biostudies-literatureNelson KJHHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)NIA NIH HHSNIEHS NIH HHSHHS | NIH | National Institute on Aging (NIA)NCI NIH HHSNIAMS NIH HHSHHS | NIH | National Cancer Institute (NCI)16376-16389https://www.ebi.ac.uk/biostudies/studies/S-EPMC6200941biostudies-literatureUnknown293(42)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 dimedoThe Journal of biological chemistryH<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.PMC6200941P 30 CA012197R33 CA126659F31 AG032796R33 CA177461P30 CA012197RO1 AG044034F32 AG032796R01 AG044034R37 AR049003R33 ES025645Collins JABurke EAReisz JAWood STPoole LBKlomsiri CBolduc JAYammani RRFurdui CMNelson KJWu HLoeser RFfalseH<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.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 dimedo2018-01-01T00:00:00Z2018 Oct2026-04-29T08:52:57.961Z2019-10-30T08:14:05ZS-EPMC62009413019032510.1074/jbc.ra118.00461310.1074/jbc.RA118.004613