Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus α-interferon (IFN-αCON1) in the hamster
Identifieur interne : 001628 ( Istex/Corpus ); précédent : 001627; suivant : 001629Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus α-interferon (IFN-αCON1) in the hamster
Auteurs : Shabbir M. Moochhala ; Kenneth W. Renton ; Nowell StebbingSource :
- Biochemical Pharmacology [ 0006-2952 ] ; 1989.
Abstract
A novel analogue of human α-interferon (IFN-αCON1) was tested for its ability to modify the hepatic cytochrome-P-450-dependent mixed-function oxidase system in the hamster. This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human α-interferon subtypes. IFN-αCON1 had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression. IFN-αCON1 also had a biphasic effect on cytochrome P-450 in the lung, adrenal and spleen but only a depressant effect in the kidney. This effect was not due to morphological damage and followed the species specificity for this type of interferon. Both the increase and the decrease in cytochrome P-450 could be prevented by the administration of the protein synthesis inhibitor puromycin. Various isozymes of cytochrome P-450 induced by phenobarbital, β-napthaflavone and clofibrate were also depressed by this interferon. The results presented in this report suggest that IFN-αCON1 interferon will likely depress drug biotransformation in humans because the antiviral effects and the “anticytochrome P-450” effect of interferons cannot be separated, and this interferon has antiviral properties in both hamster and human cells. Clinically relevant drug interactions may be common during the concomitant use of this interferon and other drugs that are metabolized by cytochrome P-450.
Url:
DOI: 10.1016/0006-2952(89)90383-3
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Renton</name><affiliation><mods:affiliation>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</mods:affiliation></affiliation></author><author><name sortKey="Stebbing, Nowell" sort="Stebbing, Nowell" uniqKey="Stebbing N" first="Nowell" last="Stebbing">Nowell Stebbing</name><affiliation><mods:affiliation>Amgen Inc., Thousand Oaks, CA, U.S.A.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:65DA78E2925BF0F4B5114DDEC102E11CE45D0649</idno><date when="1989" year="1989">1989</date><idno type="doi">10.1016/0006-2952(89)90383-3</idno><idno type="url">https://api-v5.istex.fr/document/65DA78E2925BF0F4B5114DDEC102E11CE45D0649/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001628</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001628</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus α-interferon (IFN-αCON1) in the hamster</title><author><name sortKey="Moochhala, Shabbir M" sort="Moochhala, Shabbir M" uniqKey="Moochhala S" first="Shabbir M." last="Moochhala">Shabbir M. 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Renton</name><affiliation><mods:affiliation>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</mods:affiliation></affiliation></author><author><name sortKey="Stebbing, Nowell" sort="Stebbing, Nowell" uniqKey="Stebbing N" first="Nowell" last="Stebbing">Nowell Stebbing</name><affiliation><mods:affiliation>Amgen Inc., Thousand Oaks, CA, U.S.A.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Biochemical Pharmacology</title><title level="j" type="abbrev">BCP</title><idno type="ISSN">0006-2952</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1989">1989</date><biblScope unit="volume">38</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="439">439</biblScope><biblScope unit="page" to="447">447</biblScope></imprint><idno type="ISSN">0006-2952</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2952</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A novel analogue of human α-interferon (IFN-αCON1) was tested for its ability to modify the hepatic cytochrome-P-450-dependent mixed-function oxidase system in the hamster. This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human α-interferon subtypes. IFN-αCON1 had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression. IFN-αCON1 also had a biphasic effect on cytochrome P-450 in the lung, adrenal and spleen but only a depressant effect in the kidney. This effect was not due to morphological damage and followed the species specificity for this type of interferon. Both the increase and the decrease in cytochrome P-450 could be prevented by the administration of the protein synthesis inhibitor puromycin. Various isozymes of cytochrome P-450 induced by phenobarbital, β-napthaflavone and clofibrate were also depressed by this interferon. The results presented in this report suggest that IFN-αCON1 interferon will likely depress drug biotransformation in humans because the antiviral effects and the “anticytochrome P-450” effect of interferons cannot be separated, and this interferon has antiviral properties in both hamster and human cells. Clinically relevant drug interactions may be common during the concomitant use of this interferon and other drugs that are metabolized by cytochrome P-450.