Nitric oxide protects against mitochondrial permeabilizastion induced by gluthathione depletion: role of S-nitrosylation?

Whiteman, Matthew, Chua, Yee Liu, Zhang, Dawei, Duan, Wei, Liou, Yih-Cherng and Armstrong, Jeffrey S. 2006, Nitric oxide protects against mitochondrial permeabilizastion induced by gluthathione depletion: role of S-nitrosylation?, Biochemical and biophysical research comminications, vol. 339, no. 1, pp. 255-262.

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Title Nitric oxide protects against mitochondrial permeabilizastion induced by gluthathione depletion: role of S-nitrosylation?
Author(s) Whiteman, Matthew
Chua, Yee Liu
Zhang, Dawei
Duan, Wei
Liou, Yih-Cherng
Armstrong, Jeffrey S.
Journal name Biochemical and biophysical research comminications
Volume number 339
Issue number 1
Start page 255
End page 262
Publisher Academic Press
Place of publication San Diego Calif.
Publication date 2006-01-06
ISSN 0006-291X
1090-2104
Keyword(s) nitric oxide
glutathione
S-nitrosylation
mitochondrial membrane permeabilization
peroxynitrite
superoxide
nitrotyrosine
reactive oxygen species
Summary 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 ONOOformation) 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.
Language eng
Field of Research 110199 Medical Biochemistry and Metabolomics not elsewhere classified
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2005, Elsevier Inc.
Persistent URL http://hdl.handle.net/10536/DRO/DU:30009163

Document type: Journal Article
Collection: School of Medicine
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