Inhibition of the human thioredoxin system. A molecular mechanism of mercury toxicity.
Identifieur interne : 000C00 ( Main/Exploration ); précédent : 000B99; suivant : 000C01Inhibition of the human thioredoxin system. A molecular mechanism of mercury toxicity.
Auteurs : Cristina M L. Carvalho [Portugal] ; Eng-Hui Chew ; Seyed Isaac Hashemy ; Jun Lu ; Arne HolmgrenSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules HeLa (MeSH), Composés du mercure (toxicité), Cystéine (métabolisme), Glutarédoxines (métabolisme), Glutathione reductase (métabolisme), Humains (MeSH), Mercure (toxicité), Prolifération cellulaire (effets des médicaments et des substances chimiques), Rats (MeSH), Spectrométrie de masse ESI (MeSH), Survie cellulaire (effets des médicaments et des substances chimiques), Thiols (métabolisme), Thioredoxin reductase 1 (antagonistes et inhibiteurs), Thiorédoxines (antagonistes et inhibiteurs), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Thioredoxin reductase 1, Thiorédoxines.
- composition chimique : Thiorédoxines.
- effets des médicaments et des substances chimiques : Prolifération cellulaire, Survie cellulaire.
- métabolisme : Cystéine, Glutarédoxines, Glutathione reductase, Thiols, Thiorédoxines.
- toxicité : Composés du mercure, Mercure.
- Animaux, Cellules HeLa, Humains, Rats, Spectrométrie de masse ESI.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Proliferation (drug effects), Cell Survival (drug effects), Cysteine (metabolism), Glutaredoxins (metabolism), Glutathione Reductase (metabolism), HeLa Cells (MeSH), Humans (MeSH), Mercury (toxicity), Mercury Compounds (toxicity), Rats (MeSH), Spectrometry, Mass, Electrospray Ionization (MeSH), Sulfhydryl Compounds (metabolism), Thioredoxin Reductase 1 (antagonists & inhibitors), Thioredoxins (antagonists & inhibitors), Thioredoxins (chemistry), Thioredoxins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Thioredoxin Reductase 1, Thioredoxins.
- chemical , chemistry : Thioredoxins.
- chemical , metabolism : Cysteine, Glutaredoxins, Glutathione Reductase, Sulfhydryl Compounds, Thioredoxins.
- drug effects : Cell Proliferation, Cell Survival.
- chemical , toxicity : Mercury, Mercury Compounds.
- Animals, HeLa Cells, Humans, Rats, Spectrometry, Mass, Electrospray Ionization.
Abstract
Mercury toxicity mediated by different forms of mercury is a major health problem; however, the molecular mechanisms underlying toxicity remain elusive. We analyzed the effects of mercuric chloride (HgCl(2)) and monomethylmercury (MeHg) on the proteins of the mammalian thioredoxin system, thioredoxin reductase (TrxR) and thioredoxin (Trx), and of the glutaredoxin system, glutathione reductase (GR) and glutaredoxin (Grx). HgCl(2) and MeHg inhibited recombinant rat TrxR with IC(50) values of 7.2 and 19.7 nm, respectively. Fully reduced human Trx1 bound mercury and lost all five free thiols and activity after incubation with HgCl(2) or MeHg, but only HgCl(2) generated dimers. Mass spectra analysis demonstrated binding of 2.5 mol of Hg(2+) and 5 mol of MeHg(+)/mol of Trx1 with the very strong Hg(2+) complexes involving active site and structural disulfides. Inhibition of both TrxR and Trx activity was observed in HeLa and HEK 293 cells treated with HgCl(2) or MeHg. GR was inhibited by HgCl(2) and MeHg in vitro, but no decrease in GR activity was detected in cell extracts treated with mercurials. Human Grx1 showed similar reactivity as Trx1 with both mercurial compounds, with the loss of all free thiols and Grx dimerization in the presence of HgCl(2), but no inhibition of Grx activity was observed in lysates of HeLa cells exposed to mercury. Overall, mercury inhibition was selective toward the thioredoxin system. In particular, the remarkable potency of the mercury compounds to bind to the selenol-thiol in the active site of TrxR should be a major molecular mechanism of mercury toxicity.
