Specificity of adenosine deaminase inhibitors
Identifieur interne : 000235 ( Istex/Corpus ); précédent : 000234; suivant : 000236Specificity of adenosine deaminase inhibitors
Auteurs : J. Frank Henderson ; Larry Brox ; George Zombor ; Darel Hunting ; Christopher A. LomaxSource :
- Biochemical Pharmacology [ 0006-2952 ] ; 1977.
English descriptors
- Teeft :
- Adenine, Adenine nucleotides, Adenosine, Adenosine deaminase, Adenosine deaminase inhibitors, Adenylate, Adenylate deaminase, Biochem, Coformycin, Cultured mouse lymphoma, Deaminase, Deamination, Deoxycoformycin, Ehna, Ehrlich ascites tumor cells, Glucose, Guanine, Guanine nucleotides, High concentrations, Hypoxanthine, Inhibitor, Intact cells, Methotrexate, Nucleotide, Nucleotide synthesis, Purine, Purine biosynthesis, Purine metabolism, Radioactive adenine, Radioactive adenosine, Radioactive glycine, Radioactive hypoxanthine.
Abstract
Abstract: The specificity of the potent adenosine deaminase inhibitors deoxycoformycin (covidarabine), coformycin and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), has been assessed in Ehrlich ascites tumor cells in vitro and in cultured mouse lymphoma L5178Y cells. EHNA is both less potent an inhibitor of adenosine deaminase than deoxycoformycin, and is less specific. High concentrations of deoxycoformycin and EHNA inhibit all pathways of purine ribonucleotide synthesis, and inhibit the conversion of inosinate to adenine and guanine nucleotides. These drugs also inhibit purified adenylate deaminase, but inhibition of this enzyme in intact cells can only be detected at high rates of deamination of adenylate. Deoxycoformycin potentiates the toxicity of adenine against cultured cells.
Url:
DOI: 10.1016/0006-2952(77)90003-X
Links to Exploration step
ISTEX:04E2D61B0B178806D73D8EF08ED293B2724C76AALe document en format XML
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Frank Henderson</name><affiliation><mods:affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</mods:affiliation></affiliation></author><author><name sortKey="Brox, Larry" sort="Brox, Larry" uniqKey="Brox L" first="Larry" last="Brox">Larry Brox</name><affiliation><mods:affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</mods:affiliation></affiliation></author><author><name sortKey="Zombor, George" sort="Zombor, George" uniqKey="Zombor G" first="George" last="Zombor">George Zombor</name><affiliation><mods:affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</mods:affiliation></affiliation></author><author><name sortKey="Hunting, Darel" sort="Hunting, Darel" uniqKey="Hunting D" first="Darel" last="Hunting">Darel Hunting</name><affiliation><mods:affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</mods:affiliation></affiliation></author><author><name sortKey="Lomax, Christopher A" sort="Lomax, Christopher A" uniqKey="Lomax C" first="Christopher A." last="Lomax">Christopher A. 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EHNA is both less potent an inhibitor of adenosine deaminase than deoxycoformycin, and is less specific. High concentrations of deoxycoformycin and EHNA inhibit all pathways of purine ribonucleotide synthesis, and inhibit the conversion of inosinate to adenine and guanine nucleotides. These drugs also inhibit purified adenylate deaminase, but inhibition of this enzyme in intact cells can only be detected at high rates of deamination of adenylate. 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Alberta, Canada T6G 2H7</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Larry</forename><surname>Brox</surname></persName><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation></author><author xml:id="author-0002"><persName><forename type="first">George</forename><surname>Zombor</surname></persName><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation></author><author xml:id="author-0003"><persName><forename type="first">Darel</forename><surname>Hunting</surname></persName><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation></author><author xml:id="author-0004"><persName><forename type="first">Christopher 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to="1972">1972</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1977</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: The specificity of the potent adenosine deaminase inhibitors deoxycoformycin (covidarabine), coformycin and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), has been assessed in Ehrlich ascites tumor cells in vitro and in cultured mouse lymphoma L5178Y cells. EHNA is both less potent an inhibitor of adenosine deaminase than deoxycoformycin, and is less specific. High concentrations of deoxycoformycin and EHNA inhibit all pathways of purine ribonucleotide synthesis, and inhibit the conversion of inosinate to adenine and guanine nucleotides. These drugs also inhibit purified adenylate deaminase, but inhibition of this enzyme in intact cells can only be detected at high rates of deamination of adenylate. Deoxycoformycin potentiates the toxicity of adenine against cultured cells.