Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance
Identifieur interne : 002B21 ( Istex/Corpus ); précédent : 002B20; suivant : 002B22Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance
Auteurs : Michael J. Kelner ; Richard Bagnell ; Mark Montoya ; Leita Estes ; Slavomir F. Uglik ; Peter CeruttiSource :
- Free Radical Biology and Medicine [ 0891-5849 ] ; 1994.
Abstract
Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/ copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.
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DOI: 10.1016/0891-5849(94)00167-I
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Kelner</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Bagnell, Richard" sort="Bagnell, Richard" uniqKey="Bagnell R" first="Richard" last="Bagnell">Richard Bagnell</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Montoya, Mark" sort="Montoya, Mark" uniqKey="Montoya M" first="Mark" last="Montoya">Mark Montoya</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Estes, Leita" sort="Estes, Leita" uniqKey="Estes L" first="Leita" last="Estes">Leita Estes</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Uglik, Slavomir F" sort="Uglik, Slavomir F" uniqKey="Uglik S" first="Slavomir F." last="Uglik">Slavomir F. 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Kelner</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Bagnell, Richard" sort="Bagnell, Richard" uniqKey="Bagnell R" first="Richard" last="Bagnell">Richard Bagnell</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Montoya, Mark" sort="Montoya, Mark" uniqKey="Montoya M" first="Mark" last="Montoya">Mark Montoya</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Estes, Leita" sort="Estes, Leita" uniqKey="Estes L" first="Leita" last="Estes">Leita Estes</name><affiliation><mods:affiliation>University of California, San Diego, CA, USA</mods:affiliation></affiliation></author><author><name sortKey="Uglik, Slavomir F" sort="Uglik, Slavomir F" uniqKey="Uglik S" first="Slavomir F." last="Uglik">Slavomir F. Uglik</name><affiliation><mods:affiliation>Polish Mother's Memorial Hospital, Lodz, Poland</mods:affiliation></affiliation></author><author><name sortKey="Cerutti, Peter" sort="Cerutti, Peter" uniqKey="Cerutti P" first="Peter" last="Cerutti">Peter Cerutti</name><affiliation><mods:affiliation>Department of Carcinogenesis, Swiss Institute for Experimental Cancer Research, Epalinges/Lausanne, Switzerland</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Free Radical Biology and Medicine</title><title level="j" type="abbrev">FRB</title><idno type="ISSN">0891-5849</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">18</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="497">497</biblScope><biblScope unit="page" to="506">506</biblScope></imprint><idno type="ISSN">0891-5849</idno></series><idno type="istex">C1691153098686D2F24FB244D16DC49D40B48666</idno><idno type="DOI">10.1016/0891-5849(94)00167-I</idno><idno type="PII">0891-5849(94)00167-I</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0891-5849</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/ copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Michael J. Kelner</name><affiliations><json:string>University of California, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Richard Bagnell</name><affiliations><json:string>University of California, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Mark Montoya</name><affiliations><json:string>University of California, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Leita Estes</name><affiliations><json:string>University of California, San Diego, CA, USA</json:string></affiliations></json:item><json:item><name>Slavomir F. Uglik</name><affiliations><json:string>Polish Mother's Memorial Hospital, Lodz, Poland</json:string></affiliations></json:item><json:item><name>Peter Cerutti</name><affiliations><json:string>Department of Carcinogenesis, Swiss Institute for Experimental Cancer Research, Epalinges/Lausanne, Switzerland</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Glutathione peroxidase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Hydrogen peroxide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Catalase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Fibronectin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Superoxide dismutase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>FGF</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Paraquat</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Free radicals</value></json:item></subject><language><json:string>eng</json:string></language><abstract>Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/ copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.