PubMed:10026134 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":160},"obj":"Sentence"},{"id":"T2","span":{"begin":161,"end":364},"obj":"Sentence"},{"id":"T3","span":{"begin":365,"end":599},"obj":"Sentence"},{"id":"T4","span":{"begin":600,"end":718},"obj":"Sentence"},{"id":"T5","span":{"begin":719,"end":788},"obj":"Sentence"},{"id":"T6","span":{"begin":789,"end":900},"obj":"Sentence"},{"id":"T7","span":{"begin":901,"end":965},"obj":"Sentence"},{"id":"T8","span":{"begin":966,"end":1077},"obj":"Sentence"},{"id":"T9","span":{"begin":1078,"end":1183},"obj":"Sentence"},{"id":"T10","span":{"begin":1184,"end":1403},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Cadmium-mediated activation of the metal response element in human neuroblastoma cells lacking functional metal response element-binding transcription factor-1.\nMetal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of mouse MT gene (mMT-I) promoter activation by cadmium and zinc in IMR-32 human neuroblastoma cells to determine whether MTF-1 binding to the MRE is necessary for activation by these metals. Cadmium activated a mMT-1 promoter (-150 base pairs) luciferase reporter 20-25-fold through a MRE-dependent mechanism. In contrast, zinc had little effect on the mMT-1 luciferase reporter. IMR-32 cells lacked MRE binding activity, and treatment with zinc in vitro or in vivo did not generate a MTF-1. MRE complex, suggesting that IMR-32 cells lack functional MTF-1. Overexpression of mMTF-1 regenerated a zinc-mediated induction of the MRE without affecting cadmium activation. Because no other transition metals tested activated the MRE, this effect appeared to be cadmium-specific. These data demonstrate that in IMR-32 human neuroblastoma cells, zinc and cadmium can use independent mechanisms for activation of the mMT-I promoter and cadmium-mediated MRE activation is independent of MTF-1 and zinc."}

{"project":"PennBioIE","denotations":[{"id":"T1","span":{"begin":67,"end":80},"obj":"protein"},{"id":"T2","span":{"begin":106,"end":159},"obj":"protein"},{"id":"T3","span":{"begin":170,"end":214},"obj":"protein"},{"id":"T4","span":{"begin":216,"end":221},"obj":"protein"},{"id":"T5","span":{"begin":295,"end":310},"obj":"protein"},{"id":"T6","span":{"begin":312,"end":314},"obj":"protein"},{"id":"T7","span":{"begin":417,"end":419},"obj":"protein"},{"id":"T8","span":{"begin":426,"end":431},"obj":"protein"},{"id":"T9","span":{"begin":489,"end":502},"obj":"protein"},{"id":"T10","span":{"begin":530,"end":535},"obj":"protein"},{"id":"T11","span":{"begin":620,"end":625},"obj":"protein"},{"id":"T12","span":{"begin":653,"end":663},"obj":"protein"},{"id":"T13","span":{"begin":762,"end":767},"obj":"protein"},{"id":"T14","span":{"begin":768,"end":778},"obj":"protein"},{"id":"T15","span":{"begin":894,"end":899},"obj":"protein"},{"id":"T16","span":{"begin":959,"end":964},"obj":"protein"},{"id":"T17","span":{"begin":984,"end":990},"obj":"protein"},{"id":"T18","span":{"begin":1228,"end":1241},"obj":"protein"},{"id":"T19","span":{"begin":1319,"end":1324},"obj":"protein"},{"id":"T20","span":{"begin":1388,"end":1393},"obj":"protein"}],"text":"Cadmium-mediated activation of the metal response element in human neuroblastoma cells lacking functional metal response element-binding transcription factor-1.\nMetal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of mouse MT gene (mMT-I) promoter activation by cadmium and zinc in IMR-32 human neuroblastoma cells to determine whether MTF-1 binding to the MRE is necessary for activation by these metals. Cadmium activated a mMT-1 promoter (-150 base pairs) luciferase reporter 20-25-fold through a MRE-dependent mechanism. In contrast, zinc had little effect on the mMT-1 luciferase reporter. IMR-32 cells lacked MRE binding activity, and treatment with zinc in vitro or in vivo did not generate a MTF-1. MRE complex, suggesting that IMR-32 cells lack functional MTF-1. Overexpression of mMTF-1 regenerated a zinc-mediated induction of the MRE without affecting cadmium activation. Because no other transition metals tested activated the MRE, this effect appeared to be cadmium-specific. These data demonstrate that in IMR-32 human neuroblastoma cells, zinc and cadmium can use independent mechanisms for activation of the mMT-I promoter and cadmium-mediated MRE activation is independent of MTF-1 and zinc."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":489,"end":502},"obj":"HP_0003006"},{"id":"T2","span":{"begin":1228,"end":1241},"obj":"HP_0003006"}],"text":"Cadmium-mediated activation of the metal response element in human neuroblastoma cells lacking functional metal response element-binding transcription factor-1.\nMetal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of mouse MT gene (mMT-I) promoter activation by cadmium and zinc in IMR-32 human neuroblastoma cells to determine whether MTF-1 binding to the MRE is necessary for activation by these metals. Cadmium activated a mMT-1 promoter (-150 base pairs) luciferase reporter 20-25-fold through a MRE-dependent mechanism. In contrast, zinc had little effect on the mMT-1 luciferase reporter. IMR-32 cells lacked MRE binding activity, and treatment with zinc in vitro or in vivo did not generate a MTF-1. MRE complex, suggesting that IMR-32 cells lack functional MTF-1. Overexpression of mMTF-1 regenerated a zinc-mediated induction of the MRE without affecting cadmium activation. Because no other transition metals tested activated the MRE, this effect appeared to be cadmium-specific. These data demonstrate that in IMR-32 human neuroblastoma cells, zinc and cadmium can use independent mechanisms for activation of the mMT-I promoter and cadmium-mediated MRE activation is independent of MTF-1 and zinc."