Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2005.10.200
DC FieldValue
dc.titleNitric oxide protects against mitochondrial permeabilization induced by glutathione depletion: Role of S-nitrosylation?
dc.contributor.authorWhiteman, M.
dc.contributor.authorChua, Y.L.
dc.contributor.authorZhang, D.
dc.contributor.authorDuan, W.
dc.contributor.authorLiou, Y.-C.
dc.contributor.authorArmstrong, J.S.
dc.date.accessioned2011-11-29T05:57:29Z
dc.date.available2011-11-29T05:57:29Z
dc.date.issued2006
dc.identifier.citationWhiteman, 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
dc.identifier.issn0006291X
dc.identifier.issn10902104
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/28624
dc.description.abstractNitric 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbrc.2005.10.200
dc.sourceScopus
dc.subjectGlutathione
dc.subjectMitochondrial membrane permeabilization
dc.subjectNitric oxide
dc.subjectNitrotyrosine
dc.subjectPeroxynitrite
dc.subjectReactive oxygen species
dc.subjectS-nitrosylation
dc.subjectSuperoxide
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/j.bbrc.2005.10.200
dc.description.sourcetitleBiochemical and Biophysical Research Communications
dc.description.volume339
dc.description.issue1
dc.description.page255-262
dc.description.codenBBRCA
dc.identifier.isiut000233944500039
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