Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro
Identifieur interne : 000D12 ( Istex/Corpus ); précédent : 000D11; suivant : 000D13Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro
Auteurs : V. Gene Erwin ; Richard A. DeitrichSource :
- Biochemical Pharmacology [ 0006-2952 ] ; 1973.
English descriptors
- Teeft :
- Aldehyde, Aldehyde reductase, Aldehyde reductase activity, Anticonvulsant, Anticonvulsant actions, Anticonvulsant activity, Anticonvulsant compounds, Assay system, Barbiturate, Bovine, Bovine brain aldehyde reductase, Bovine brain aldehyde reductase inhibition, Brain aldehyde reductase activity, Brain tissue, Derivative, Dimethadione, Diphenylhydantoin, Enzyme activity, Enzyme protein, Erwin, Ethosuximide, Ethotoin, Experimental conditions, Hydantoin, Inhibition, Inhibitor, Nadph, Nadph oxidation, Nmoles nadph, Noncompetitive, Pharmac, Phenobarbital, Reaction mixture, Reaction mixtures, Reductase, Sodium phosphate, Specific activity, Trimethadione, Variable substrate, Various anticonvulsants, Various barbiturates, Various compounds, Various inhibitors.
Abstract
Abstract: The catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited in vitro by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.
Url:
DOI: 10.1016/0006-2952(73)90070-1
Links to Exploration step
ISTEX:D9C061695E6DC1300EA5AE9E05C1481FAC657C1ALe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro</title><author><name sortKey="Gene Erwin, V" sort="Gene Erwin, V" uniqKey="Gene Erwin V" first="V." last="Gene Erwin">V. Gene Erwin</name></author><author><name sortKey="Deitrich, Richard A" sort="Deitrich, Richard A" uniqKey="Deitrich R" first="Richard A." last="Deitrich">Richard A. Deitrich</name><affiliation><mods:affiliation>School of Pharmacy, University of Colorado, Boulder, Col. 80302, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Pharmacology, University of Colorado Medical Center, Denver, Col. 80220, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>†Recipient of Career Development Award NIH.</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:D9C061695E6DC1300EA5AE9E05C1481FAC657C1A</idno><date when="1973" year="1973">1973</date><idno type="doi">10.1016/0006-2952(73)90070-1</idno><idno type="url">https://api.istex.fr/document/D9C061695E6DC1300EA5AE9E05C1481FAC657C1A/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000D12</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000D12</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro</title><author><name sortKey="Gene Erwin, V" sort="Gene Erwin, V" uniqKey="Gene Erwin V" first="V." last="Gene Erwin">V. Gene Erwin</name></author><author><name sortKey="Deitrich, Richard A" sort="Deitrich, Richard A" uniqKey="Deitrich R" first="Richard A." last="Deitrich">Richard A. Deitrich</name><affiliation><mods:affiliation>School of Pharmacy, University of Colorado, Boulder, Col. 80302, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Pharmacology, University of Colorado Medical Center, Denver, Col. 80220, U.S.A.</mods:affiliation></affiliation><affiliation><mods:affiliation>†Recipient of Career Development Award NIH.</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="1973">1973</date><biblScope unit="volume">22</biblScope><biblScope unit="issue">20</biblScope><biblScope unit="page" from="2615">2615</biblScope><biblScope unit="page" to="2624">2624</biblScope></imprint><idno type="ISSN">0006-2952</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2952</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Aldehyde</term><term>Aldehyde reductase</term><term>Aldehyde reductase activity</term><term>Anticonvulsant</term><term>Anticonvulsant actions</term><term>Anticonvulsant activity</term><term>Anticonvulsant compounds</term><term>Assay system</term><term>Barbiturate</term><term>Bovine</term><term>Bovine brain aldehyde reductase</term><term>Bovine brain aldehyde reductase inhibition</term><term>Brain aldehyde reductase activity</term><term>Brain tissue</term><term>Derivative</term><term>Dimethadione</term><term>Diphenylhydantoin</term><term>Enzyme activity</term><term>Enzyme protein</term><term>Erwin</term><term>Ethosuximide</term><term>Ethotoin</term><term>Experimental conditions</term><term>Hydantoin</term><term>Inhibition</term><term>Inhibitor</term><term>Nadph</term><term>Nadph