</p></abstract></profileDesc><revisionDesc><change when="1977">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-M8G46M8M-Q/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>7790003X</aid><ce:pii>0006-2952(77)90003-X</ce:pii><ce:doi>10.1016/0006-2952(77)90003-X</ce:doi><ce:copyright type="unknown" year="1977"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was supported by the National Cancer Institute and Medical Research Council of Canada.</ce:note-para></ce:article-footnote><ce:title>Specificity of adenosine deaminase inhibitors</ce:title><ce:author-group><ce:author><ce:given-name>J.Frank</ce:given-name><ce:surname>Henderson</ce:surname></ce:author><ce:author><ce:given-name>Larry</ce:given-name><ce:surname>Brox</ce:surname></ce:author><ce:author><ce:given-name>George</ce:given-name><ce:surname>Zombor</ce:surname></ce:author><ce:author><ce:given-name>Darel</ce:given-name><ce:surname>Hunting</ce:surname></ce:author><ce:author><ce:given-name>Christopher A.</ce:given-name><ce:surname>Lomax</ce:surname></ce:author><ce:affiliation><ce:textfn>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="31" month="12" year="1976"></ce:date-received><ce:date-accepted day="25" month="2" year="1977"></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 specificity of the potent adenosine deaminase inhibitors deoxycoformycin (covidarabine), coformycin and <ce:italic>erythro</ce:italic>-9-(2-hydroxy-3-nonyl)adenine (EHNA), has been assessed in Ehrlich ascites tumor cells <ce:italic>in vitro</ce:italic> and in cultured mouse lymphoma L5178Y cells. EHNA is both less potent an inhibitor of adenosine deaminase than deoxycoformycin, and is less specific. High concentrations of deoxycoformycin and EHNA inhibit all pathways of purine ribonucleotide synthesis, and inhibit the conversion of inosinate to adenine and guanine nucleotides. These drugs also inhibit purified adenylate deaminase, but inhibition of this enzyme in intact cells can only be detected at high rates of deamination of adenylate. Deoxycoformycin potentiates the toxicity of adenine against cultured cells.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Specificity of adenosine deaminase inhibitors</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Specificity of adenosine deaminase inhibitors</title></titleInfo><name type="personal"><namePart type="given">J.Frank</namePart><namePart type="family">Henderson</namePart><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Larry</namePart><namePart type="family">Brox</namePart><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">George</namePart><namePart type="family">Zombor</namePart><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Darel</namePart><namePart type="family">Hunting</namePart><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Christopher A.</namePart><namePart type="family">Lomax</namePart><affiliation>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta, Canada T6G 2H7</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">1977</dateIssued><copyrightDate encoding="w3cdtf">1977</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Abstract: The specificity of the potent adenosine deaminase inhibitors deoxycoformycin (covidarabine), coformycin and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA), has been assessed in Ehrlich ascites tumor cells in vitro and in cultured mouse lymphoma L5178Y cells. EHNA is both less potent an inhibitor of adenosine deaminase than deoxycoformycin, and is less specific. High concentrations of deoxycoformycin and EHNA inhibit all pathways of purine ribonucleotide synthesis, and inhibit the conversion of inosinate to adenine and guanine nucleotides. These drugs also inhibit purified adenylate deaminase, but inhibition of this enzyme in intact cells can only be detected at high rates of deamination of adenylate. Deoxycoformycin potentiates the toxicity of adenine against cultured cells.</abstract><note>This work was supported by the National Cancer Institute and Medical Research Council of Canada.</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">1977</dateIssued></originInfo><identifier type="ISSN">0006-2952</identifier><identifier type="PII">S0006-2952(00)X0737-X</identifier><part><date>1977</date><detail type="volume"><number>26</number><caption>vol.</caption></detail><detail type="issue"><number>21</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1955</start><end>2090</end></extent><extent unit="pages"><start>1967</start><end>1972</end></extent></part></relatedItem><identifier type="istex">04E2D61B0B178806D73D8EF08ED293B2724C76AA</identifier><identifier type="ark">ark:/67375/6H6-M8G46M8M-Q</identifier><identifier type="DOI">10.1016/0006-2952(77)90003-X</identifier><identifier type="PII">0006-2952(77)90003-X</identifier><identifier type="ArticleID">7790003X</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/ark:/67375/6H6-M8G46M8M-Q/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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