Effect of starvation and insulin-induced hypoglycemia on oxidative stress scavenger system and electron transport chain complexes from rat brain, liver, and kidney

1998 ◽  
Vol 34 (2-3) ◽  
pp. 157-168 ◽  
Author(s):  
Sanjeev Kumar Bhardwaj ◽  
Madan Lal Sharma ◽  
Govind Gulati ◽  
Arvind Chhabra ◽  
Reena Kaushik ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Electron Transport ◽  
Rat Brain ◽  
Electron Transport Chain ◽  
Chain Complexes ◽  
Transport Chain ◽  
Liver And Kidney

scholarly journals Transcriptomic and Functional Analyses of Mitochondrial Dysfunction in Pressure Overload‐Induced Right Ventricular Failure

2021 ◽  
Vol 10 (4) ◽  
Author(s):  
HyunTae V. Hwang ◽  
Nefthi Sandeep ◽  
Ramesh V. Nair ◽  
Dong‐Qing Hu ◽  
Mingming Zhao ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Electron Transport ◽  
Mitochondrial Dysfunction ◽  
Electron Transport Chain ◽  
Mitochondrial Fission ◽  
Pressure Overload ◽  
Energy Generation ◽  
Complex Congenital Heart Disease ◽  
Chain Complexes ◽  
Transport Chain

Background In complex congenital heart disease patients such as those with tetralogy of Fallot, the right ventricle (RV) is subject to pressure overload, leading to RV hypertrophy and eventually RV failure. The mechanisms that promote the transition from stable RV hypertrophy to RV failure are unknown. We evaluated the role of mitochondrial bioenergetics in the development of RV failure. Methods and Results We created a murine model of RV pressure overload by pulmonary artery banding and compared with sham‐operated controls. Gene expression by RNA‐sequencing, oxidative stress, mitochondrial respiration, dynamics, and structure were assessed in pressure overload‐induced RV failure. RV failure was characterized by decreased expression of electron transport chain genes and mitochondrial antioxidant genes (aldehyde dehydrogenase 2 and superoxide dismutase 2) and increased expression of oxidant stress markers (heme oxygenase, 4‐hydroxynonenal). The activities of all electron transport chain complexes decreased with RV hypertrophy and further with RV failure (oxidative phosphorylation: sham 552.3±43.07 versus RV hypertrophy 334.3±30.65 versus RV failure 165.4±36.72 pmol/(s×mL), P <0.0001). Mitochondrial fission protein DRP1 (dynamin 1‐like) trended toward an increase, while MFF (mitochondrial fission factor) decreased and fusion protein OPA1 (mitochondrial dynamin like GTPase) decreased. In contrast, transcription of electron transport chain genes increased in the left ventricle of RV failure. Conclusions Pressure overload‐induced RV failure is characterized by decreased transcription and activity of electron transport chain complexes and increased oxidative stress which are associated with decreased energy generation. An improved understanding of the complex processes of energy generation could aid in developing novel therapies to mitigate mitochondrial dysfunction and delay the onset of RV failure.

scholarly journals Dopamine and Methamphetamine Differentially Affect Electron Transport Chain Complexes and Parkin in Rat Striatum: New Insight into Methamphetamine Neurotoxicity

2021 ◽  
Vol 23 (1) ◽  
pp. 363
Author(s):  
Viktoriia Bazylianska ◽  
Akhil Sharma ◽  
Heli Chauhan ◽  
Bernard Schneider ◽  
Anna Moszczynska
Keyword(s):  
Oxidative Stress ◽  
Electron Transport ◽  
Mitochondrial Dysfunction ◽  
Complex I ◽  
Electron Transport Chain ◽  
Rat Striatum ◽  
Experimental Conditions ◽  
Chain Complexes ◽  
Transport Chain

Methamphetamine (METH) is a highly abused psychostimulant that is neurotoxic to dopaminergic (DAergic) nerve terminals in the striatum and increases the risk of developing Parkinson’s disease (PD). In vivo, METH-mediated DA release, followed by DA-mediated oxidative stress and mitochondrial dysfunction in pre- and postsynaptic neurons, mediates METH neurotoxicity. METH-triggered oxidative stress damages parkin, a neuroprotective protein involved in PD etiology via its involvement in the maintenance of mitochondria. It is not known whether METH itself contributes to mitochondrial dysfunction and whether parkin regulates complex I, an enzymatic complex downregulated in PD. To determine this, we separately assessed the effects of METH or DA alone on electron transport chain (ETC) complexes and the protein parkin in isolated striatal mitochondria. We show that METH decreases the levels of selected complex I, II, and III subunits (NDUFS3, SDHA, and UQCRC2, respectively), whereas DA decreases the levels only of the NDUFS3 subunit in our preparations. We also show that the selected subunits are not decreased in synaptosomal mitochondria under similar experimental conditions. Finally, we found that parkin overexpression does not influence the levels of the NDUFS3 subunit in rat striatum. The presented results indicate that METH itself is a factor promoting dysfunction of striatal mitochondria; therefore, it is a potential drug target against METH neurotoxicity. The observed decreases in ETC complex subunits suggest that DA and METH decrease activities of the ETC complexes via oxidative damage to their subunits and that synaptosomal mitochondria may be somewhat “resistant” to DA- and METH-induced disruption in mitochondrial ETC complexes than perikaryal mitochondria. The results also suggest that parkin does not regulate NDUFS3 turnover in rat striatum.

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