Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects

Iglesias, Darío E.; Bombicino, Silvina Sonia; Valdez, Laura B.; Boveris, Alberto

doi:10.1016/j.freeradbiomed.2015.08.024

Cited by 39 publications

(32 citation statements)

References 56 publications

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“…Similarly, complex IV activity, which is reversibly inhibited by NO, was also unaffected in GSNOR -/-TA muscles. Also, GSNO can inhibit complex III activity in cardiac sub-mitochondrial particles, whereas GSNOR depletion did not impact complex III activity in skeletal muscle, supporting differences in GSNOR function between heart and skeletal muscles (37,40). Taken together, these data argue against increased mitochondrial respiratory chain activity as a mechanism to explain increased strength and fatigue resistance of GSNOR -/-TA muscles.…”

Section: Discussionmentioning

confidence: 68%

GSNOR Deficiency EnhancesIn SituSkeletal Muscle Strength, Fatigue Resistance, and RyR1 S-Nitrosylation Without Impacting Mitochondrial Content and Activity

Moon

Cao

Zhu

et al. 2017

Antioxidants & Redox Signaling

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Section: Discussionmentioning

confidence: 68%

GSNOR Deficiency EnhancesIn SituSkeletal Muscle Strength, Fatigue Resistance, and RyR1 S-Nitrosylation Without Impacting Mitochondrial Content and Activity

Moon

Cao

Zhu

et al. 2017

Antioxidants & Redox Signaling

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“…Taken together, the findings in this study indicate that ARG2 is protective for the mitochondrial function, particularly in the intracellular environment of high-level NO synthesis. Prior studies have shown that NO has inhibitory effects on the respiratory chain (complex I and III) and consequently decreases oxygen consumption and cellular respiration (54). Inhibition of the respiratory chain by NO results in an increase in the rate of aerobic glycolysis (Warburg effect), and an increase in the conversion of pyruvate to lactate.…”

Section: Discussionmentioning

confidence: 99%

Increased mitochondrial arginine metabolism supports bioenergetics in asthma

Xu¹,

Ghosh²,

Comhair³

et al. 2016

Journal of Clinical Investigation

104

119

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“…At higher concentrations of GSNO, effects extend to the rate of relaxation and cross‐bridge turnover and should be relevant for pathophysiological effects. GSNO (500 μM) interacts with mitochondrial complex III bovine heart mitochondria (antimycin‐like effect) [Iglesias et al, ] and cause human ECs apoptosis [Liu et al, ]. These evidences reveal that GSNO possesses the dual effects on cardio and vascular cells in the different concentrations.…”

mentioning

confidence: 99%

Enhanced Aerobic Glycolysis by S-Nitrosoglutathione via HIF-1α Associated GLUT1/Aldolase A Axis in Human Endothelial Cells

et al. 2017

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S-nitrosoglutathione (GSNO)-induced apoptosis is associated with reactive oxygen species and loss of mitochondrial Omi/HtrA2 in human endothelial cells (ECs). But its upstream regulation is still not elucidated. Here, we demonstrate that hypoxia induced factor-1α (HIF-1α)-linked aerobic glycolysis is associated with mitochondrial abnormality by treatment of human EC-derived EA.hy926 cells with GSNO (500 µM) for 6 h. GSNO exposure increased the levels of Aldolase A and glucose transporter-1 (GLUT1) mRNAs and proteins. And selectively enhanced aldolase A activity to form glyceraldehyde 3-phosphate, dihydroxyacetone phosphate, which subsequently increased intracellular levels of methylglyoxal and reactive oxygen species in parallel. Using the biotin switch assay, we found that GSNO increased the S-nitrosylating levels of total protein and HIF-1α. Knockdown of HIF-1α with siRNA attenuated its target aldolase A and GLUT1 expression but not VEGF. In contrast, nitrosylation scanvenger dithiothreitol could decrease all the protein levels. It suggested that aerobic glycolytic flux was more dependent on HIF-1α level, and that HIF-1α S-nitrosylation was crucial for its target expression under the normoxic condition. Moreover, GSNO-induced PI3 K (phosphoinositide 3-kinase)/Akt phosphorylation might contribute to HIF-1α stabilization and nucleus translocation, thereby aiding aldolase A and GLUT1 mRNAs upregulation. Taken together, higher concentration GSNO promotes glycolytic flux enhancement and methylglyoxal formation via HIF-1α S-nitrosylation. These findings reveal the mechanism of enhanced glycolysis-associated mitochondrial dysfunction in ECs by GSNO exposure under normoxic and non-hyperglycemic condition. And offer the early potential targets for vascular pathophysiological evaluation. J. Cell. Biochem. 118: 2443-2453, 2017. © 2017 Wiley Periodicals, Inc.

show abstract

Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects

Cited by 39 publications

References 56 publications

GSNOR Deficiency EnhancesIn SituSkeletal Muscle Strength, Fatigue Resistance, and RyR1 S-Nitrosylation Without Impacting Mitochondrial Content and Activity

GSNOR Deficiency EnhancesIn SituSkeletal Muscle Strength, Fatigue Resistance, and RyR1 S-Nitrosylation Without Impacting Mitochondrial Content and Activity

Increased mitochondrial arginine metabolism supports bioenergetics in asthma

Enhanced Aerobic Glycolysis by S-Nitrosoglutathione via HIF-1α Associated GLUT1/Aldolase A Axis in Human Endothelial Cells

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