Use of the “Tag-Switch” Method for the Detection of Protein S-Sulfhydration

Park, Chung‐Min; Macinkovic, Igor; Filipovic, Milos R.; Xian, Ming

doi:10.1016/bs.mie.2014.11.033

Cited by 39 publications

(54 citation statements)

References 29 publications

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“…To overcome this limitation, Xian and colleagues recently developed a selective two-step approach to detect protein Ssulfhydration (Fig. 4E) (91,92). In the first step, nucleophilic protein thiol species (-SH and -SSH) are tagged with the electrophile, methylsulfonyl benzathiazole.…”

Section: The Expanding Landscape Of the Thiol Redox Proteomementioning

confidence: 99%

The Expanding Landscape of the Thiol Redox Proteome

Yang

Carroll

Liebler

2016

Molecular & Cellular Proteomics

182

111

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Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide redox equilibria, including S-sulfenylation (-SOH), S-sulfinylation (-SO 2 H), S-sulfonylation (-SO 3 H), S-nitrosylation (-SNO), S-sulfhydration (-SSH), S-glutathionylation (-SSG), and others. Emerging evidence suggests that these post-translational modifications (PTM) are important in cellular redox regulation and protection against oxidative damage. Identification of protein targets of thiol redox modifications is crucial to understanding their roles in biology and disease. However, analysis of these highly labile and dynamic modifications poses challenges. Recent advances in the design of probes for thiol redox forms, together with innovative mass spectrometry based chemoproteomics methods make it possible to perform global, site-specific, and quantitative analyses of thiol redox modifications in complex proteomes.

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Section: The Expanding Landscape Of the Thiol Redox Proteomementioning

confidence: 99%

The Expanding Landscape of the Thiol Redox Proteome

Yang

Carroll

Liebler

2016

Molecular & Cellular Proteomics

182

111

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“…"Tag-Switch" Method Nrf2 and Keap1 S-sulfhydration was detected with the "tag-switch" method (21). The protein of Keap1 was pulled down with immunoprecipitation and treated with biotin-linked cyanoacetate.…”

Section: Immunoprecipitationmentioning

confidence: 99%

Hydrogen Sulfide Induces Keap1 S-sulfhydration and Suppresses Diabetes-Accelerated Atherosclerosis via Nrf2 Activation

et al. 2016

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Hydrogen sulfide (H2S) has been shown to have powerful antioxidative and anti-inflammatory properties that can regulate multiple cardiovascular functions. However, its precise role in diabetes-accelerated atherosclerosis remains unclear. We report here that H2S reduced aortic atherosclerotic plaque formation with reduction in superoxide (O2−) generation and the adhesion molecules in streptozotocin (STZ)-induced LDLr−/− mice but not in LDLr−/−Nrf2−/− mice. In vitro, H2S inhibited foam cell formation, decreased O2− generation, and increased nuclear factor erythroid 2–related factor 2 (Nrf2) nuclear translocation and consequently heme oxygenase 1 (HO-1) expression upregulation in high glucose (HG) plus oxidized LDL (ox-LDL)–treated primary peritoneal macrophages from wild-type but not Nrf2−/− mice. H2S also decreased O2− and adhesion molecule levels and increased Nrf2 nuclear translocation and HO-1 expression, which were suppressed by Nrf2 knockdown in HG/ox-LDL–treated endothelial cells. H2S increased S-sulfhydration of Keap1, induced Nrf2 dissociation from Keap1, enhanced Nrf2 nuclear translocation, and inhibited O2− generation, which were abrogated after Keap1 mutated at Cys151, but not Cys273, in endothelial cells. Collectively, H2S attenuates diabetes-accelerated atherosclerosis, which may be related to inhibition of oxidative stress via Keap1 sulfhydrylation at Cys151 to activate Nrf2 signaling. This may provide a novel therapeutic target to prevent atherosclerosis in the context of diabetes.

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“…2-(Methylsulfonyl)1,3-benzothiazole was purchased from Santa Cruz Biotechnology. CN-biotin was synthesized as described previously (19,30).…”

Section: Kinetics Of Hydrogen Sulfide Reactions With Disulfides By DImentioning

confidence: 99%

“…Tag-switch Assay-Labeling of persulfides in HSA preparations (dot blots) and fixed cells was performed following an established protocol (19,30). 2-(Methylsulfonyl)1,3-benzothiazole was purchased from Santa Cruz Biotechnology.…”

Section: Kinetics Of Hydrogen Sulfide Reactions With Disulfides By DImentioning

confidence: 99%

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Cuevasanta

Lange

Bonanata

et al. 2015

Journal of Biological Chemistry

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282

344

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Background:Hydrogen sulfide (H 2 S) modulates physiological processes in mammals. Results: The reactivity of H 2 S toward disulfides (RSSR) and albumin sulfenic acid (RSOH) to form persulfides (RSSH) was assessed. Conclusion: H 2 S is less reactive than thiols. Persulfides have enhanced nucleophilicity. Significance: This kinetic study helps rationalize the contribution of the reactions with oxidized thiol derivatives to H 2 S biology.

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Use of the “Tag-Switch” Method for the Detection of Protein S-Sulfhydration

Cited by 39 publications

References 29 publications

The Expanding Landscape of the Thiol Redox Proteome

The Expanding Landscape of the Thiol Redox Proteome

Hydrogen Sulfide Induces Keap1 S-sulfhydration and Suppresses Diabetes-Accelerated Atherosclerosis via Nrf2 Activation

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

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