Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1.
Identifieur interne : 000C01 ( Main/Exploration ); précédent : 000C00; suivant : 000C02Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1.
Auteurs : Pascal Dammeyer [Suède] ; Anastasios E. Damdimopoulos ; Tomas Nordman ; Alberto Jiménez ; Antonio Miranda-Vizuete ; Elias S J. ArnérSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Actines (métabolisme), Amorces ADN (génétique), Cellules HeLa (MeSH), Glutarédoxines (composition chimique), Humains (MeSH), Lignée cellulaire (MeSH), Lignée cellulaire tumorale (MeSH), Membrane cellulaire (enzymologie), Membrane cellulaire (métabolisme), Membrane cellulaire (ultrastructure), Mâle (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Structure tertiaire des protéines (MeSH), Séquence nucléotidique (MeSH), Testicule (enzymologie), Testicule (ultrastructure), Thioredoxin reductase 1 (composition chimique), Thioredoxin reductase 1 (génétique), Thioredoxin reductase 1 (physiologie), Transfection (MeSH), Tubuline (métabolisme), Épissage alternatif (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Protéines recombinantes, Thioredoxin reductase 1.
- enzymologie : Membrane cellulaire, Testicule.
- génétique : Amorces ADN, Protéines recombinantes, Thioredoxin reductase 1.
- métabolisme : Actines, Membrane cellulaire, Protéines recombinantes, Tubuline.
- physiologie : Thioredoxin reductase 1.
- ultrastructure : Cellules HeLa, Humains, Lignée cellulaire, Lignée cellulaire tumorale, Membrane cellulaire, Mâle, Structure tertiaire des protéines, Séquence nucléotidique, Testicule, Transfection, Épissage alternatif.
English descriptors
- KwdEn :
- Actins (metabolism), Alternative Splicing (MeSH), Base Sequence (MeSH), Cell Line (MeSH), Cell Line, Tumor (MeSH), Cell Membrane (enzymology), Cell Membrane (metabolism), Cell Membrane (ultrastructure), DNA Primers (genetics), Glutaredoxins (chemistry), HeLa Cells (MeSH), Humans (MeSH), Male (MeSH), Protein Structure, Tertiary (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Testis (enzymology), Testis (ultrastructure), Thioredoxin Reductase 1 (chemistry), Thioredoxin Reductase 1 (genetics), Thioredoxin Reductase 1 (physiology), Transfection (MeSH), Tubulin (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Recombinant Proteins, Thioredoxin Reductase 1.
- chemical , genetics : DNA Primers, Recombinant Proteins, Thioredoxin Reductase 1.
- chemical , metabolism : Actins, Recombinant Proteins, Tubulin.
- enzymology : Cell Membrane, Testis.
- metabolism : Cell Membrane.
- chemical , physiology : Thioredoxin Reductase 1.
- ultrastructure : Cell Membrane, Testis.
- Alternative Splicing, Base Sequence, Cell Line, Cell Line, Tumor, HeLa Cells, Humans, Male, Protein Structure, Tertiary, Transfection.
Abstract
The human thioredoxin system has a wide range of functions in cells including regulation of cell proliferation and differentiation, immune system modulation, antioxidant defense, redox control of transcription factor activity, and promotion of cancer development. A key component of this enzymatic system is the selenoprotein thioredoxin reductase 1 (TrxR1), encoded by the TXNRD1 gene. Transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. Here we have studied the TXNRD1_v3 isoform containing an atypical N-terminal glutaredoxin (Grx) domain. Expression of the transcript of this isoform was found predominantly in testis but was also detected in ovary, spleen, heart, liver, kidney, and pancreas. By immunohistochemical analysis in human testis with antibodies specific for the Grx domain of TXNRD1_v3, the protein was found to be predominantly expressed in the Leydig cells. Expression of the TXNRD1_v3 transcript was also found in several cancer cell lines (HCC1937, H23, A549, U1810, or H157), and in HeLa cells, it was induced by estradiol or testosterone treatments. Surprisingly, green fluorescent protein fusions with the complete TXNRD1_v3 protein or with only its Grx domain localized to distinct cellular sites in proximity to actin, and furthermore, had a potent capacity to rapidly induce cell membrane protrusions. Analyses of these structures suggested that the Grx domain of TXNRD1_v3 localizes first in the emerging protrusion and is then followed into the protrusions by actin and subsequently by tubulin. The results presented thus reveal that TXNRD1_v3 has a unique and distinct expression pattern in human cells and suggest that the protein can guide actin polymerization in relation to cell membrane restructuring.