DOI: 10.1074/jbc.M710133200
PubMed: 18321861
Affiliations:
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A molecular mechanism of mercury toxicity.</title><author><name sortKey="Carvalho, Cristina M L" sort="Carvalho, Cristina M L" uniqKey="Carvalho C" first="Cristina M L" last="Carvalho">Cristina M L. Carvalho</name><affiliation wicri:level="1"><nlm:affiliation>I-Med, Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, Portugal.</nlm:affiliation><country xml:lang="fr">Portugal</country><wicri:regionArea>I-Med, Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon</wicri:regionArea><wicri:noRegion>1649-003 Lisbon</wicri:noRegion></affiliation></author><author><name sortKey="Chew, Eng Hui" sort="Chew, Eng Hui" uniqKey="Chew E" first="Eng-Hui" last="Chew">Eng-Hui Chew</name></author><author><name sortKey="Hashemy, Seyed Isaac" sort="Hashemy, Seyed Isaac" uniqKey="Hashemy S" first="Seyed Isaac" last="Hashemy">Seyed Isaac Hashemy</name></author><author><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cell Proliferation (drug effects)</term><term>Cell Survival (drug effects)</term><term>Cysteine (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione Reductase (metabolism)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Mercury (toxicity)</term><term>Mercury Compounds (toxicity)</term><term>Rats (MeSH)</term><term>Spectrometry, Mass, Electrospray Ionization (MeSH)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Thioredoxin Reductase 1 (antagonists & inhibitors)</term><term>Thioredoxins (antagonists & inhibitors)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules HeLa (MeSH)</term><term>Composés du mercure (toxicité)</term><term>Cystéine (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathione reductase (métabolisme)</term><term>Humains (MeSH)</term><term>Mercure (toxicité)</term><term>Prolifération cellulaire (effets des médicaments et des substances chimiques)</term><term>Rats (MeSH)</term><term>Spectrométrie de masse ESI (MeSH)</term><term>Survie cellulaire (effets des médicaments et des substances chimiques)</term><term>Thiols (métabolisme)</term><term>Thioredoxin reductase 1 (antagonistes et inhibiteurs)</term><term>Thiorédoxines (antagonistes et inhibiteurs)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Thioredoxin Reductase 1</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Glutaredoxins</term><term>Glutathione Reductase</term><term>Sulfhydryl Compounds</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Thioredoxin reductase 1</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Proliferation</term><term>Cell Survival</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Prolifération cellulaire</term><term>Survie cellulaire</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term><term>Glutarédoxines</term><term>Glutathione reductase</term><term>Thiols</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Mercury</term><term>Mercury Compounds</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Composés du mercure</term><term>Mercure</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>HeLa Cells</term><term>Humans</term><term>Rats</term><term>Spectrometry, Mass, Electrospray Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Humains</term><term>Rats</term><term>Spectrométrie de masse ESI</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mercury toxicity mediated by different forms of mercury is a major health problem; however, the molecular mechanisms underlying toxicity remain elusive. We analyzed the effects of mercuric chloride (HgCl(2)) and monomethylmercury (MeHg) on the proteins of the mammalian thioredoxin system, thioredoxin reductase (TrxR) and thioredoxin (Trx), and of the glutaredoxin system, glutathione reductase (GR) and glutaredoxin (Grx). HgCl(2) and MeHg inhibited recombinant rat TrxR with IC(50) values of 7.2 and 19.7 nm, respectively. Fully reduced human Trx1 bound mercury and lost all five free thiols and activity after incubation with HgCl(2) or MeHg, but only HgCl(2) generated dimers. Mass spectra analysis demonstrated binding of 2.5 mol of Hg(2+) and 5 mol of MeHg(+)/mol of Trx1 with the very strong Hg(2+) complexes involving active site and structural disulfides. Inhibition of both TrxR and Trx activity was observed in HeLa and HEK 293 cells treated with HgCl(2) or MeHg. GR was inhibited by HgCl(2) and MeHg in