{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nelson KJ"],"funding":["HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)","NIA NIH HHS","NIEHS NIH HHS","HHS | NIH | National Institute on Aging (NIA)","NCI NIH HHS","NIAMS NIH HHS","HHS | NIH | National Cancer Institute (NCI)"],"pagination":["16376-16389"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6200941"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["293(42)"],"pubmed_abstract":["Reactive oxygen species (ROS), in particular H<sub>2</sub>O<sub>2</sub>, regulate intracellular signaling through reversible oxidation of reactive protein thiols present in a number of kinases and phosphatases. H<sub>2</sub>O<sub>2</sub> has been shown to regulate mitogen-activated protein kinase (MAPK) signaling depending on the cellular context. We report here that in human articular chondrocytes, the MAPK family member c-Jun N-terminal kinase 2 (JNK2) is activated by fibronectin fragments and low physiological levels of H<sub>2</sub>O<sub>2</sub> and inhibited by oxidation due to elevated levels of H<sub>2</sub>O<sub>2</sub> The kinase activity of affinity-purified, phosphorylated JNK2 from cultured chondrocytes was reversibly inhibited by 5-20 μm H<sub>2</sub>O<sub>2</sub> Using dimedo"],"journal":["The Journal of biological chemistry"],"pubmed_title":["H<sub>2</sub>O<sub>2</sub> oxidation of cysteine residues in c-Jun N-terminal kinase 2 (JNK2) contributes to redox regulation in human articular chondrocytes."],"pmcid":["PMC6200941"],"funding_grant_id":["P 30 CA012197","R33 CA126659","F31 AG032796","R33 CA177461","P30 CA012197","RO1 AG044034","F32 AG032796","R01 AG044034","R37 AR049003","R33 ES025645"],"pubmed_authors":["Collins JA","Burke EA","Reisz JA","Wood ST","Poole LB","Klomsiri C","Bolduc JA","Yammani RR","Furdui CM","Nelson KJ","Wu H","Loeser RF"],"additional_accession":[]},"is_claimable":false,"name":"H<sub>2</sub>O<sub>2</sub> oxidation of cysteine residues in c-Jun N-terminal kinase 2 (JNK2) contributes to redox regulation in human articular chondrocytes.","description":"Reactive oxygen species (ROS), in particular H<sub>2</sub>O<sub>2</sub>, regulate intracellular signaling through reversible oxidation of reactive protein thiols present in a number of kinases and phosphatases. H<sub>2</sub>O<sub>2</sub> has been shown to regulate mitogen-activated protein kinase (MAPK) signaling depending on the cellular context. We report here that in human articular chondrocytes, the MAPK family member c-Jun N-terminal kinase 2 (JNK2) is activated by fibronectin fragments and low physiological levels of H<sub>2</sub>O<sub>2</sub> and inhibited by oxidation due to elevated levels of H<sub>2</sub>O<sub>2</sub> The kinase activity of affinity-purified, phosphorylated JNK2 from cultured chondrocytes was reversibly inhibited by 5-20 μm H<sub>2</sub>O<sub>2</sub> Using dimedo","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2026-04-29T08:52:57.961Z","creation":"2019-10-30T08:14:05Z"},"accession":"S-EPMC6200941","cross_references":{"pubmed":["30190325"],"doi":["10.1074/jbc.ra118.004613","10.1074/jbc.RA118.004613"]}}