The aryl hydrocarbon receptor and glucocorticoid receptor interact to activate human metallothionein 2A

Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other physiological events, crosstalk between these receptors has been the subject of much debate. Metallothioneins are classic glucocorticoid-inducible...

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Published inToxicology and applied pharmacology Vol. 273; no. 1; pp. 90 - 99
Main Authors Sato, Shoko, Shirakawa, Hitoshi, Tomita, Shuhei, Tohkin, Masahiro, Gonzalez, Frank J., Komai, Michio
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Inc 15.11.2013
Elsevier
Subjects
3-METHYLCHOLANTHRENE
60 APPLIED LIFE SCIENCES
AMINO ACIDS
ANIMAL TISSUES
Animals
Aryl hydrocarbon receptor
Biological and medical sciences
Cercopithecus aethiops
CHROMATIN
Chromatin Immunoprecipitation
COS Cells
DEXAMETHASONE
Dexamethasone - pharmacology
GENES
Glucocorticoid receptor
Hep G2 Cells
Humans
Immunoprecipitation
Medical sciences
MESSENGER-RNA
METALLOTHIONEIN
Metallothionein - genetics
Metallothionein - metabolism
Methylcholanthrene - pharmacology
Promoter Regions, Genetic
Protein Interaction Domains and Motifs - drug effects
RECEPTORS
Receptors, Aryl Hydrocarbon - agonists
Receptors, Aryl Hydrocarbon - genetics
Receptors, Aryl Hydrocarbon - metabolism
Receptors, Glucocorticoid - agonists
Receptors, Glucocorticoid - genetics
Receptors, Glucocorticoid - metabolism
Response Elements - drug effects
RNA, Messenger - genetics
RNA, Messenger - metabolism
RODENTS
Signal Transduction
Toxicology
Transcription
Transcriptional Activation
Dexamethasone
bHLH/PAS
Transcription
3-Methylcholanthrene
3-MC
MT
XRE
AHR
GR
ChIP
Aryl hydrocarbon receptor
MT2A
Dex
Glucocorticoid receptor
GRE
Metallothionein
Human
Corticosteroid
Hydrocarbon
Steroid hormone
Antiinflammatory agent
Ah receptor
3―Methylcholanthrene
Hormonal receptor
metallothionein 2A
glucocorticoid response element
chromatin immunoprecipitation
xenobiotic response element
basic helix–loop–helix/Per–Arnt–Sim
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Abstract Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other physiological events, crosstalk between these receptors has been the subject of much debate. Metallothioneins are classic glucocorticoid-inducible genes that were reported to increase upon treatment with AHR agonists in rodent tissues and cultured human cells. In this study, the mechanism of human metallothionein 2A (MT2A) gene transcription activation by AHR was investigated. Cotreatment with 3-methylcholanthrene and dexamethasone, agonists of AHR and GR respectively, synergistically increased MT2A mRNA levels in HepG2 cells. MT2A induction was suppressed by RNA interference against AHR or GR. Coimmunoprecipitation experiments revealed a physical interaction between AHR and GR proteins. Moreover, chromatin immunoprecipitation assays indicated that AHR was recruited to the glucocorticoid response element in the MT2A promoter. Thus, we provide a novel mechanism whereby AHR modulates expression of human MT2A via the glucocorticoid response element and protein–protein interactions with GR. •Aryl hydrocarbon receptor forms a complex with glucocorticoid receptor in cells.•Human metallothionein gene is regulated by the AHR and GR interaction.•AHR–GR complex binds to glucocorticoid response element in metallothionein gene.•We demonstrated a novel transcriptional mechanism via AHR and GR interaction.