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Shabbir M. Moochhala</name><affiliations><json:string>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</json:string></affiliations></json:item><json:item><name>Kenneth W. Renton</name><affiliations><json:string>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</json:string></affiliations></json:item><json:item><name>Nowell Stebbing</name><affiliations><json:string>Amgen Inc., Thousand Oaks, CA, U.S.A.</json:string></affiliations></json:item></author><articleId><json:string>89903833</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>A novel analogue of human α-interferon (IFN-αCON1) was tested for its ability to modify the hepatic cytochrome-P-450-dependent mixed-function oxidase system in the hamster. This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human α-interferon subtypes. IFN-αCON1 had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression. IFN-αCON1 also had a biphasic effect on cytochrome P-450 in the lung, adrenal and spleen but only a depressant effect in the kidney. This effect was not due to morphological damage and followed the species specificity for this type of interferon. Both the increase and the decrease in cytochrome P-450 could be prevented by the administration of the protein synthesis inhibitor puromycin. Various isozymes of cytochrome P-450 induced by phenobarbital, β-napthaflavone and clofibrate were also depressed by this interferon. The results presented in this report suggest that IFN-αCON1 interferon will likely depress drug biotransformation in humans because the antiviral effects and the “anticytochrome P-450” effect of interferons cannot be separated, and this interferon has antiviral properties in both hamster and human cells. 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This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human α-interferon subtypes. IFN-αCON1 had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression. IFN-αCON1 also had a biphasic effect on cytochrome P-450 in the lung, adrenal and spleen but only a depressant effect in the kidney. This effect was not due to morphological damage and followed the species specificity for this type of interferon. Both the increase and the decrease in cytochrome P-450 could be prevented by the administration of the protein synthesis inhibitor puromycin. Various isozymes of cytochrome P-450 induced by phenobarbital, β-napthaflavone and clofibrate were also depressed by this interferon. The results presented in this report suggest that IFN-αCON1 interferon will likely depress drug biotransformation in humans because the antiviral effects and the “anticytochrome P-450” effect of interferons cannot be separated, and this interferon has antiviral properties in both hamster and human cells. Clinically relevant drug interactions may be common during the concomitant use of this interferon and other drugs that are metabolized by cytochrome P-450.</p></abstract></profileDesc><revisionDesc><change when="1989">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api-v5.istex.fr/document/65DA78E2925BF0F4B5114DDEC102E11CE45D0649/fulltext/txt</uri></json:item></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" xml:lang="en"><item-info><jid>BCP</jid><aid>89903833</aid><ce:pii>0006-2952(89)90383-3</ce:pii><ce:doi>10.1016/0006-2952(89)90383-3</ce:doi><ce:copyright type="unknown" year="1989"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was supported by a grant from the Medical Research Council of Canada. S. M. M. was a recipient of a studentship from the Canadian Heart Foundation.</ce:note-para></ce:article-footnote><ce:title>Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus α-interferon (IFN-αCON<ce:inf loc="post">1</ce:inf>) in the hamster</ce:title><ce:author-group><ce:author><ce:given-name>Shabbir M.</ce:given-name><ce:surname>Moochhala</ce:surname><ce:cross-ref refid="FN1"><ce:sup loc="post">†</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Kenneth W.</ce:given-name><ce:surname>Renton</ce:surname><ce:cross-ref refid="COR1"><ce:sup loc="post">‡</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>‡</ce:label><ce:text>author to whom all correspondence should be addressed.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>†</ce:label><ce:note-para>Present address: Department of Pharmacology, University of Singapore, Singapore.</ce:note-para></ce:footnote></ce:author-group><ce:author-group><ce:author><ce:given-name>Nowell</ce:given-name><ce:surname>Stebbing</ce:surname><ce:cross-ref refid="FN2"><ce:sup loc="post">§</ce:sup></ce:cross-ref></ce:author><ce:affiliation><ce:textfn>Amgen Inc., Thousand Oaks, CA, U.S.A.