Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B

Shetty, Vivekananda; Neubert, Thomas A.

doi:10.1016/j.jasms.2009.04.011

Cited by 21 publications

(12 citation statements)

References 42 publications

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“…Similar patterns of mass losses were reported by Shetty and Nubert for the sulfinamide product and sulfonic acid of a synthetic peptide containing a cysteine residue. (14, 15)…”

Section: Resultsmentioning

confidence: 99%

Cys34 Adducts of Reactive Oxygen Species in Human Serum Albumin

Grigoryan

Iavarone

et al. 2012

Chem. Res. Toxicol.

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Long-term exposures to reactive oxygen species (ROS) have been linked to scores of chronic diseases. This has motivated interest in oxidation products of the only free cysteine residue (Cys34) of human serum albumin (HSA) as possible biomarkers of ROS exposure. However, Cys34 oxidation products have not been detected in human serum or plasma. Using liquid chromatography-high resolution tandem mass spectrometry, we report accurate masses and molecular compositions of Cys34 oxidation products in the 2432 Da peptide resulting from tryptic digestion of HSA. Peptides containing the expected sulfinic (Cys-SO2H) and sulfonic (Cys-SO3H) acids, as well as an adduct representing addition of one oxygen atom and loss of two hydrogen atoms, were detected in four archived samples of human plasma and one fresh sample of human serum. We speculate that this latter adduct is a sulfinamide formed by intramolecular reaction between either the Cys34 sulfenic acid (Cys-SOH) or sulfinic acid (Cys-SO2H) and the adjacent glutamine residue (Gln33). All three Cys34 adducts were measured in the five human samples with levels decreasing in the order sulfinic acid > (proposed) sulfinamide > sulfonic acid. Parallel measurements of a negative control detected only small amounts of the Cys34 sulfonic acid and the (proposed) sulfinamide and did not detect the sulfinic acid.

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“…Similar patterns of mass losses were reported by Shetty and Nubert for the sulfinamide product and sulfonic acid of a synthetic peptide containing a cysteine residue. (14, 15)…”

Section: Resultsmentioning

confidence: 99%

Cys34 Adducts of Reactive Oxygen Species in Human Serum Albumin

Grigoryan

Iavarone

et al. 2012

Chem. Res. Toxicol.

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“…Therefore, one should not simply rely only on the MS analysis to assess formation of CySOH. Mutagenesis, chemical labeling, and MS/MS studies should accompany this as has been used to demonstrate the presence of sulfenic acids in a number of proteins (Boschi-Muller et al, 2000;Fuangthong & Helmann, 2002;Poole et al, 2007;Rehder & Borges, 2010a;Qian et al, 2011Qian et al, , 2012 and peptides (Shetty, Spellman, & Neubert, 2007;Shetty & Neubert, 2009;Rehder & Borges, 2010a).…”

Section: Direct Observation Of Sulfenic Acids By Mass Spectrometrymentioning

confidence: 99%

Chemical approaches to detect and analyze protein sulfenic acids

Furdui

Poole

2013

Mass Spectrometry Reviews

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Orchestration of many processes relying on intracellular signal transduction is recognized to require the generation of hydrogen peroxide as a second messenger, yet relatively few molecular details of how this oxidant acts to regulate protein function are currently understood. This review describes emerging chemical tools and approaches that can be applied to study protein oxidation in biological systems, with a particular emphasis on a key player in protein redox regulation, cysteine sulfenic acid. While sulfenic acids (within purified proteins or simple mixtures) are detectable by physical approaches like X-ray crystallography, nuclear magnetic resonance and mass spectrometry, the propensity of these moieties to undergo further modification in complex biological systems has necessitated the development of chemical probes, reporter groups and analytical approaches to allow for their selective detection and quantification. Provided is an overview of techniques that are currently available for the study of sulfenic acids, and some of the biologically meaningful data that have been collected using such approaches.

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“…A further MS-based analysis of peptides exposed to HOCl revealed a variety of possible sulfur-nitrogen cross-links including both sulfenamides and sulfinamides following reaction of oxidized cysteine residues with lysine, arginine or N-terminal amines (54). Sulfinamide products have also been detected following initial SOH formation in peptides corresponding to the active site of both matrix metalloproteinase-7 and protein tyrosine phosphatase 1B (132–133). …”

Section: Reactivity Of Protein-soh Intermediatesmentioning

confidence: 99%

Formation, Reactivity, and Detection of Protein Sulfenic Acids

Kettenhofen

Wood

2010

Chem. Res. Toxicol.

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It has become clear in recent decades that the post-translational modification of protein cysteine residues is a crucial regulatory event in biology. Evidence supports the reversible oxidation of cysteine thiol groups as a mechanism of redox-based signal transduction while the accumulation of proteins with irreversible thiol oxidations is a hallmark of stress-induced cellular damage. The initial formation of cysteine sulfenic acid (SOH) derivatives, along with the reactive properties of this functional group, serves as a crossroads whereby the local redox environment may dictate the progression of either regulatory or pathological outcomes. Protein-SOH are established as transient intermediates in the formation of more stable cysteine oxidation products both under basal conditions and in response to several redox-active extrinsic compounds. This review details both direct and multi-step chemical routes proposed to generate protein-SOH, the spectrum of secondary reactions that may follow their initial formation and the arsenal of experimental tools available for their detection. Both the pioneering studies that have provided a framework for our current understanding of protein-SOH as well as state-of-the-art proteomic strategies designed for global assessments of this post-translational modification are highlighted.

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Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B

Cited by 21 publications

References 42 publications

Cys34 Adducts of Reactive Oxygen Species in Human Serum Albumin

Cys34 Adducts of Reactive Oxygen Species in Human Serum Albumin

Chemical approaches to detect and analyze protein sulfenic acids

Formation, Reactivity, and Detection of Protein Sulfenic Acids

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