AbstractList Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other physiological events, crosstalk between these receptors has been the subject of much debate. Metallothioneins are classic glucocorticoid-inducible genes that were reported to increase upon treatment with AHR agonists in rodent tissues and cultured human cells. In this study, the mechanism of human metallothionein 2A ( MT2A ) gene transcription activation by AHR was investigated. Cotreatment with 3-methylcholanthrene and dexamethasone, agonists of AHR and GR respectively, synergistically increased MT2A mRNA levels in HepG2 cells. MT2A induction was suppressed by RNA interference against AHR or GR. Coimmunoprecipitation experiments revealed a physical interaction between AHR and GR proteins. Moreover, chromatin immunoprecipitation assays indicated that AHR was recruited to the glucocorticoid response element in the MT2A promoter. Thus, we provide a novel mechanism whereby AHR modulates expression of human MT2A via the glucocorticoid response element and protein–protein interactions with GR.
Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other physiological events, crosstalk between these receptors has been the subject of much debate. Metallothioneins are classic glucocorticoid-inducible genes that were reported to increase upon treatment with AHR agonists in rodent tissues and cultured human cells. In this study, the mechanism of human metallothionein 2A (MT2A) gene transcription activation by AHR was investigated. Cotreatment with 3-methylcholanthrene and dexamethasone, agonists of AHR and GR respectively, synergistically increased MT2A mRNA levels in HepG2 cells. MT2A induction was suppressed by RNA interference against AHR or GR. Coimmunoprecipitation experiments revealed a physical interaction between AHR and GR proteins. Moreover, chromatin immunoprecipitation assays indicated that AHR was recruited to the glucocorticoid response element in the MT2A promoter. Thus, we provide a novel mechanism whereby AHR modulates expression of human MT2A via the glucocorticoid response element and protein–protein interactions with GR. - Highlights: • Aryl hydrocarbon receptor forms a complex with glucocorticoid receptor in cells. • Human metallothionein gene is regulated by the AHR and GR interaction. • AHR–GR complex binds to glucocorticoid response element in metallothionein gene. • We demonstrated a novel transcriptional mechanism via AHR and GR interaction.
Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other physiological events, crosstalk between these receptors has been the subject of much debate. Metallothioneins are classic glucocorticoid-inducible genes that were reported to increase upon treatment with AHR agonists in rodent tissues and cultured human cells. In this study, the mechanism of human metallothionein 2A (MT2A) gene transcription activation by AHR was investigated. Cotreatment with 3-methylcholanthrene and dexamethasone, agonists of AHR and GR respectively, synergistically increased MT2A mRNA levels in HepG2 cells. MT2A induction was suppressed by RNA interference against AHR or GR. Coimmunoprecipitation experiments revealed a physical interaction between AHR and GR proteins. Moreover, chromatin immunoprecipitation assays indicated that AHR was recruited to the glucocorticoid response element in the MT2A promoter. Thus, we provide a novel mechanism whereby AHR modulates expression of human MT2A via the glucocorticoid response element and protein-protein interactions with GR.
Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other physiological events, crosstalk between these receptors has been the subject of much debate. Metallothioneins are classic glucocorticoid-inducible genes that were reported to increase upon treatment with AHR agonists in rodent tissues and cultured human cells. In this study, the mechanism of human metallothionein 2A (MT2A) gene transcription activation by AHR was investigated. Cotreatment with 3-methylcholanthrene and dexamethasone, agonists of AHR and GR respectively, synergistically increased MT2A mRNA levels in HepG2 cells. MT2A induction was suppressed by RNA interference against AHR or GR. Coimmunoprecipitation experiments revealed a physical interaction between AHR and GR proteins. Moreover, chromatin immunoprecipitation assays indicated that AHR was recruited to the glucocorticoid response element in the MT2A promoter. Thus, we provide a novel mechanism whereby AHR modulates expression of human MT2A via the glucocorticoid response element and protein–protein interactions with GR. •Aryl hydrocarbon receptor forms a complex with glucocorticoid receptor in cells.•Human metallothionein gene is regulated by the AHR and GR interaction.•AHR–GR complex binds to glucocorticoid response element in metallothionein gene.•We demonstrated a novel transcriptional mechanism via AHR and GR interaction.
