Redox Regulation of Protein Function via Cysteine S-Nitrosylation and Its Relevance to Neurodegenerative Diseases
Joint Authors
Akhtar, Mohd Waseem
Lipton, Stuart A.
Nakamura, Tomohiro
Sunico, Carmen R.
Source
International Journal of Cell Biology
Issue
Vol. 2012, Issue 2012 (31 Dec. 2012), pp.1-9, 9 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2012-08-16
Country of Publication
Egypt
No. of Pages
9
Main Subjects
Abstract EN
Debilitating neurodegenerative diseases, such as Alzheimer's disease (AD) and Parkinson's disease (PD), can be attributed to neuronal cell damage in specific brain regions.
An important hallmark of these diseases is increased oxidative and nitrosative stress that occurs via overproduction of highly reactive free radicals known as reactive oxygen species (ROS) and reactive nitrogen species (RNS).
These molecules are normally removed by cellular antioxidant systems.
Under physiological conditions, ROS/RNS are present at low levels, mediating several neurotrophic and neuroprotective signaling pathways.
In contrast, under pathological conditions, there is a pronounced increase in ROS/RNS generation, impairing normal neurological function.
Nitric oxide (NO) is one such molecule that functions as a signaling agent under physiological conditions but causes nitrosative stress under pathological conditions due to its enhanced production.
As first reported by our group and colleagues, the toxic effects of NO can be in part attributed to thiol S-nitrosylation, a posttranslational modification of cysteine residues on specific proteins.
Here, we review several reports appearing over the past decade showing that S-nitrosylation of an increasing number of proteins compromises important cellular functions, including mitochondrial dynamics, endoplasmic reticulum (ER) protein folding, and signal transduction, thereby promoting synaptic damage, cell death, and neurodegeneration.
American Psychological Association (APA)
Akhtar, Mohd Waseem& Sunico, Carmen R.& Nakamura, Tomohiro& Lipton, Stuart A.. 2012. Redox Regulation of Protein Function via Cysteine S-Nitrosylation and Its Relevance to Neurodegenerative Diseases. International Journal of Cell Biology،Vol. 2012, no. 2012, pp.1-9.
https://search.emarefa.net/detail/BIM-473603
Modern Language Association (MLA)
Akhtar, Mohd Waseem…[et al.]. Redox Regulation of Protein Function via Cysteine S-Nitrosylation and Its Relevance to Neurodegenerative Diseases. International Journal of Cell Biology No. 2012 (2012), pp.1-9.
https://search.emarefa.net/detail/BIM-473603
American Medical Association (AMA)
Akhtar, Mohd Waseem& Sunico, Carmen R.& Nakamura, Tomohiro& Lipton, Stuart A.. Redox Regulation of Protein Function via Cysteine S-Nitrosylation and Its Relevance to Neurodegenerative Diseases. International Journal of Cell Biology. 2012. Vol. 2012, no. 2012, pp.1-9.
https://search.emarefa.net/detail/BIM-473603
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-473603