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":67,"end":80},"obj":"Phenotype"},{"id":"T2","span":{"begin":489,"end":502},"obj":"Phenotype"},{"id":"T3","span":{"begin":1228,"end":1241},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0003006"},{"id":"A2","pred":"hp_id","subj":"T2","obj":"HP:0003006"},{"id":"A3","pred":"hp_id","subj":"T3","obj":"HP:0003006"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Cadmium-mediated activation of the metal response element in human neuroblastoma cells lacking functional metal response element-binding transcription factor-1.\nMetal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of mouse MT gene (mMT-I) promoter activation by cadmium and zinc in IMR-32 human neuroblastoma cells to determine whether MTF-1 binding to the MRE is necessary for activation by these metals. Cadmium activated a mMT-1 promoter (-150 base pairs) luciferase reporter 20-25-fold through a MRE-dependent mechanism. In contrast, zinc had little effect on the mMT-1 luciferase reporter. IMR-32 cells lacked MRE binding activity, and treatment with zinc in vitro or in vivo did not generate a MTF-1. MRE complex, suggesting that IMR-32 cells lack functional MTF-1. Overexpression of mMTF-1 regenerated a zinc-mediated induction of the MRE without affecting cadmium activation. Because no other transition metals tested activated the MRE, this effect appeared to be cadmium-specific. These data demonstrate that in IMR-32 human neuroblastoma cells, zinc and cadmium can use independent mechanisms for activation of the mMT-I promoter and cadmium-mediated MRE activation is independent of MTF-1 and zinc."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":67,"end":80},"obj":"Disease"},{"id":"T2","span":{"begin":489,"end":502},"obj":"Disease"},{"id":"T3","span":{"begin":1228,"end":1241},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005072"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005072"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005072"}],"text":"Cadmium-mediated activation of the metal response element in human neuroblastoma cells lacking functional metal response element-binding transcription factor-1.\nMetal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of mouse MT gene (mMT-I) promoter activation by cadmium and zinc in IMR-32 human neuroblastoma cells to determine whether MTF-1 binding to the MRE is necessary for activation by these metals. Cadmium activated a mMT-1 promoter (-150 base pairs) luciferase reporter 20-25-fold through a MRE-dependent mechanism. In contrast, zinc had little effect on the mMT-1 luciferase reporter. IMR-32 cells lacked MRE binding activity, and treatment with zinc in vitro or in vivo did not generate a MTF-1. MRE complex, suggesting that IMR-32 cells lack functional MTF-1. Overexpression of mMTF-1 regenerated a zinc-mediated induction of the MRE without affecting cadmium activation. Because no other transition metals tested activated the MRE, this effect appeared to be cadmium-specific. These data demonstrate that in IMR-32 human neuroblastoma cells, zinc and cadmium can use independent mechanisms for activation of the mMT-I promoter and cadmium-mediated MRE activation is independent of MTF-1 and zinc."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":61,"end":66},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":411,"end":416},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":483,"end":488},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1222,"end":1227},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"10088"},{"id":"A3","pred":"db_id","subj":"T2","obj":"10090"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"}],"text":"Cadmium-mediated activation of the metal response element in human neuroblastoma cells lacking functional metal response element-binding transcription factor-1.\nMetal response element-binding transcription factor-1 (MTF-1) binds specifically to metal response elements (MREs) and transactivates metallothionein (MT) gene expression in response to zinc and cadmium. This investigation contrasts the mechanism of mouse MT gene (mMT-I) promoter activation by cadmium and zinc in IMR-32 human neuroblastoma cells to determine whether MTF-1 binding to the MRE is necessary for activation by these metals. Cadmium activated a mMT-1 promoter (-150 base pairs) luciferase reporter 20-25-fold through a MRE-dependent mechanism. In contrast, zinc had little effect on the mMT-1 luciferase reporter. IMR-32 cells lacked MRE binding activity, and treatment with zinc in vitro or in vivo did not generate a MTF-1. MRE complex, suggesting that IMR-32 cells lack functional MTF-1. Overexpression of mMTF-1 regenerated a zinc-mediated induction of the MRE without affecting cadmium activation. Because no other transition metals tested activated the MRE, this effect appeared to be cadmium-specific. These data demonstrate that in IMR-32 human neuroblastoma cells, zinc and cadmium can use independent mechanisms for activation of the mMT-I promoter and cadmium-mediated MRE activation is independent of MTF-1 and zinc."}