DOI: 10.1074/jbc.M708939200
PubMed: 18042542
Affiliations:
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Arnér</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>Actins (metabolism)</term><term>Alternative Splicing (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cell Line (MeSH)</term><term>Cell Line, Tumor (MeSH)</term><term>Cell Membrane (enzymology)</term><term>Cell Membrane (metabolism)</term><term>Cell Membrane (ultrastructure)</term><term>DNA Primers (genetics)</term><term>Glutaredoxins (chemistry)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Male (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Testis (enzymology)</term><term>Testis (ultrastructure)</term><term>Thioredoxin Reductase 1 (chemistry)</term><term>Thioredoxin Reductase 1 (genetics)</term><term>Thioredoxin Reductase 1 (physiology)</term><term>Transfection (MeSH)</term><term>Tubulin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Actines (métabolisme)</term><term>Amorces ADN (génétique)</term><term>Cellules HeLa (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Humains (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Lignée cellulaire tumorale (MeSH)</term><term>Membrane cellulaire (enzymologie)</term><term>Membrane cellulaire (métabolisme)</term><term>Membrane cellulaire (ultrastructure)</term><term>Mâle (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Testicule (enzymologie)</term><term>Testicule (ultrastructure)</term><term>Thioredoxin reductase 1 (composition chimique)</term><term>Thioredoxin reductase 1 (génétique)</term><term>Thioredoxin reductase 1 (physiologie)</term><term>Transfection (MeSH)</term><term>Tubuline (métabolisme)</term><term>Épissage alternatif (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Recombinant Proteins</term><term>Thioredoxin Reductase 1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term><term>Recombinant Proteins</term><term>Thioredoxin Reductase 1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actins</term><term>Recombinant Proteins</term><term>Tubulin</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines recombinantes</term><term>Thioredoxin reductase 1</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Membrane cellulaire</term><term>Testicule</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Membrane</term><term>Testis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Amorces ADN</term><term>Protéines recombinantes</term><term>Thioredoxin reductase 1</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Actines</term><term>Membrane cellulaire</term><term>Protéines recombinantes</term><term>Tubuline</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Thioredoxin reductase 1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Thioredoxin Reductase 1</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Cell Membrane</term><term>Testis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Alternative Splicing</term><term>Base Sequence</term><term>Cell Line</term><term>Cell Line, Tumor</term><term>HeLa Cells</term><term>Humans</term><term>Male</term><term>Protein Structure, Tertiary</term><term>Transfection</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Cellules HeLa</term><term>Humains</term><term>Lignée cellulaire</term><term>Lignée cellulaire tumorale</term><term>Membrane cellulaire</term><term>Mâle</term><term>Structure tertiaire des protéines</term><term>Séquence nucléotidique</term><term>Testicule</term><term>Transfection</term><term>Épissage alternatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The human thioredoxin system has a wide range of functions in cells including regulation of cell proliferation and differentiation, immune system modulation, antioxidant defense, redox control of transcription factor activity, and promotion of cancer development. A key component of this enzymatic system is the selenoprotein thioredoxin reductase 1 (TrxR1), encoded by the TXNRD1 gene. Transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. Here we have studied the TXNRD1_v3 isoform containing an atypical N-terminal glutaredoxin (Grx) domain. Expression of the transcript of this isoform was found predominantly in testis but was also detected in ovary, spleen, heart, liver, kidney, and pancreas. By immunohistochemical analysis in human testis with antibodies specific for the Grx domain of TXNRD1_v3, the protein was found to be predominantly expressed in the Leydig cells. Expression of the TXNRD1_v3 transcript was also found in several cancer cell lines (HCC1937, H23, A549, U1810, or H157), and in HeLa cells, it was induced by estradiol or testosterone treatments. Surprisingly, green fluorescent protein fusions with the complete TXNRD1_v3 protein or with only its Grx domain localized to distinct cellular sites in proximity to actin, and furthermore, had a potent capacity to rapidly induce cell membrane protrusions. Analyses of these structures suggested that the Grx domain of TXNRD1_v3 localizes first in the emerging protrusion and is then followed into the protrusions by actin and subsequently by tubulin. The results presented thus reveal that TXNRD1_v3 has a unique and distinct expression pattern in human cells and suggest that the protein can guide actin polymerization in relation to cell membrane restructuring.