PubMed:17110372 JSONTXT

{"project":"LitCoin-PubTator-for-Tuning","denotations":[{"id":"2","span":{"begin":9,"end":20},"obj":"ChemicalEntity"},{"id":"3","span":{"begin":39,"end":44},"obj":"GeneOrGeneProduct"},{"id":"18","span":{"begin":89,"end":94},"obj":"GeneOrGeneProduct"},{"id":"19","span":{"begin":236,"end":241},"obj":"ChemicalEntity"},{"id":"20","span":{"begin":257,"end":262},"obj":"GeneOrGeneProduct"},{"id":"21","span":{"begin":305,"end":316},"obj":"ChemicalEntity"},{"id":"22","span":{"begin":321,"end":326},"obj":"GeneOrGeneProduct"},{"id":"23","span":{"begin":516,"end":521},"obj":"GeneOrGeneProduct"},{"id":"24","span":{"begin":626,"end":637},"obj":"ChemicalEntity"},{"id":"25","span":{"begin":651,"end":675},"obj":"ChemicalEntity"},{"id":"26","span":{"begin":907,"end":931},"obj":"ChemicalEntity"},{"id":"27","span":{"begin":942,"end":945},"obj":"ChemicalEntity"},{"id":"28","span":{"begin":999,"end":1010},"obj":"ChemicalEntity"},{"id":"29","span":{"begin":1053,"end":1064},"obj":"ChemicalEntity"},{"id":"30","span":{"begin":1087,"end":1092},"obj":"GeneOrGeneProduct"},{"id":"31","span":{"begin":1148,"end":1153},"obj":"GeneOrGeneProduct"}],"attributes":[{"id":"A2","pred":"tao:has_database_id","subj":"2","obj":"MESH:D002784"},{"id":"A3","pred":"tao:has_database_id","subj":"3","obj":"Gene:1181"},{"id":"A18","pred":"tao:has_database_id","subj":"18","obj":"Gene:1181"},{"id":"A19","pred":"tao:has_database_id","subj":"19","obj":"MESH:D008055"},{"id":"A20","pred":"tao:has_database_id","subj":"20","obj":"Gene:1181"},{"id":"A21","pred":"tao:has_database_id","subj":"21","obj":"MESH:D002784"},{"id":"A22","pred":"tao:has_database_id","subj":"22","obj":"Gene:1181"},{"id":"A23","pred":"tao:has_database_id","subj":"23","obj":"Gene:1181"},{"id":"A24","pred":"tao:has_database_id","subj":"24","obj":"MESH:D002784"},{"id":"A25","pred":"tao:has_database_id","subj":"25","obj":"MESH:C108732"},{"id":"A26","pred":"tao:has_database_id","subj":"26","obj":"MESH:D020122"},{"id":"A27","pred":"tao:has_database_id","subj":"27","obj":"MESH:D000255"},{"id":"A28","pred":"tao:has_database_id","subj":"28","obj":"MESH:D002784"},{"id":"A29","pred":"tao:has_database_id","subj":"29","obj":"MESH:D002784"},{"id":"A30","pred":"tao:has_database_id","subj":"30","obj":"Gene:1181"},{"id":"A31","pred":"tao:has_database_id","subj":"31","obj":"Gene:1181"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}

{"project":"LitCoin-PubTator_CellLine","denotations":[{"id":"T1","span":{"begin":465,"end":471},"obj":"CellLine"}],"attributes":[{"id":"A1","pred":"cellosaurus_accession_id","subj":"T1","obj":"CVCL_0045"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":174},"obj":"Sentence"},{"id":"T3","span":{"begin":175,"end":365},"obj":"Sentence"},{"id":"T4","span":{"begin":366,"end":515},"obj":"Sentence"},{"id":"T5","span":{"begin":516,"end":676},"obj":"Sentence"},{"id":"T6","span":{"begin":677,"end":805},"obj":"Sentence"},{"id":"T7","span":{"begin":806,"end":956},"obj":"Sentence"},{"id":"T8","span":{"begin":957,"end":1031},"obj":"Sentence"},{"id":"T9","span":{"begin":1032,"end":1261},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":568,"end":586},"obj":"HP_0003103"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":71,"end":87},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0025464"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"Body_part"},{"id":"T4","span":{"begin":227,"end":235},"obj":"Body_part"},{"id":"T7","span":{"begin":343,"end":351},"obj":"Body_part"},{"id":"T10","span":{"begin":568,"end":577},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A6","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A8","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A9","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A11","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A12","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":581,"end":586},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0002324"}],"text":"Membrane cholesterol content modulates ClC-2 gating and sensitivity to oxidative stress.\nClC-2 is a broadly expressed member of the voltage-gated ClC chloride channel family. In this study, we aimed to evaluate the role of the membrane lipid environment in ClC-2 function, and in particular the effect of cholesterol and ClC-2 distribution in membrane microdomains. Detergent-resistant and detergent-soluble microdomains (DSM) were isolated from stably transfected HEK293 cells by a discontinuous OptiPrep gradient. ClC-2 was found concentrated in detergent-insoluble membranes in basal conditions and relocalized to DSM upon cholesterol depletion by methyl-beta-cyclodextrin. As assessed by patch clamp recordings, relocalization was accompanied by acceleration of the activation kinetics of the channel. A similar distribution and activation pattern were obtained when cells were treated with the oxidant tert-butyl hydroperoxide and after ATP depletion. In both cases activation was prevented by cholesterol enrichment of cells. We conclude that the cholesterol environment regulates ClC-2 activity, and we provide evidence that the increase in ClC-2 activity in response to acute oxidative or metabolic stress involves relocalization of this channel to DSM."}