Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2005.10.200
Title: Nitric oxide protects against mitochondrial permeabilization induced by glutathione depletion: Role of S-nitrosylation?
Authors: Whiteman, M. 
Chua, Y.L.
Zhang, D.
Duan, W. 
Liou, Y.-C. 
Armstrong, J.S. 
Keywords: Glutathione
Mitochondrial membrane permeabilization
Nitric oxide
Nitrotyrosine
Peroxynitrite
Reactive oxygen species
S-nitrosylation
Superoxide
Issue Date: 2006
Source: Whiteman, M.,Chua, Y.L.,Zhang, D.,Duan, W.,Liou, Y.-C.,Armstrong, J.S. (2006). Nitric oxide protects against mitochondrial permeabilization induced by glutathione depletion: Role of S-nitrosylation?. Biochemical and Biophysical Research Communications 339 (1) : 255-262. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2005.10.200
Abstract: Nitric oxide (NO) is known to mediate a multitude of biological effects including inhibition of respiration at cytochrome c oxidase (COX), formation of peroxynitrite (ONOO-) by reaction with mitochondrial superoxide (O2-), and S-nitrosylation of proteins. In this study, we investigated pathways of NO metabolism in lymphoblastic leukemic CEM cells in response to glutathione (GSH) depletion. We found that NO blocked mitochondrial protein thiol oxidation, membrane permeabilization, and cell death. The effects of NO were: (1) independent of respiratory chain inhibition since protection was also observed in CEM cells lacking mitochondrial DNA (ρ0) which do not possess a functional respiratory chain and (2) independent of ONOO - formation since nitrotyrosine (a marker for ONOO- formation) was not detected in extracts from cells treated with NO after GSH depletion. However, NO increased the level of mitochondrial protein S-nitrosylation (SNO) determined by the Biotin Switch assay and by the release of NO from mitochondrial fractions treated with mercuric chloride (which cleaves SNO bonds to release NO). In conclusion, these results indicate that NO blocks cell death after GSH depletion by preserving the redox status of mitochondrial protein thiols probably by a mechanism that involves S-nitrosylation of mitochondrial protein thiols. © 2005 Elsevier Inc. All rights reserved.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/28624
ISSN: 0006291X
10902104
DOI: 10.1016/j.bbrc.2005.10.200
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