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18042542</PMID><DateCompleted><Year>2008</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2008</Year><Month>01</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>283</Volume><Issue>5</Issue><PubDate><Year>2008</Year><Month>Feb</Month><Day>01</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1.</ArticleTitle><Pagination><MedlinePgn>2814-21</MedlinePgn></Pagination><Abstract><AbstractText>The human thioredoxin system has a wide range of functions in cells including regulation of cell proliferation and differentiation, immune system modulation, antioxidant defense, redox control of transcription factor activity, and promotion of cancer development. A key component of this enzymatic system is the selenoprotein thioredoxin reductase 1 (TrxR1), encoded by the TXNRD1 gene. Transcription of TXNRD1 involves alternative splicing, leading to a number of transcripts also encoding isoforms of TrxR1 that differ from each other at their N-terminal domains. Here we have studied the TXNRD1_v3 isoform containing an atypical N-terminal glutaredoxin (Grx) domain. Expression of the transcript of this isoform was found predominantly in testis but was also detected in ovary, spleen, heart, liver, kidney, and pancreas. By immunohistochemical analysis in human testis with antibodies specific for the Grx domain of TXNRD1_v3, the protein was found to be predominantly expressed in the Leydig cells. Expression of the TXNRD1_v3 transcript was also found in several cancer cell lines (HCC1937, H23, A549, U1810, or H157), and in HeLa cells, it was induced by estradiol or testosterone treatments. Surprisingly, green fluorescent protein fusions with the complete TXNRD1_v3 protein or with only its Grx domain localized to distinct cellular sites in proximity to actin, and furthermore, had a potent capacity to rapidly induce cell membrane protrusions. Analyses of these structures suggested that the Grx domain of TXNRD1_v3 localizes first in the emerging protrusion and is then followed into the protrusions by actin and subsequently by tubulin. The results presented thus reveal that TXNRD1_v3 has a unique and distinct expression pattern in human cells and suggest that the protein can guide actin polymerization in relation to cell membrane restructuring.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dammeyer</LastName><ForeName>Pascal</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Damdimopoulos</LastName><ForeName>Anastasios E</ForeName><Initials>AE</Initials></Author><Author ValidYN="Y"><LastName>Nordman</LastName><ForeName>Tomas</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Jiménez</LastName><ForeName>Alberto</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Miranda-Vizuete</LastName><ForeName>Antonio</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Arnér</LastName><ForeName>Elias S J</ForeName><Initials>ES</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>11</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000199">Actins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014404">Tubulin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="C516124">TXNRD1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D054481">Thioredoxin Reductase 1</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000199" MajorTopicYN="N">Actins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017398" MajorTopicYN="N">Alternative Splicing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013737" MajorTopicYN="N">Testis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054481" MajorTopicYN="N">Thioredoxin Reductase 1</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014404" MajorTopicYN="N">Tubulin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>11</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>4</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>11</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18042542</ArticleId><ArticleId IdType="pii">M708939200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M708939200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Arner, Elias S J" sort="Arner, Elias S J" uniqKey="Arner E" first="Elias S J" last="Arnér">Elias S J. Arnér</name><name sortKey="Damdimopoulos, Anastasios E" sort="Damdimopoulos, Anastasios E" uniqKey="Damdimopoulos A" first="Anastasios E" last="Damdimopoulos">Anastasios E. Damdimopoulos</name><name sortKey="Jimenez, Alberto" sort="Jimenez, Alberto" uniqKey="Jimenez A" first="Alberto" last="Jiménez">Alberto Jiménez</name><name sortKey="Miranda Vizuete, Antonio" sort="Miranda Vizuete, Antonio" uniqKey="Miranda Vizuete A" first="Antonio" last="Miranda-Vizuete">Antonio Miranda-Vizuete</name><name sortKey="Nordman, Tomas" sort="Nordman, Tomas" uniqKey="Nordman T" first="Tomas" last="Nordman">Tomas Nordman</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Dammeyer, Pascal" sort="Dammeyer, Pascal" uniqKey="Dammeyer P" first="Pascal" last="Dammeyer">Pascal Dammeyer</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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