{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tsou PS"],"funding":["NHLBI NIH HHS"],"pagination":["649-56"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2672869"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["329(2)"],"pubmed_abstract":["We hypothesize that nitroglycerin (NTG) causes direct oxidation of multiple cellular sulfhydryl (SH) proteins and that manipulation of SH redox status affects NTG tolerance. In LLC-PK1 cells, we found that nitrate tolerance, as indicated by cGMP accumulation toward NTG, was accompanied by increased protein [(35)S]cysteine incorporation, significant S-glutathionylation of multiple proteins, and decreased metabolic activity of several SH-sensitive enzymes, including creatine kinase, xanthine oxidoreductase, and glutaredoxin (GRX). Cells overexpressing GRX exhibited reduced cellular protein S-glutathionylation (PSSG) and absence of NTG tolerance, whereas those with silenced GRX showed increased extent of NTG-induced tolerance. Incubation of LLC-PK1 cells with oxidized glutathione led to sever"],"journal":["The Journal of pharmacology and experimental therapeutics"],"pubmed_title":["Role of glutaredoxin-mediated protein S-glutathionylation in cellular nitroglycerin tolerance."],"pmcid":["PMC2672869"],"funding_grant_id":["HL081580"],"pubmed_authors":["Tsou PS","Fung HL","Page NA","Addanki V","Haas JA"],"additional_accession":[]},"is_claimable":false,"name":"Role of glutaredoxin-mediated protein S-glutathionylation in cellular nitroglycerin tolerance.","description":"We hypothesize that nitroglycerin (NTG) causes direct oxidation of multiple cellular sulfhydryl (SH) proteins and that manipulation of SH redox status affects NTG tolerance. In LLC-PK1 cells, we found that nitrate tolerance, as indicated by cGMP accumulation toward NTG, was accompanied by increased protein [(35)S]cysteine incorporation, significant S-glutathionylation of multiple proteins, and decreased metabolic activity of several SH-sensitive enzymes, including creatine kinase, xanthine oxidoreductase, and glutaredoxin (GRX). Cells overexpressing GRX exhibited reduced cellular protein S-glutathionylation (PSSG) and absence of NTG tolerance, whereas those with silenced GRX showed increased extent of NTG-induced tolerance. Incubation of LLC-PK1 cells with oxidized glutathione led to sever","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 May","modification":"2025-04-22T06:48:51.635Z","creation":"2019-03-27T00:21:58Z"},"accession":"S-EPMC2672869","cross_references":{"pubmed":["19223666"],"doi":["10.1124/jpet.108.149997"]}}