Regulation of hyperoxia-induced neonatal lung injury via post-translational cysteine redox modifications

Zhang, Tong; Day, Nicholas; Gaffrey, Matthew J.; Weitz, Karl K.; Attah, Kwame; Mimche, Patrice N.; Paine, Robert; Qian, Weijun; Helms, My N.

doi:10.1016/j.redox.2022.102405

Cited by 4 publications

(6 citation statements)

References 96 publications

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“…Protein S-glutathionylation plays a critical role in ROS-mediated signaling and various cellular functions under physiological conditions, while abnormal regulation of SSG can lead to disease development. Recent biochemical and analytical advances have enabled in-depth SSG proteome profiling, and several studies have reported that the SSG modifications occur broadly across all subcellular compartments [ 77 , 78 , 83 ]. The coverage of the SSG proteome might be further enhanced by adopting recent workflows involving fractionation followed by LC-MS/MS, where a deep coverage of the thiol redox proteome was demonstrated for thiol oxidation [ 87 , 119 ].…”

Section: Discussionmentioning

confidence: 99%

“…RAC-TMT and similar approaches have been applied to investigate protein SSG changes under physiological and pathological conditions in different cell types and tissues [ 8 , 77 , 78 , 81 , 82 ]. For example, in a recent study of redox regulation in hyperoxia-induced lung injury, over 7600 SSG sites were quantified by RAC-TMT, providing a landscape view of the SSG proteome in the mouse lung [ 83 ]. In another study, Duan et al quantified both SSG and total oxidation occupancies for ~4000 Cys sites under basal conditions in mouse RAW macrophages, revealing a mean occupancy of 4.0% for SSG and 11.9% for total oxidation [ 78 ].…”

Section: Methods For Characterizing Protein S-glutathionylationmentioning

confidence: 99%

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Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches

Zhang

Day

et al. 2022

Antioxidants

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Protein S-glutathionylation (SSG) is a reversible post-translational modification (PTM) featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein structure, activity, subcellular localization, and interaction with small molecules and other proteins. Thus, it plays a critical role in redox signaling and regulation in various physiological activities and pathological events. In this review, we summarize current biochemical and analytical approaches for characterizing SSG at both the proteome level and at individual protein levels. To illustrate the mechanism underlying SSG-mediated redox regulation, we highlight recent examples of functional and structural consequences of SSG modifications. Finally, we discuss the analytical challenges in characterizing SSG and the thiol PTM landscape, future directions for understanding of the role of SSG in redox signaling and regulation and its interplay with other PTMs, and the potential role of computational approaches to accelerate functional discovery.

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Section: Discussionmentioning

confidence: 99%

Section: Methods For Characterizing Protein S-glutathionylationmentioning

confidence: 99%

Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches

Zhang

Day

et al. 2022

Antioxidants

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“…The occupancies of thiol oxidation at site-specific level are calculated by comparing TMT intensities between thiol oxidation channels and total thiol channels for individual Cys sites. RAC-TMT has been applied to cyanobacteria [54], metazoan cell lines [52,55,56], and mammalian tissues [19,38,57]. Besides TMT-based quantification, RAC has been employed for label-free quantification to characterize thiol oxidation in various organisms [58][59][60][61].…”

Section: General Principles and Methods For Thiol Oxidationmentioning

confidence: 99%

“…Under basal conditions, the average SSG and total oxidation occupancies were 4.0% and 11.9%, respectively, in macrophages cells. This workflow had also been applied to several other studies, including muscle and lung tissues [19, 38, 55].…”

Section: Selective Reduction and Tagging‐based Approachesmentioning

confidence: 99%

“…Mass spectrometry (MS) has become the leading platform for large-scale PTM profiling, including redox PTMs [14][15][16]. The emerging field of redox proteomics is focused on advancing analytical approaches for enabling quantitative, site-specific measurements of various types of redox PTMs to decipher redox-dependent mechanisms in various biological systems [17][18][19]. Redox proteomics approaches can be categorized into several general strategies according to their chemical principles.…”

Section: Introductionmentioning

confidence: 99%

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Thiol redox proteomics: Characterization of thiol‐based post‐translational modifications

Gluth

Zhang

et al. 2023

Proteomics

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Redox post-translational modifications on cysteine thiols (redox PTMs) have profound effects on protein structure and function, thus enabling regulation of various biological processes. Redox proteomics approaches aim to characterize the landscape of redox PTMs at the systems level. These approaches facilitate studies of condition-specific, dynamic processes implicating redox PTMs and have furthered our understanding of redox signaling and regulation. Mass spectrometry (MS) is a powerful tool for such analyses which has been demonstrated by significant advances in redox proteomics during the last decade. A group of well-established approaches involves the initial blocking of free thiols followed by selective reduction of oxidized PTMs and subsequent enrichment for downstream detection. Alternatively, novel chemoselective probe-based approaches have been developed for various redox PTMs. Direct detection of redox PTMs without any enrichment has also been demonstrated given the sensitivity of contemporary MS instruments. This review discusses the general principles behind different analytical strategies and covers recent advances in redox proteomics. Several applications of redox proteomics are also highlighted to illustrate how large-scale redox proteomics data can lead to novel biological insights.

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Recent advances in mass spectrometry-based methods to investigate reversible cysteine oxidation

Stair,

Hicks

2023

Current Opinion in Chemical Biology

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Regulation of hyperoxia-induced neonatal lung injury via post-translational cysteine redox modifications

Cited by 4 publications

References 96 publications

Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches

Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches

Thiol redox proteomics: Characterization of thiol‐based post‐translational modifications

Recent advances in mass spectrometry-based methods to investigate reversible cysteine oxidation

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