Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat
Identifieur interne : 000A52 ( Istex/Corpus ); précédent : 000A51; suivant : 000A53Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat
Auteurs : Margherita Strolin Benedetti ; Thierry Boucher ; Arvid Carlsson ; Christopher J. FowlerSource :
- Biochemical Pharmacology [ 0006-2952 ] ; 1983.
Abstract
The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different Km and Vmax values towards tyramine. The Km values for the A-form of the enzyme towards this substrate were around 120 μM in both cases, whereas the values for the B-form were about 240 μM. As a consequence, the ratio of activities (MAO-A: MAO-B) towards tyramine are dependent upon the substrate concentration. The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with Ki values of 3.4 μM and 3.7 nM respectively. The significance of these results in relation to the “cheese effect”, a pressor response to tyramine after monoamine oxidase inhibition, are discussed.
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DOI: 10.1016/0006-2952(83)90650-0
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Fowler</name><affiliation><mods:affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:DAB018C16B263CC461F6C0BA5C1158F2C618CB09</idno><date when="1983" year="1983">1983</date><idno type="doi">10.1016/0006-2952(83)90650-0</idno><idno type="url">https://api.istex.fr/document/DAB018C16B263CC461F6C0BA5C1158F2C618CB09/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000A52</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000A52</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat</title><author><name sortKey="Benedetti, Margherita Strolin" sort="Benedetti, Margherita Strolin" uniqKey="Benedetti M" first="Margherita Strolin" last="Benedetti">Margherita Strolin Benedetti</name><affiliation><mods:affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</mods:affiliation></affiliation></author><author><name sortKey="Boucher, Thierry" sort="Boucher, Thierry" uniqKey="Boucher T" first="Thierry" last="Boucher">Thierry Boucher</name><affiliation><mods:affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</mods:affiliation></affiliation></author><author><name sortKey="Carlsson, Arvid" sort="Carlsson, Arvid" uniqKey="Carlsson A" first="Arvid" last="Carlsson">Arvid Carlsson</name><affiliation><mods:affiliation>Department of Pharmacology, University of Göteborg, S-400 33 Göteborg, Sweden</mods:affiliation></affiliation></author><author><name sortKey="Fowler, Christopher J" sort="Fowler, Christopher J" uniqKey="Fowler C" first="Christopher J." last="Fowler">Christopher J. Fowler</name><affiliation><mods:affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</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="1983">1983</date><biblScope unit="volume">32</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="47">47</biblScope><biblScope unit="page" to="52">52</biblScope></imprint><idno type="ISSN">0006-2952</idno></series><idno type="istex">DAB018C16B263CC461F6C0BA5C1158F2C618CB09</idno><idno type="DOI">10.1016/0006-2952(83)90650-0</idno><idno type="PII">0006-2952(83)90650-0</idno><idno type="ArticleID">83906500</idno></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">The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different Km and Vmax values towards tyramine. The Km values for the A-form of the enzyme towards this substrate were around 120 μM in both cases, whereas the values for the B-form were about 240 μM. As a consequence, the ratio of activities (MAO-A: MAO-B) towards tyramine are dependent upon the substrate concentration. The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with Ki values of 3.4 μM and 3.7 nM respectively. The significance of these results in relation to the “cheese effect”, a pressor response to tyramine after monoamine oxidase inhibition, are discussed.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>Margherita Strolin Benedetti</name><affiliations><json:string>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</json:string></affiliations></json:item><json:item><name>Thierry Boucher</name><affiliations><json:string>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</json:string></affiliations></json:item><json:item><name>Arvid Carlsson</name><affiliations><json:string>Department of Pharmacology, University of Göteborg, S-400 33 Göteborg, Sweden</json:string></affiliations></json:item><json:item><name>Christopher J. 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The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with Ki values of 3.4 μM and 3.7 nM respectively. 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Strolin Benedetti.</p></note><affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</affiliation></author><author xml:id="author-2"><persName><forename type="first">Thierry</forename><surname>Boucher</surname></persName><affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Arvid</forename><surname>Carlsson</surname></persName><affiliation>Department of Pharmacology, University of Göteborg, S-400 33 Göteborg, Sweden</affiliation></author><author xml:id="author-4"><persName><forename type="first">Christopher J.</forename><surname>Fowler</surname></persName><note type="biography">Present address: Astra, Läkemedel AB, S-151 85 Södertälje, Sweden.</note><affiliation>Present address: Astra, Läkemedel AB, S-151 85 Södertälje, Sweden.</affiliation><affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</affiliation></author></analytic><monogr><title level="j">Biochemical Pharmacology</title><title level="j" type="abbrev">BCP</title><idno type="pISSN">0006-2952</idno><idno type="PII">S0006-2952(00)X0880-5</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1983"></date><biblScope unit="volume">32</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="47">47</biblScope><biblScope unit="page" to="52">52</biblScope></imprint></monogr><idno type="istex">DAB018C16B263CC461F6C0BA5C1158F2C618CB09</idno><idno type="DOI">10.1016/0006-2952(83)90650-0</idno><idno type="PII">0006-2952(83)90650-0</idno><idno type="ArticleID">83906500</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1983</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different Km and Vmax values towards tyramine. The Km values for the A-form of the enzyme towards this substrate were around 120 μM in both cases, whereas the values for the B-form were about 240 μM. As a consequence, the ratio of activities (MAO-A: MAO-B) towards tyramine are dependent upon the substrate concentration. The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with Ki values of 3.4 μM and 3.7 nM respectively. The significance of these results in relation to the “cheese effect”, a pressor response to tyramine after monoamine oxidase inhibition, are discussed.