Oxidant stress impaired DNA-binding of estrogen receptor from human breast cancer
Identifieur interne : 003B36 ( Main/Exploration ); précédent : 003B35; suivant : 003B37Oxidant stress impaired DNA-binding of estrogen receptor from human breast cancer
Auteurs : Xiaoshan Liang [États-Unis] ; Biao Lu [États-Unis] ; Gary K. Scott [États-Unis] ; Chuan-Hsiung Chang [États-Unis] ; Michael A. Baldwin [États-Unis] ; Christopher C. Benz [États-Unis]Source :
- Molecular and Cellular Endocrinology [ 0303-7207 ] ; 1998.
English descriptors
- KwdEn :
- Teeft :
- Abbott labs, Acetylation products, Alkylator, Amino acids, Assay, Benz, Breast cancer, Breast tumor extracts, Breast tumors, Cell lines, Cellular, Cellular endocrinology, Chloramphenicol acetyltransferase, Choer, Choer cells, Circular dichroism, Circular dichroism spectrometry, Cognate estrogen response element, Complete denaturation, Complete loss, Complex formation, Culture treatment, Defect, Diamide, Dnabinding, Dnabinding capacity, Elsevier science ireland, Emsa, Emsa analysis, Endocrinology, Estradiol binding, Estrogen, Estrogen receptor, Extracellular, Extracellular oxidant stress, Extracellular redox stress, Extract, Free radic, Fresh serum, Full restoration, Human breast tumors, Immunoreactive, Immunoreactive estrogen receptor, Intracellular, Iodoacetamide, Iodosobenzoate, Liang, Menadione, Monoclonal antibody, Oxidant, Oxidant stress, Oxidant treatment, Oxidative, Oxidative stress, Partial reversibility, Peak induction, Previous studies, Primary antibody, Primary breast tumors, Reagent, Receptor, Recombinant, Redox, Reversible defect, Room temperature, Sample loading buffer, Secondary structure, Solution structure, Strong thiol, Thiol, Thiol alkylation, Thiol reduction, Transactivating functions, Transcription factors, Transcriptional, Transcriptional activators, Transcriptional activity, Transient transfection, Treatment conditions, Tumor microvessels, Tumor samples, Untreated, Western blot detection, Western blots.
Abstract
Abstract: Full-length (67 kDa) immunoreactive estrogen receptor (ER) extracted from a third of untreated ER-positive primary breast tumors appears unable to bind to its cognate estrogen response element (ERE). We have observed partial reversibility of this ER DNA-binding defect upon treatment of these tumor extracts with excess thiol reducing agent (DTT), suggesting that ER DNA-binding is subject to redox modulation as is reported for other zinc-finger proteins and transcriptional activators. Treatment of recombinant ER DNA-binding domain (ER-DBD) or ER-enriched extracts from CHOER and MCF-7 cells with thiol-reacting oxidants (diamide, iodosobenzoate, H2O2) or alkylator (iodoacetamide) produces a dose-dependent loss in ER DNA-binding capacity. Thiol-specific oxidative loss in ER DNA-binding is fully reversible by DTT reduction, unlike the defect caused by thiol-specific alkylation. Circular dichroism spectrometry shows that both forms of treatment substantially modify ER secondary structure, inducing loss of α-helical content within the ER-DBD that is reversible after thiol oxidation but not after thiol alkylation. Oxidant (H2O2, menadione) exposure of cultured CHOER or MCF-7 cells impairs the ability of endogenous ER to bind DNA and transactivate an ER-responsive reporter gene (ERE-tk-CAT), demonstrating that extracellular redox stress can modulate intracellular ER function. Since these thiol-specific oxidant and alkylator treatments have no significant effect on either recombinant ER ligand-binding or intracellular immunoreactive ER content, our findings suggest that DNA-binding and transactivation are the most sensitive intracellular ER functions impaired by oxidant stress in some ER-positive human breast tumors.
Url:
DOI: 10.1016/S0303-7207(98)00161-0
Affiliations:
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Le document en format XML
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<term>Acetylation products</term>
<term>Alkylator</term>
<term>Amino acids</term>
<term>Assay</term>
<term>Benz</term>
<term>Breast cancer</term>
<term>Breast tumor extracts</term>
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<term>Cellular</term>
<term>Cellular endocrinology</term>
<term>Chloramphenicol acetyltransferase</term>
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<term>Circular dichroism spectrometry</term>
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<term>Complex formation</term>
<term>Culture treatment</term>
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<term>Estrogen</term>
<term>Estrogen receptor</term>
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<term>Extracellular redox stress</term>
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<term>Immunoreactive estrogen receptor</term>
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<term>Iodosobenzoate</term>
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<term>Transcriptional activators</term>
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<front><div type="abstract" xml:lang="en">Abstract: Full-length (67 kDa) immunoreactive estrogen receptor (ER) extracted from a third of untreated ER-positive primary breast tumors appears unable to bind to its cognate estrogen response element (ERE). We have observed partial reversibility of this ER DNA-binding defect upon treatment of these tumor extracts with excess thiol reducing agent (DTT), suggesting that ER DNA-binding is subject to redox modulation as is reported for other zinc-finger proteins and transcriptional activators. Treatment of recombinant ER DNA-binding domain (ER-DBD) or ER-enriched extracts from CHOER and MCF-7 cells with thiol-reacting oxidants (diamide, iodosobenzoate, H2O2) or alkylator (iodoacetamide) produces a dose-dependent loss in ER DNA-binding capacity. Thiol-specific oxidative loss in ER DNA-binding is fully reversible by DTT reduction, unlike the defect caused by thiol-specific alkylation. Circular dichroism spectrometry shows that both forms of treatment substantially modify ER secondary structure, inducing loss of α-helical content within the ER-DBD that is reversible after thiol oxidation but not after thiol alkylation. Oxidant (H2O2, menadione) exposure of cultured CHOER or MCF-7 cells impairs the ability of endogenous ER to bind DNA and transactivate an ER-responsive reporter gene (ERE-tk-CAT), demonstrating that extracellular redox stress can modulate intracellular ER function. Since these thiol-specific oxidant and alkylator treatments have no significant effect on either recombinant ER ligand-binding or intracellular immunoreactive ER content, our findings suggest that DNA-binding and transactivation are the most sensitive intracellular ER functions impaired by oxidant stress in some ER-positive human breast tumors.</div>
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