Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells.
Identifieur interne : 002359 ( PubMed/Corpus ); précédent : 002358; suivant : 002360Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells.
Auteurs : P. Thomas ; Y. Pang ; E J Filardo ; J. DongSource :
- Endocrinology [ 0013-7227 ] ; 2005.
English descriptors
- KwdEn :
- Adenylyl Cyclases (metabolism), Breast Neoplasms, Cell Line, Tumor, Cell Membrane (metabolism), Estrogens (metabolism), Estrogens (pharmacology), GTP-Binding Protein alpha Subunits, Gs (metabolism), Humans, Kidney (cytology), Membrane Proteins (metabolism), Receptors, Estrogen (metabolism), Receptors, G-Protein-Coupled (genetics), Receptors, G-Protein-Coupled (metabolism), Signal Transduction (physiology), Sulfur Radioisotopes, Transfection.
- MESH :
- chemical , genetics : Receptors, G-Protein-Coupled.
- chemical , metabolism : Adenylyl Cyclases, Estrogens, GTP-Binding Protein alpha Subunits, Gs, Membrane Proteins, Receptors, Estrogen, Receptors, G-Protein-Coupled.
- cytology : Kidney.
- metabolism : Cell Membrane.
- chemical , pharmacology : Estrogens.
- physiology : Signal Transduction.
- Breast Neoplasms, Cell Line, Tumor, Humans, Sulfur Radioisotopes, Transfection.
Abstract
Although nonclassical estrogen actions initiated at the cell surface have been described in many tissues, the identities of the membrane estrogen receptors (mERs) mediating these actions remain unclear. Here we show that GPR30, an orphan receptor unrelated to nuclear estrogen receptors, has all the binding and signaling characteristics of a mER. A high-affinity (dissociation constant 2.7 nm), limited capacity, displaceable, single binding site specific for estrogens was detected in plasma membranes of SKBR3 breast cancer cells that express GPR30 but lack nuclear estrogen receptors. Progesterone-induced increases and small interfering RNA-induced decreases in GPR30 expression in SKBR3 cells were accompanied by parallel changes in specific estradiol-17beta (E2) binding. Plasma membranes of human embryonic kidney 293 cells transfected with GPR30, but not those of untransfected cells, and human placental tissues that express GPR30 also displayed high-affinity, specific estrogen binding typical of mERs. E2 treatment of transfected cell membranes caused activation of a stimulatory G protein that is directly coupled to the receptor, indicating GPR30 is a G protein-coupled receptor (GPCR), and also increased adenylyl cyclase activity. The finding that the antiestrogens tamoxifen and ICI 182,780, and an environmental estrogen, ortho,para-dichlorodiphenyldichloroethylene (o,p'-DDE), have high binding affinities to the receptor and mimic the actions of E2 has important implications for both the development and treatment of estrogen-dependent breast cancer. GPR30 is structurally unrelated to the recently discovered family of GPCR-like membrane progestin receptors. The identification of a second distinct class of GPCR-like steroid membrane receptors suggests a widespread role for GPCRs in nonclassical steroid hormone actions.
DOI: 10.1210/en.2004-1064
PubMed: 15539556
Links to Exploration step
pubmed:15539556Le document en format XML
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Dong</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:15539556</idno><idno type="pmid">15539556</idno><idno type="doi">10.1210/en.2004-1064</idno><idno type="wicri:Area/PubMed/Corpus">002359</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002359</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells.</title><author><name sortKey="Thomas, P" sort="Thomas, P" uniqKey="Thomas P" first="P" last="Thomas">P. Thomas</name><affiliation><nlm:affiliation>University of Texas Marine Science Institute, 750 Channel View Drive, Port Aransas, Texas 78373, USA. thomas@utmsi.utexas.edu</nlm:affiliation></affiliation></author><author><name sortKey="Pang, Y" sort="Pang, Y" uniqKey="Pang Y" first="Y" last="Pang">Y. Pang</name></author><author><name sortKey="Filardo, E J" sort="Filardo, E J" uniqKey="Filardo E" first="E J" last="Filardo">E J Filardo</name></author><author><name sortKey="Dong, J" sort="Dong, J" uniqKey="Dong J" first="J" last="Dong">J. Dong</name></author></analytic><series><title level="j">Endocrinology</title><idno type="ISSN">0013-7227</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenylyl Cyclases (metabolism)</term><term>Breast Neoplasms</term><term>Cell Line, Tumor</term><term>Cell Membrane (metabolism)</term><term>Estrogens (metabolism)</term><term>Estrogens (pharmacology)</term><term>GTP-Binding Protein alpha Subunits, Gs (metabolism)</term><term>Humans</term><term>Kidney (cytology)</term><term>Membrane Proteins (metabolism)</term><term>Receptors, Estrogen (metabolism)</term><term>Receptors, G-Protein-Coupled (genetics)</term><term>Receptors, G-Protein-Coupled (metabolism)</term><term>Signal Transduction (physiology)</term><term>Sulfur Radioisotopes</term><term>Transfection</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Receptors, G-Protein-Coupled</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenylyl Cyclases</term><term>Estrogens</term><term>GTP-Binding Protein alpha Subunits, Gs</term><term>Membrane