Cysteine Metabolism in Neuronal Redox Homeostasis.

Trends Pharmacol Sci

The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA; Department of Psychiatry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address:

Published: May 2018

AI Article Synopsis

  • Cysteine is crucial for protein synthesis and acts as an antioxidant by being part of glutathione (GSH) and working independently.
  • Cysteine undergoes various modifications that influence important physiological processes, particularly in the brain.
  • Imbalances in cysteine metabolism are linked to neurodegenerative diseases, and restoring this balance may provide therapeutic benefits, especially in conditions like Huntington's disease and molybdenum cofactor deficiency.

Article Abstract

Besides its essential role in protein synthesis, cysteine plays vital roles in redox homeostasis, being a component of the major antioxidant glutathione (GSH) and a potent antioxidant by itself. In addition, cysteine undergoes a variety of post-translational modifications that modulate several physiological processes. It is becoming increasingly clear that redox-modulated events play important roles not only in peripheral tissues but also in the brain where cysteine disposition is central to these pathways. Dysregulated cysteine metabolism is associated with several neurodegenerative disorders. Accordingly, restoration of cysteine balance has therapeutic benefits. This review discusses metabolic signaling pathways pertaining to cysteine disposition in the brain under normal and pathological conditions, highlighting recent findings on cysteine metabolism during aging and in neurodegenerative conditions such as Huntington's disease (HD) and molybdenum cofactor (MoCo) deficiency (MoCD) among others.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5912966PMC
http://dx.doi.org/10.1016/j.tips.2018.02.007DOI Listing

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