oxidation</term><term>Nmoles nadph</term><term>Noncompetitive</term><term>Pharmac</term><term>Phenobarbital</term><term>Reaction mixture</term><term>Reaction mixtures</term><term>Reductase</term><term>Sodium phosphate</term><term>Specific activity</term><term>Trimethadione</term><term>Variable substrate</term><term>Various anticonvulsants</term><term>Various barbiturates</term><term>Various compounds</term><term>Various inhibitors</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited in vitro by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>aldehyde</json:string><json:string>reductase</json:string><json:string>anticonvulsant</json:string><json:string>nadph</json:string><json:string>hydantoin</json:string><json:string>aldehyde reductase</json:string><json:string>dimethadione</json:string><json:string>ethosuximide</json:string><json:string>phenobarbital</json:string><json:string>trimethadione</json:string><json:string>inhibitor</json:string><json:string>diphenylhydantoin</json:string><json:string>ethotoin</json:string><json:string>pharmac</json:string><json:string>noncompetitive</json:string><json:string>enzyme activity</json:string><json:string>variable substrate</json:string><json:string>barbiturate</json:string><json:string>erwin</json:string><json:string>anticonvulsant actions</json:string><json:string>aldehyde reductase activity</json:string><json:string>anticonvulsant activity</json:string><json:string>derivative</json:string><json:string>inhibition</json:string><json:string>various anticonvulsants</json:string><json:string>enzyme protein</json:string><json:string>specific activity</json:string><json:string>nmoles nadph</json:string><json:string>sodium phosphate</json:string><json:string>nadph oxidation</json:string><json:string>bovine brain aldehyde reductase</json:string><json:string>brain aldehyde reductase activity</json:string><json:string>reaction mixtures</json:string><json:string>experimental conditions</json:string><json:string>various compounds</json:string><json:string>reaction mixture</json:string><json:string>various barbiturates</json:string><json:string>brain tissue</json:string><json:string>assay system</json:string><json:string>various inhibitors</json:string><json:string>anticonvulsant compounds</json:string><json:string>bovine brain aldehyde reductase inhibition</json:string><json:string>bovine</json:string></teeft></keywords><author><json:item><name>V. Gene Erwin</name></json:item><json:item><name>Richard A. Deitrich</name><affiliations><json:string>School of Pharmacy, University of Colorado, Boulder, Col. 80302, U.S.A.</json:string><json:string>Department of Pharmacology, University of Colorado Medical Center, Denver, Col. 80220, U.S.A.</json:string><json:string>†Recipient of Career Development Award NIH.</json:string></affiliations></json:item></author><articleId><json:string>73900701</json:string></articleId><arkIstex>ark:/67375/6H6-G879S1PK-H</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Abstract: The catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited in vitro by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. 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In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.</p></abstract></profileDesc><revisionDesc><change when="1973">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/D9C061695E6DC1300EA5AE9E05C1481FAC657C1A/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>73900701</aid><ce:pii>0006-2952(73)90070-1</ce:pii><ce:doi>10.1016/0006-2952(73)90070-1</ce:doi><ce:copyright type="unknown" year="1973"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was supported in part by Public Health Service Grants NIMH 18948, 18971 and 15908, National Institutes of Mental Health.</ce:note-para></ce:article-footnote><ce:title>Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds <ce:italic>in vitro</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>V.</ce:given-name><ce:surname>Gene Erwin</ce:surname></ce:author><ce:author><ce:given-name>Richard A.</ce:given-name><ce:surname>Deitrich</ce:surname><ce:cross-ref refid="AFF1"><ce:sup loc="post">a</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF2"><ce:sup loc="post">b</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>a</ce:label><ce:textfn>School of Pharmacy, University of Colorado, Boulder, Col. 80302, U.S.A.