</ce:textfn></ce:affiliation><ce:footnote id="FN2"><ce:label>§</ce:label><ce:note-para>Present address: ICI Pharmaceuticals Division, Alderney Park, Macclesfield, EngLond.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="12" month="11" year="1987"></ce:date-received><ce:date-accepted day="30" month="6" year="1988"></ce:date-accepted><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">A novel analogue of human α-interferon (IFN-αCON<ce:inf loc="post">1</ce:inf>) was tested for its ability to modify the hepatic cytochrome-P-450-dependent mixed-function oxidase system in the hamster. This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human α-interferon subtypes. IFN-αCON<ce:inf loc="post">1</ce:inf> had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression. IFN-αCON<ce:inf loc="post">1</ce:inf> also had a biphasic effect on cytochrome P-450 in the lung, adrenal and spleen but only a depressant effect in the kidney. This effect was not due to morphological damage and followed the species specificity for this type of interferon. Both the increase and the decrease in cytochrome P-450 could be prevented by the administration of the protein synthesis inhibitor puromycin. Various isozymes of cytochrome P-450 induced by phenobarbital, β-napthaflavone and clofibrate were also depressed by this interferon. The results presented in this report suggest that IFN-αCON<ce:inf loc="post">1</ce:inf> interferon will likely depress drug biotransformation in humans because the antiviral effects and the “anticytochrome P-450” effect of interferons cannot be separated, and this interferon has antiviral properties in both hamster and human cells. Clinically relevant drug interactions may be common during the concomitant use of this interferon and other drugs that are metabolized by cytochrome P-450.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus α-interferon (IFN-αCON1) in the hamster</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Induction and depression of cytochrome P-450-dependent mixed-function oxidase by a cloned consensus α-interferon (IFN-αCON</title></titleInfo><name type="personal"><namePart type="given">Shabbir M.</namePart><namePart type="family">Moochhala</namePart><affiliation>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</affiliation><description>Present address: Department of Pharmacology, University of Singapore, Singapore.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Kenneth W.</namePart><namePart type="family">Renton</namePart><affiliation>Department of Pharmacology, Dalhousie University, Halifax, Nova Scotia, Canada B3H 4H7</affiliation><description>author to whom all correspondence should be addressed.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Nowell</namePart><namePart type="family">Stebbing</namePart><affiliation>Amgen Inc., Thousand Oaks, CA, U.S.A.</affiliation><description>Present address: ICI Pharmaceuticals Division, Alderney Park, Macclesfield, EngLond.</description><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">1989</dateIssued><copyrightDate encoding="w3cdtf">1989</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">A novel analogue of human α-interferon (IFN-αCON1) was tested for its ability to modify the hepatic cytochrome-P-450-dependent mixed-function oxidase system in the hamster. This cloned interferon was derived by selecting the most frequently observed amino acid sequences at each position in the known human α-interferon subtypes. IFN-αCON1 had a biphasic effect on cytochrome P-450 and related drug biotransformation in the hamster causing an initial increase followed by a significant depression. IFN-αCON1 also had a biphasic effect on cytochrome P-450 in the lung, adrenal and spleen but only a depressant effect in the kidney. This effect was not due to morphological damage and followed the species specificity for this type of interferon. Both the increase and the decrease in cytochrome P-450 could be prevented by the administration of the protein synthesis inhibitor puromycin. Various isozymes of cytochrome P-450 induced by phenobarbital, β-napthaflavone and clofibrate were also depressed by this interferon. The results presented in this report suggest that IFN-αCON1 interferon will likely depress drug biotransformation in humans because the antiviral effects and the “anticytochrome P-450” effect of interferons cannot be separated, and this interferon has antiviral properties in both hamster and human cells. Clinically relevant drug interactions may be common during the concomitant use of this interferon and other drugs that are metabolized by cytochrome P-450.</abstract><note>This work was supported by a grant from the Medical Research Council of Canada. S. M. 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