Detection of thiol modifications by hydrogen sulfide.
Hydrogen sulfide (H2S) is an important gasotransmitter in both animals and plants. Many physiological events, including responses to stress, have been suggested to involve H2S, at least in part. On the other hand, numerous responses have been reported following treatment with H2S, including changes in the levels of antioxidants and the activities of transcription factors. Therefore, it is important to understand and unravel the events that are taking place downstream of H2S in signaling pathways. H2S is known to interact with other reactive signaling molecules such as reactive oxygen species (ROS) and nitric oxide (NO). One of the mechanisms by which ROS and NO have effects in a cell is the modification of thiol groups on proteins, by oxidation or S-nitrosylation, respectively. Recently, it has been reported that H2S can also modify thiols. Here we report a method for the determination of thiol modifications on proteins following the treatment with biological samples with H2S donors. Here, the nematode Caenorhabditis elegans is used as a model system but this method can be used for samples from other animals or plants.
Faculty of Health and Applied Sciences, University of the West of England, Bristol, United Kingdom.
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Williams
Faculty of Health and Applied Sciences, University of the West of England, Bristol, United Kingdom.
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Pead
University of Exeter Medical School, University of Exeter, Exeter, United Kingdom.
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Whiteman
Biosciences, University of Exeter, Exeter, United Kingdom.
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Wood
Faculty of Health and Applied Sciences, University of the West of England, Bristol, United Kingdom.
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Wilson
Faculty of Health and Applied Sciences, University of the West of England, Bristol, United Kingdom.
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Ladomery
Faculty of Agriculture, University of Osijek, Osijek, Croatia.
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Teklic
Faculty of Agriculture, University of Osijek, Osijek, Croatia.
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Lisjak
Faculty of Health and Applied Sciences, University of the West of England, Bristol, United Kingdom. Electronic address: john.hancock@uwe.ac.uk.
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Hancock
D000818:Animals; D001522:Behavior, Animal / Q000187:drug effects; D017173:Caenorhabditis elegans / Q000187:drug effects* / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005452:Fluoresceins / Q000737:chemistry; D015801:Helminth Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006862:Hydrogen Sulfide / Q000378:metabolism / Q000494:pharmacology*; D009068:Movement / Q000187:drug effects; D009569:Nitric Oxide / Q000378:metabolism; D010084:Oxidation-Reduction; D011499:Protein Processing, Post-Translational; D017382:Reactive Oxygen Species / Q000378:metabolism; D015398:Signal Transduction; D013194:Staining and Labeling / Q000379:methods; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*; D013440:Sulfides / Q000737:chemistry / Q000494:pharmacology
D004220:Disulfides; D005452:Fluoresceins; D015801:Helminth Proteins; D017382:Reactive Oxygen Species; D013438:Sulfhydryl Compounds; D013440:Sulfides; D009569:Nitric Oxide; C015296:5-iodoacetamidofluorescein; D006861:Hydrogen Peroxide; C025451:sodium bisulfide; D006862:Hydrogen Sulfide
C. elegans; Hydrogen sulfide; Nitric oxide; Protein modification; Reactive oxygen species; Thiols