Role of Mitochondrial Respiratory Chain in Neurotoxic Action of Heavy Metals: Comparison of Cd2+, Hg2+ and Cu2+| Chapter 11 | Cutting Edge Research in Biology Vol. 2

 The aim of the work was to elucidate the duty of mitochondrial electron transport chain (mtETC) in neurotoxicity of severe metals, such as Cd2+, Hg2+ and Cu2+. In particular, the effects of these bivalent harmonized ions on cell being, intracellular reactive oxygen species era, respiration and mitochondrial sheet potential of rat neuron-like PC12 cell line were intentional in the absence and in the demeanor of various antioxidants and mitochondrial function modulators. As revealed, the metals substitute caused, even though in a different way, dose- and opportunity-dependent changes of all earlier parameters. Noteworthy, beginning from 10 µM and once at short incubation period (3 h), Cd2+ significantly inhibited rates of maximally uncoupled container respiration. In addition, nearly complete suppression of cellular breathing was achieved following in position or time 3 h of incubation with 50 µM Hg2+ or 500 µM Cd2+, inasmuch as even after 48 h of exposure to 500 µM Cu2+, only 50% abolition of respiration accepted place. It has been established that not only differing antioxidants (N-acetylcysteine, butylhydroxytoluene, mannitol, vitamin E, tetramethylpiperidine-1-oxyl) and inhibitors of mitochondrial permeability change (MPT) pores (cyclosporin A, bongkrekic acid, ruthenium red), but also specific mtETC modulators as FCCP (a widely used pretended uncoupler) and stigmatellin (a complex III inhibitor), partially look after from cell damage presented by Cd2+. However, all used mtETC modulators did not look after against Hg2+- or Cu2+-induced container injury. Importantly, stigmatellin was shown expected one of the most powerful protectors against Cd2+-induced container damage, producing a 15-20% increase in container viability. Molecular mechanisms of the difficulty of mtETC in heavy metal-inferred mitochondrial membrane permeabilization and cell cessation are discussed. As a result, the friendship between mtETC and MPT pore has become more transparent.

Author(s) Details:

Elena A. Belyaeva,
Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, Thorez pr. 44, 194223, St.-Petersburg, Russia.

Please see the link here: https://stm.bookpi.org/CERB-V2/article/view/8893