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S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a common paradigm for gasotransmitter signaling by H2S and NO.
Methods. 2013 Aug 01; 62(2):177-81.M

Abstract

Sulfhydryl groups on protein Cys residues undergo an array of oxidative reactions and modifications, giving rise to a virtual redox zip code with physiological and pathophysiological relevance for modulation of protein structure and functions. While over two decades of studies have established NO-dependent S-nitrosylation as ubiquitous and fundamental for the regulation of diverse protein activities, proteomic methods for studying H2S-dependent S-sulfhydration have only recently been described and now suggest that this is also an abundant modification with potential for global physiological importance. Notably, protein S-sulfhydration and S-nitrosylation bear striking similarities in terms of their chemical and biological determinants, as well as reversal of these modifications via group-transfer to glutathione, followed by the removal from glutathione by enzymes that have apparently evolved to selectively catalyze denitrosylation and desulfhydration. Here we review determinants of protein and low-molecular-weight thiol S-sulfhydration/desulfhydration, similarities with S-nitrosylation/denitrosylation, and methods that are being employed to investigate and quantify these gasotransmitter-mediated cell signaling systems.

Authors+Show Affiliations

Department of Pharmacology, Weill Cornell College of Medicine, 1300 York Avenue, New York, NY, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Review

Language

eng

PubMed ID

23811297

Citation

Lu, Changyuan, et al. "S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a Common Paradigm for Gasotransmitter Signaling By H2S and NO." Methods (San Diego, Calif.), vol. 62, no. 2, 2013, pp. 177-81.
Lu C, Kavalier A, Lukyanov E, et al. S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a common paradigm for gasotransmitter signaling by H2S and NO. Methods. 2013;62(2):177-81.
Lu, C., Kavalier, A., Lukyanov, E., & Gross, S. S. (2013). S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a common paradigm for gasotransmitter signaling by H2S and NO. Methods (San Diego, Calif.), 62(2), 177-81. https://doi.org/10.1016/j.ymeth.2013.05.020
Lu C, et al. S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a Common Paradigm for Gasotransmitter Signaling By H2S and NO. Methods. 2013 Aug 1;62(2):177-81. PubMed PMID: 23811297.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a common paradigm for gasotransmitter signaling by H2S and NO. AU - Lu,Changyuan, AU - Kavalier,Adam, AU - Lukyanov,Eugene, AU - Gross,Steven S, Y1 - 2013/06/27/ PY - 2013/04/22/received PY - 2013/05/28/accepted PY - 2013/7/2/entrez PY - 2013/7/3/pubmed PY - 2014/3/13/medline KW - (N-[(6-biotinamido) hexyl]-3′-(2′-pyridyldithio) propionamide) KW - 2-(4-carboxyphenyl)-4,5-dihydro-4,4,5,5-tetramethyl-1H-imidazolyl-1-oxy-3-oxide KW - Biotin Switch KW - Biotin-HPDP KW - CBS KW - CSE KW - Cysteine KW - ETHE1 KW - GSNO KW - GSSH KW - Glutathione KW - Hydrogen sulfide KW - MMTS KW - MS/MS KW - MST KW - Nitric oxide KW - Persulfide KW - S-nitrosoglutathione KW - SH KW - SNOSID KW - SQR KW - SRB KW - Sulfhydration KW - Sulfhydryl KW - TST KW - carboxy-PTIO KW - cystathionine β-synthase KW - cystathionine γ-lyase KW - glutathione persulfide KW - mercaptopyruvate sulfurtransferase KW - methyl methane thiosulfonate KW - persulfide dioxygenase KW - sulfate reducing bacteria KW - sulfide quinone reductase KW - tandem mass spectrometry KW - thiol KW - thiosulfate sulfur transferase (a.k.a. rhodanese) SP - 177 EP - 81 JF - Methods (San Diego, Calif.) JO - Methods VL - 62 IS - 2 N2 - Sulfhydryl groups on protein Cys residues undergo an array of oxidative reactions and modifications, giving rise to a virtual redox zip code with physiological and pathophysiological relevance for modulation of protein structure and functions. While over two decades of studies have established NO-dependent S-nitrosylation as ubiquitous and fundamental for the regulation of diverse protein activities, proteomic methods for studying H2S-dependent S-sulfhydration have only recently been described and now suggest that this is also an abundant modification with potential for global physiological importance. Notably, protein S-sulfhydration and S-nitrosylation bear striking similarities in terms of their chemical and biological determinants, as well as reversal of these modifications via group-transfer to glutathione, followed by the removal from glutathione by enzymes that have apparently evolved to selectively catalyze denitrosylation and desulfhydration. Here we review determinants of protein and low-molecular-weight thiol S-sulfhydration/desulfhydration, similarities with S-nitrosylation/denitrosylation, and methods that are being employed to investigate and quantify these gasotransmitter-mediated cell signaling systems. SN - 1095-9130 UR - https://www.unboundmedicine.com/medline/citation/23811297/S_sulfhydration/desulfhydration_and_S_nitrosylation/denitrosylation:_a_common_paradigm_for_gasotransmitter_signaling_by_H2S_and_NO_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1046-2023(13)00184-9 DB - PRIME DP - Unbound Medicine ER -