Proteins</term><term>Receptors, Estrogen</term><term>Receptors, G-Protein-Coupled</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Kidney</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Estrogens</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Breast Neoplasms</term><term>Cell Line, Tumor</term><term>Humans</term><term>Sulfur Radioisotopes</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Although nonclassical estrogen actions initiated at the cell surface have been described in many tissues, the identities of the membrane estrogen receptors (mERs) mediating these actions remain unclear. Here we show that GPR30, an orphan receptor unrelated to nuclear estrogen receptors, has all the binding and signaling characteristics of a mER. A high-affinity (dissociation constant 2.7 nm), limited capacity, displaceable, single binding site specific for estrogens was detected in plasma membranes of SKBR3 breast cancer cells that express GPR30 but lack nuclear estrogen receptors. Progesterone-induced increases and small interfering RNA-induced decreases in GPR30 expression in SKBR3 cells were accompanied by parallel changes in specific estradiol-17beta (E2) binding. Plasma membranes of human embryonic kidney 293 cells transfected with GPR30, but not those of untransfected cells, and human placental tissues that express GPR30 also displayed high-affinity, specific estrogen binding typical of mERs. E2 treatment of transfected cell membranes caused activation of a stimulatory G protein that is directly coupled to the receptor, indicating GPR30 is a G protein-coupled receptor (GPCR), and also increased adenylyl cyclase activity. The finding that the antiestrogens tamoxifen and ICI 182,780, and an environmental estrogen, ortho,para-dichlorodiphenyldichloroethylene (o,p'-DDE), have high binding affinities to the receptor and mimic the actions of E2 has important implications for both the development and treatment of estrogen-dependent breast cancer. GPR30 is structurally unrelated to the recently discovered family of GPCR-like membrane progestin receptors. The identification of a second distinct class of GPCR-like steroid membrane receptors suggests a widespread role for GPCRs in nonclassical steroid hormone actions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15539556</PMID><DateCompleted><Year>2005</Year><Month>02</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0013-7227</ISSN><JournalIssue CitedMedium="Print"><Volume>146</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Endocrinology</Title><ISOAbbreviation>Endocrinology</ISOAbbreviation></Journal><ArticleTitle>Identity of an estrogen membrane receptor coupled to a G protein in human breast cancer cells.</ArticleTitle><Pagination><MedlinePgn>624-32</MedlinePgn></Pagination><Abstract><AbstractText>Although nonclassical estrogen actions initiated at the cell surface have been described in many tissues, the identities of the membrane estrogen receptors (mERs) mediating these actions remain unclear. Here we show that GPR30, an orphan receptor unrelated to nuclear estrogen receptors, has all the binding and signaling characteristics of a mER. A high-affinity (dissociation constant 2.7 nm), limited capacity, displaceable, single binding site specific for estrogens was detected in plasma membranes of SKBR3 breast cancer cells that express GPR30 but lack nuclear estrogen receptors. Progesterone-induced increases and small interfering RNA-induced decreases in GPR30 expression in SKBR3 cells were accompanied by parallel changes in specific estradiol-17beta (E2) binding. Plasma membranes of human embryonic kidney 293 cells transfected with GPR30, but not those of untransfected cells, and human placental tissues that express GPR30 also displayed high-affinity, specific estrogen binding typical of mERs. E2 treatment of transfected cell membranes caused activation of a stimulatory G protein that is directly coupled to the receptor, indicating GPR30 is a G protein-coupled receptor (GPCR), and also increased adenylyl cyclase activity. The finding that the antiestrogens tamoxifen and ICI 182,780, and an environmental estrogen, ortho,para-dichlorodiphenyldichloroethylene (o,p'-DDE), have high binding affinities to the receptor and mimic the actions of E2 has important implications for both the development and treatment of estrogen-dependent breast cancer. GPR30 is structurally unrelated to the recently discovered family of GPCR-like membrane progestin receptors. The identification of a second distinct class of GPCR-like steroid membrane receptors suggests a widespread role for GPCRs in nonclassical steroid hormone actions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Thomas</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>University of Texas Marine Science Institute, 750 Channel View Drive, Port Aransas, Texas 78373, USA. thomas@utmsi.utexas.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pang</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Filardo</LastName><ForeName>E J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Dong</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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