</abstract><qualityIndicators><score>7.028</score><pdfVersion>1.2</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>8</keywordCount><abstractCharCount>1358</abstractCharCount><pdfWordCount>6249</pdfWordCount><pdfCharCount>38042</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>169</abstractWordCount></qualityIndicators><title>Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance</title><pii><json:string>0891-5849(94)00167-I</json:string></pii><genre><json:string>research-article</json:string></genre><serie><volume>Vol. 283</volume><pages><last>309</last><first>305</first></pages><genre></genre><language><json:string>unknown</json:string></language><title>Biol. reactive intermediates IV. 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Kelner, UCSD, 200 West Arbor Drive, San Diego, CA 92103-8320, USA.</affiliation><affiliation>University of California, San Diego, CA, USA</affiliation></author><author><persName><forename type="first">Richard</forename><surname>Bagnell</surname></persName><affiliation>University of California, San Diego, CA, USA</affiliation></author><author><persName><forename type="first">Mark</forename><surname>Montoya</surname></persName><affiliation>University of California, San Diego, CA, USA</affiliation></author><author><persName><forename type="first">Leita</forename><surname>Estes</surname></persName><affiliation>University of California, San Diego, CA, USA</affiliation></author><author><persName><forename type="first">Slavomir F.</forename><surname>Uglik</surname></persName><affiliation>Polish Mother's Memorial Hospital, Lodz, Poland</affiliation></author><author><persName><forename type="first">Peter</forename><surname>Cerutti</surname></persName><affiliation>Department of Carcinogenesis, Swiss Institute for Experimental Cancer Research, Epalinges/Lausanne, Switzerland</affiliation></author></analytic><monogr><title level="j">Free Radical Biology and Medicine</title><title level="j" type="abbrev">FRB</title><idno type="pISSN">0891-5849</idno><idno type="PII">S0891-5849(00)X0022-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1994"></date><biblScope unit="volume">18</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="497">497</biblScope><biblScope unit="page" to="506">506</biblScope></imprint></monogr><idno type="istex">C1691153098686D2F24FB244D16DC49D40B48666</idno><idno type="DOI">10.1016/0891-5849(94)00167-I</idno><idno type="PII">0891-5849(94)00167-I</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1995</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/ copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Glutathione peroxidase</term></item><item><term>Hydrogen peroxide</term></item><item><term>Catalase</term></item><item><term>Fibronectin</term></item><item><term>Superoxide dismutase</term></item><item><term>FGF</term></item><item><term>Paraquat</term></item><item><term>Free radicals</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1994-07-13">Registration</change><change when="1994-07-08">Modified</change><change when="1994">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>FRB</jid><aid>9400167I</aid><ce:pii>0891-5849(94)00167-I</ce:pii><ce:doi>10.1016/0891-5849(94)00167-I</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:dochead><ce:textfn>Original contribution</ce:textfn></ce:dochead><ce:title>Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance</ce:title><ce:author-group><ce:author><ce:given-name>Michael J.</ce:given-name><ce:surname>Kelner</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Richard</ce:given-name><ce:surname>Bagnell</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Mark</ce:given-name><ce:surname>Montoya</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Leita</ce:given-name><ce:surname>Estes</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Slavomir F.</ce:given-name><ce:surname>Uglik</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Peter</ce:given-name><ce:surname>Cerutti</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>∗</ce:label><ce:textfn>University of California, San Diego, CA, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>†</ce:label><ce:textfn>Polish Mother's Memorial Hospital, Lodz, Poland</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>‡</ce:label><ce:textfn>Department of Carcinogenesis, Swiss Institute for Experimental Cancer Research, Epalinges/Lausanne, Switzerland</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Address correspondence to: Michael J. Kelner, UCSD, 200 West Arbor Drive, San Diego, CA 92103-8320, USA.