Author Komai, Michio
Gonzalez, Frank J.
Shirakawa, Hitoshi
Tomita, Shuhei
Sato, Shoko
Tohkin, Masahiro
AuthorAffiliation a Laboratory of Nutrition, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan
d Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
c Department of Medical Safety Science, Graduate School of Pharmaceutical Science, Nagoya City University, Nagoya 267-8603, Japan
b Division of Molecular Pharmacology, Department of Pathophysiological and Therapeutic Science, Yonago 683-8503, Japan
AuthorAffiliation_xml – name: a Laboratory of Nutrition, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan
– name: d Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA
– name: b Division of Molecular Pharmacology, Department of Pathophysiological and Therapeutic Science, Yonago 683-8503, Japan
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  surname: Sato
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  givenname: Masahiro
  surname: Tohkin
  fullname: Tohkin, Masahiro
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  givenname: Frank J.
  surname: Gonzalez
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  givenname: Michio
  surname: Komai
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  email: mkomai@m.tohoku.ac.jp
  organization: Laboratory of Nutrition, Graduate School of Agricultural Science, Tohoku University, Sendai 981-8555, Japan
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Issue 1
Keywords Dexamethasone
bHLH/PAS
Transcription
3-Methylcholanthrene
3-MC
MT
XRE
AHR
GR
ChIP
Aryl hydrocarbon receptor
MT2A
Dex
Glucocorticoid receptor
GRE
Metallothionein
Human
Corticosteroid
Hydrocarbon
Steroid hormone
Antiinflammatory agent
Ah receptor
3―Methylcholanthrene
Hormonal receptor
metallothionein 2A
glucocorticoid response element
chromatin immunoprecipitation
xenobiotic response element
basic helix–loop–helix/Per–Arnt–Sim
Language English
License CC BY 4.0
2013.
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PMID 23994556
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PublicationDate 2013-11-15
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PublicationTitle Toxicology and applied pharmacology
PublicationTitleAlternate Toxicol Appl Pharmacol
PublicationYear 2013
Publisher Elsevier Inc
Elsevier
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Snippet Although the aryl hydrocarbon receptor (AHR) and glucocorticoid receptor (GR) play essential roles in mammalian development, stress responses, and other...
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SubjectTerms 3-METHYLCHOLANTHRENE
60 APPLIED LIFE SCIENCES
AMINO ACIDS
ANIMAL TISSUES
Animals
Aryl hydrocarbon receptor
Biological and medical sciences
Cercopithecus aethiops
CHROMATIN
Chromatin Immunoprecipitation
COS Cells
DEXAMETHASONE
Dexamethasone - pharmacology
GENES
Glucocorticoid receptor
Hep G2 Cells
Humans
Immunoprecipitation
Medical sciences
MESSENGER-RNA
METALLOTHIONEIN
Metallothionein - genetics
Metallothionein - metabolism
Methylcholanthrene - pharmacology
Promoter Regions, Genetic
Protein Interaction Domains and Motifs - drug effects
RECEPTORS
Receptors, Aryl Hydrocarbon - agonists
Receptors, Aryl Hydrocarbon - genetics
Receptors, Aryl Hydrocarbon - metabolism
Receptors, Glucocorticoid - agonists
Receptors, Glucocorticoid - genetics
Receptors, Glucocorticoid - metabolism
Response Elements - drug effects
RNA, Messenger - genetics
RNA, Messenger - metabolism
RODENTS
Signal Transduction
Toxicology
Transcription
Transcriptional Activation
Title The aryl hydrocarbon receptor and glucocorticoid receptor interact to activate human metallothionein 2A
URI https://dx.doi.org/10.1016/j.taap.2013.08.017
https://www.ncbi.nlm.nih.gov/pubmed/23994556
https://www.osti.gov/biblio/22285491
https://pubmed.ncbi.nlm.nih.gov/PMC6301017
Volume 273
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