vitro, but no decrease in GR activity was detected in cell extracts treated with mercurials. Human Grx1 showed similar reactivity as Trx1 with both mercurial compounds, with the loss of all free thiols and Grx dimerization in the presence of HgCl(2), but no inhibition of Grx activity was observed in lysates of HeLa cells exposed to mercury. Overall, mercury inhibition was selective toward the thioredoxin system. In particular, the remarkable potency of the mercury compounds to bind to the selenol-thiol in the active site of TrxR should be a major molecular mechanism of mercury toxicity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18321861</PMID><DateCompleted><Year>2008</Year><Month>06</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>18</Issue><PubDate><Year>2008</Year><Month>May</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Inhibition of the human thioredoxin system. A molecular mechanism of mercury toxicity.</ArticleTitle><Pagination><MedlinePgn>11913-23</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M710133200</ELocationID><Abstract><AbstractText>Mercury toxicity mediated by different forms of mercury is a major health problem; however, the molecular mechanisms underlying toxicity remain elusive. We analyzed the effects of mercuric chloride (HgCl(2)) and monomethylmercury (MeHg) on the proteins of the mammalian thioredoxin system, thioredoxin reductase (TrxR) and thioredoxin (Trx), and of the glutaredoxin system, glutathione reductase (GR) and glutaredoxin (Grx). HgCl(2) and MeHg inhibited recombinant rat TrxR with IC(50) values of 7.2 and 19.7 nm, respectively. Fully reduced human Trx1 bound mercury and lost all five free thiols and activity after incubation with HgCl(2) or MeHg, but only HgCl(2) generated dimers. Mass spectra analysis demonstrated binding of 2.5 mol of Hg(2+) and 5 mol of MeHg(+)/mol of Trx1 with the very strong Hg(2+) complexes involving active site and structural disulfides. Inhibition of both TrxR and Trx activity was observed in HeLa and HEK 293 cells treated with HgCl(2) or MeHg. GR was inhibited by HgCl(2) and MeHg in vitro, but no decrease in GR activity was detected in cell extracts treated with mercurials. Human Grx1 showed similar reactivity as Trx1 with both mercurial compounds, with the loss of all free thiols and Grx dimerization in the presence of HgCl(2), but no inhibition of Grx activity was observed in lysates of HeLa cells exposed to mercury. Overall, mercury inhibition was selective toward the thioredoxin system. In particular, the remarkable potency of the mercury compounds to bind to the selenol-thiol in the active site of TrxR should be a major molecular mechanism of mercury toxicity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Carvalho</LastName><ForeName>Cristina M L</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>I-Med, Faculty of Pharmacy, University of Lisbon, Av. 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rat</NameOfSubstance></Chemical><Chemical><RegistryNumber>FXS1BY2PGL</RegistryNumber><NameOfSubstance UI="D008628">Mercury</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049109" MajorTopicYN="N">Cell Proliferation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002470" MajorTopicYN="N">Cell Survival</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054481" MajorTopicYN="N">Thioredoxin Reductase 1</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>3</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>6</Month><Day>20</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>3</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18321861</ArticleId><ArticleId IdType="pii">M710133200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M710133200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Portugal</li></country></list><tree><noCountry><name sortKey="Chew, Eng Hui" sort="Chew, Eng Hui" uniqKey="Chew E" first="Eng-Hui" last="Chew">Eng-Hui Chew</name><name sortKey="Hashemy, Seyed Isaac" sort="Hashemy, Seyed Isaac" uniqKey="Hashemy S" first="Seyed Isaac" last="Hashemy">Seyed Isaac Hashemy</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name></noCountry><country name="Portugal"><noRegion><name sortKey="Carvalho, Cristina M L" sort="Carvalho, Cristina M L" uniqKey="Carvalho C" first="Cristina M L" last="Carvalho">Cristina M L. 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