</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Department of Pharmacology, University of Colorado Medical Center, Denver, Col. 80220, U.S.A.</ce:textfn></ce:affiliation><ce:footnote id="FN1"><ce:label>†</ce:label><ce:note-para>Recipient of Career Development Award NIH.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="15" month="12" year="1972"></ce:date-received><ce:date-accepted day="30" month="3" year="1973"></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 catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited <ce:italic>in vitro</ce:italic> by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase <ce:italic>in vitro</ce:italic> paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (<ce:italic>K</ce:italic><ce:inf loc="post">i</ce:inf> values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10<ce:sup loc="post">−4</ce:sup> M, 1.7 × 10<ce:sup loc="post">−4</ce:sup> M, 4.7 × 10<ce:sup loc="post">−4</ce:sup> M and 5.5 × 10<ce:sup loc="post">−3</ce:sup> M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds in vitro</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Inhibition of bovine brain aldehyde reductase by anticonvulsant compounds</title></titleInfo><name type="personal"><namePart type="given">V.</namePart><namePart type="family">Gene Erwin</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Richard A.</namePart><namePart type="family">Deitrich</namePart><affiliation>School of Pharmacy, University of Colorado, Boulder, Col. 80302, U.S.A.</affiliation><affiliation>Department of Pharmacology, University of Colorado Medical Center, Denver, Col. 80220, U.S.A.</affiliation><affiliation>†Recipient of Career Development Award NIH.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1973</dateIssued><copyrightDate encoding="w3cdtf">1973</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The catalytic activity of partially purified NADPH-linked aldehyde reductase (alcohol: NADP oxidoreductase, EC 1.1.1.2) from bovine brain was markedly inhibited in vitro by anticonvulsant compounds. In general, the ability of these drugs to inhibit aldehyde reductase in vitro paralleled their anticonvulsant activity. Inhibition by various barbiturates, hydantoins or succinimides was non-competitive with either NADPH or aldehyde as the variable substrate, whereas the 2,4-oxazolidinediones produced a mixed type of inhibition. Inhibition by all ionizable compounds was found to vary with the pH of the reaction mixture, while the non-ionizable substances, paradione, trimethadione, methsuximide, 3-methyl-5-ethyl-5-phenylhydantoin, were not inhibitory. At pH 7.0 the inhibitor constants (Ki values) for phenobarbital, 5,5-diphenylhydantoin, 5,5-dimethyloxazolidinedione and ethosuximide were 1.2 × 10−4 M, 1.7 × 10−4 M, 4.7 × 10−4 M and 5.5 × 10−3 M respectively. The possibility that inhibition of brain NADPH-linked aldehyde reductase by these agents is concerned with their anticonvulsant actions is discussed.</abstract><note>This work was supported in part by Public Health Service Grants NIMH 18948, 18971 and 15908, National Institutes of Mental Health.</note><relatedItem type="host"><titleInfo><title>Biochemical Pharmacology</title></titleInfo><titleInfo type="abbreviated"><title>BCP</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">19731015</dateIssued></originInfo><identifier type="ISSN">0006-2952</identifier><identifier type="PII">S0006-2952(00)X0678-8</identifier><part><date>19731015</date><detail type="volume"><number>22</number><caption>vol.</caption></detail><detail type="issue"><number>20</number><caption>no.</caption></detail><extent unit="issue-pages"><start>2501</start><end>2644</end></extent><extent unit="pages"><start>2615</start><end>2624</end></extent></part></relatedItem><identifier type="istex">D9C061695E6DC1300EA5AE9E05C1481FAC657C1A</identifier><identifier type="ark">ark:/67375/6H6-G879S1PK-H</identifier><identifier type="DOI">10.1016/0006-2952(73)90070-1</identifier><identifier type="PII">0006-2952(73)90070-1</identifier><identifier type="ArticleID">73900701</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/D9C061695E6DC1300EA5AE9E05C1481FAC657C1A/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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