</p></abstract></profileDesc><revisionDesc><change when="1983">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/DAB018C16B263CC461F6C0BA5C1158F2C618CB09/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>83906500</aid><ce:pii>0006-2952(83)90650-0</ce:pii><ce:doi>10.1016/0006-2952(83)90650-0</ce:doi><ce:copyright type="unknown" year="1983"></ce:copyright></item-info><head><ce:title>Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat</ce:title><ce:author-group><ce:author><ce:given-name>Margherita Strolin</ce:given-name><ce:surname>Benedetti</ce:surname><ce:cross-ref refid="COR1"><ce:sup loc="post">†</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup loc="post">∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Thierry</ce:given-name><ce:surname>Boucher</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">∗</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Arvid</ce:given-name><ce:surname>Carlsson</ce:surname><ce:cross-ref refid="AFF2"><ce:sup loc="post">‡</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Christopher J.</ce:given-name><ce:surname>Fowler</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">∗</ce:sup></ce:cross-ref><ce:cross-ref refid="FN1"><ce:sup loc="post">§</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>∗</ce:label><ce:textfn>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>‡</ce:label><ce:textfn>Department of Pharmacology, University of Göteborg, S-400 33 Göteborg, Sweden</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>†</ce:label><ce:text>Correspondence to Dr. M. Strolin Benedetti.</ce:text></ce:correspondence><ce:footnote id="FN1"><ce:label>§</ce:label><ce:note-para>Present address: Astra, Läkemedel AB, S-151 85 Södertälje, Sweden.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="10" month="5" year="1982"></ce:date-received><ce:date-accepted day="7" month="7" year="1982"></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">The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different <ce:italic>K</ce:italic><ce:inf loc="post"><ce:italic>m</ce:italic></ce:inf> and <ce:italic>V</ce:italic><ce:inf loc="post">max</ce:inf> values towards tyramine. The <ce:italic>K</ce:italic><ce:inf loc="post"><ce:italic>m</ce:italic></ce:inf> values for the A-form of the enzyme towards this substrate were around 120 μM in both cases, whereas the values for the B-form were about 240 μM. As a consequence, the ratio of activities (MAO-A: MAO-B) towards tyramine are dependent upon the substrate concentration. The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with <ce:italic>K</ce:italic><ce:inf loc="post"><ce:italic>i</ce:italic></ce:inf> values of 3.4 μM and 3.7 nM respectively. The significance of these results in relation to the “cheese effect”, a pressor response to tyramine after monoamine oxidase inhibition, are discussed.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Intestinal metabolism of tyramine by both forms of monoamine oxidase in the rat</title></titleInfo><name type="personal"><namePart type="given">Margherita Strolin</namePart><namePart type="family">Benedetti</namePart><affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</affiliation><description>Correspondence to Dr. M. Strolin Benedetti.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Thierry</namePart><namePart type="family">Boucher</namePart><affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Arvid</namePart><namePart type="family">Carlsson</namePart><affiliation>Department of Pharmacology, University of Göteborg, S-400 33 Göteborg, Sweden</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christopher J.</namePart><namePart type="family">Fowler</namePart><affiliation>Centre de Recherche Delalae, 10 rue des Carrières, F-92500 Rueil-Malmaison, France</affiliation><description>Present address: Astra, Läkemedel AB, S-151 85 Södertälje, Sweden.</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">1983</dateIssued><copyrightDate encoding="w3cdtf">1983</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">The two forms of monoamine oxidase (MAO) in rat intestine and brain homogenates were found to have different Km and Vmax values towards tyramine. The Km values for the A-form of the enzyme towards this substrate were around 120 μM in both cases, whereas the values for the B-form were about 240 μM. As a consequence, the ratio of activities (MAO-A: MAO-B) towards tyramine are dependent upon the substrate concentration. The MAO-A-selective inhibitors, toloxatone and cimoxatone, were found to be competitive inhibitors of the oxidation of tyramine by the A-form of this enzyme in the rat intestine, with Ki values of 3.4 μM and 3.7 nM respectively. The significance of these results in relation to the “cheese effect”, a pressor response to tyramine after monoamine oxidase inhibition, are discussed.</abstract><relatedItem type="host"><titleInfo><title>Biochemical Pharmacology</title></titleInfo><titleInfo type="abbreviated"><title>BCP</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19830101</dateIssued></originInfo><identifier type="ISSN">0006-2952</identifier><identifier type="PII">S0006-2952(00)X0880-5</identifier><part><date>19830101</date><detail type="volume"><number>32</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>188</end></extent><extent unit="pages"><start>47</start><end>52</end></extent></part></relatedItem><identifier type="istex">DAB018C16B263CC461F6C0BA5C1158F2C618CB09</identifier><identifier type="DOI">10.1016/0006-2952(83)90650-0</identifier><identifier type="PII">0006-2952(83)90650-0</identifier><identifier type="ArticleID">83906500</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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