guzun et al., 2012, Myer et al., 1984, and Wallimann et al., 2011.19, 20, 21, 22
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