ArticleJournal of the American Society for Mass Spectrometry2007
Identification of redox sensitive thiols of protein disulfide isomerase using isotope coded affinity technology and mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- A How-To Guide for Mode of Action Analysis of Antimicrobial Peptides.Frontiers in cellular and infection microbiology · 2020Review
- Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47Arteriosclerosis, thrombosis, and vascular biology · 2019Article
- Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein-disulfide isomerase.The Journal of biological chemistry · 2018Article
- Structural and Functional Properties Changes of β-Conglycinin Exposed to Hydroxyl Radical-Generating Systems.Molecules (Basel, Switzerland) · 2017Article
- Regulation of neovascularization by S-glutathionylation via the Wnt5a/sFlt-1 pathway.Biochemical Society transactions · 2014Review
- Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Molecular & cellular proteomics : MCP · 2012Review
- Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach.Molecular & cellular proteomics : MCP · 2010Article
- Probing mechanisms of axonopathy. Part I: Protein targets of 1,2-diacetylbenzene, the neurotoxic metabolite of aromatic solvent 1,2-diethylbenzene.Toxicological sciences : an official journal of the Society of Toxicology · 2008Article
- Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
6 authors.
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Abstract
Regulation of the redox state of protein disulfide isomerase (PDI) is critical for its various catalytic functions. Here we describe a procedure utilizing isotope-coded affinity tag (ICAT) technology and mass spectrometry that quantitates relative changes in the dynamic thiol and disulfide states of human PDI. Human PDI contains six cysteine residues, four present in two active sites within the a and a' domains, and two present in the b' domain. ICAT labeling of human PDI indicates a difference between the redox state of the two active sites. Furthermore, under auto-oxidation conditions an approximately 80% decrease in available thiols within the a domain was detected. Surprisingly, the redox state of one of the two cysteines, Cys-295, within the b' domain was altered between the fully reduced and the auto-oxidized state of PDI while the other b' domain cysteine remained fully reduced. An interesting mono- and dioxidation modification of an invariable tryptophan residue, Trp-35, within the active site was also mapped by tandem mass spectrometry. Our findings indicate that ICAT methodology in conjunction with mass spectrometry represents a powerful tool to monitor changes in the redox state of individual cysteine residues within PDI under various conditions.
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