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="4" month="4" year="1994"></ce:date-received><ce:date-revised day="8" month="7" year="1994"></ce:date-revised><ce:date-accepted day="13" month="7" year="1994"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/ copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Glutathione peroxidase</ce:text></ce:keyword><ce:keyword><ce:text>Hydrogen peroxide</ce:text></ce:keyword><ce:keyword><ce:text>Catalase</ce:text></ce:keyword><ce:keyword><ce:text>Fibronectin</ce:text></ce:keyword><ce:keyword><ce:text>Superoxide dismutase</ce:text></ce:keyword><ce:keyword><ce:text>FGF</ce:text></ce:keyword><ce:keyword><ce:text>Paraquat</ce:text></ce:keyword><ce:keyword><ce:text>Free radicals</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Transfection with human copper-zinc superoxide dismutase induces bidirectional alterations in other antioxidant enzymes, proteins, growth factor response, and paraquat resistance</title></titleInfo><name type="personal"><namePart type="given">Michael J.</namePart><namePart type="family">Kelner</namePart><affiliation>University of California, San Diego, CA, USA</affiliation><description>Address correspondence to: Michael J. Kelner, UCSD, 200 West Arbor Drive, San Diego, CA 92103-8320, USA.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Richard</namePart><namePart type="family">Bagnell</namePart><affiliation>University of California, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Mark</namePart><namePart type="family">Montoya</namePart><affiliation>University of California, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Leita</namePart><namePart type="family">Estes</namePart><affiliation>University of California, San Diego, CA, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Slavomir F.</namePart><namePart type="family">Uglik</namePart><affiliation>Polish Mother's Memorial Hospital, Lodz, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Peter</namePart><namePart type="family">Cerutti</namePart><affiliation>Department of Carcinogenesis, Swiss Institute for Experimental Cancer Research, Epalinges/Lausanne, Switzerland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1994</dateIssued><dateValid encoding="w3cdtf">1994-07-13</dateValid><dateModified encoding="w3cdtf">1994-07-08</dateModified><copyrightDate encoding="w3cdtf">1995</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Transfection of a pSV2 human copper-zinc superoxide dismutase expression vector into murine fibroblasts resulted in stable transgenic clones producing increased amounts of copper-zinc superoxide dismutase. Two classes of transfectants were observed and were characterized by the presence or absence of an increase in endogenous glutathione peroxidase activity. In addition, increases and decreases in individual clones in the activities of manganese superoxide dismutase, glutathione reductase, and NADPH-reductase were detected. In general, these alterations in enzyme activity correlated to the cellular glutathione peroxidase/copper-zinc superoxide dismutase ratio. Parameters of cellular physiological functions were also altered, including cell division time, FGF and EGF response, fibronectin content, paraquat resistance, hydrogen peroxide release into media, and sensitivity to radiation. Some of these cellular parameters were also bidirectional and reflected the cellular glutathione peroxidase/ copper-zinc superoxide dismutase ratio. Our results indicate that small deviations from the normal physiological copper-zinc superoxide dismutase/seleno-glutathione peroxidase ratios can have pronounced effects on other antioxidant enzymes, growth rate, growth factor response, and expression of proteins normally not associated with oxygen metabolism.</abstract><note type="content">Section title: Original contribution</note><subject><genre>Keywords</genre><topic>Glutathione peroxidase</topic><topic>Hydrogen peroxide</topic><topic>Catalase</topic><topic>Fibronectin</topic><topic>Superoxide dismutase</topic><topic>FGF</topic><topic>Paraquat</topic><topic>Free radicals</topic></subject><relatedItem type="host"><titleInfo><title>Free Radical Biology and Medicine</title></titleInfo><titleInfo type="abbreviated"><title>FRB</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">199503</dateIssued></originInfo><identifier type="ISSN">0891-5849</identifier><identifier type="PII">S0891-5849(00)X0022-6</identifier><part><date>199503</date><detail type="volume"><number>18</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>383</start><end>632</end></extent><extent unit="pages"><start>497</start><end>506</end></extent></part></relatedItem><identifier type="istex">C1691153098686D2F24FB244D16DC49D40B48666</identifier><identifier type="DOI">10.1016/0891-5849(94)00167-I</identifier><identifier type="PII">0891-5849(94)00167-I</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/C1691153098686D2F24FB244D16DC49D40B48666/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">ENDOCRINOLOGY & METABOLISM</classCode><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments></istex></record>Pour manipuler ce document sous Unix (Dilib)
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