Specificity of adenosine deaminase inhibitors
Identifieur interne : 001764 ( Main/Exploration ); précédent : 001763; suivant : 001765Specificity of adenosine deaminase inhibitors
Auteurs : J. Frank Henderson [Canada] ; Larry Brox [Canada] ; George Zombor [Canada] ; Darel Hunting [Canada] ; Christopher A. Lomax [Canada]Source :
- 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
Affiliations:
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Le document en format XML
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Frank" last="Henderson">J. Frank Henderson</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta</wicri:regionArea><wicri:noRegion>Alberta</wicri:noRegion></affiliation></author><author><name sortKey="Brox, Larry" sort="Brox, Larry" uniqKey="Brox L" first="Larry" last="Brox">Larry Brox</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta</wicri:regionArea><wicri:noRegion>Alberta</wicri:noRegion></affiliation></author><author><name sortKey="Zombor, George" sort="Zombor, George" uniqKey="Zombor G" first="George" last="Zombor">George Zombor</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta</wicri:regionArea><wicri:noRegion>Alberta</wicri:noRegion></affiliation></author><author><name sortKey="Hunting, Darel" sort="Hunting, Darel" uniqKey="Hunting D" first="Darel" last="Hunting">Darel Hunting</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta</wicri:regionArea><wicri:noRegion>Alberta</wicri:noRegion></affiliation></author><author><name sortKey="Lomax, Christopher A" sort="Lomax, Christopher A" uniqKey="Lomax C" first="Christopher A." last="Lomax">Christopher A. Lomax</name><affiliation wicri:level="1"><country>Canada</country><wicri:regionArea>University of Alberta Cancer Research Unit (McEachern Laboratory) and Department of Biochemistry, Edmonton, Alberta</wicri:regionArea><wicri:noRegion>Alberta</wicri:noRegion></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="1977">1977</date><biblScope unit="volume">26</biblScope><biblScope unit="issue">21</biblScope><biblScope unit="page" from="1967">1967</biblScope><biblScope unit="page" to="1972">1972</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>Adenine</term><term>Adenine nucleotides</term><term>Adenosine</term><term>Adenosine deaminase</term><term>Adenosine deaminase inhibitors</term><term>Adenylate</term><term>Adenylate deaminase</term><term>Biochem</term><term>Coformycin</term><term>Cultured mouse lymphoma</term><term>Deaminase</term><term>Deamination</term><term>Deoxycoformycin</term><term>Ehna</term><term>Ehrlich ascites tumor cells</term><term>Glucose</term><term>Guanine</term><term>Guanine nucleotides</term><term>High concentrations</term><term>Hypoxanthine</term><term>Inhibitor</term><term>Intact cells</term><term>Methotrexate</term><term>Nucleotide</term><term>Nucleotide synthesis</term><term>Purine</term><term>Purine biosynthesis</term><term>Purine metabolism</term><term>Radioactive adenine</term><term>Radioactive adenosine</term><term>Radioactive glycine</term><term>Radioactive hypoxanthine</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml: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.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Henderson, J Frank" sort="Henderson, J Frank" uniqKey="Henderson J" first="J. Frank" last="Henderson">J. Frank Henderson</name></noRegion><name sortKey="Brox, Larry" sort="Brox, Larry" uniqKey="Brox L" first="Larry" last="Brox">Larry Brox</name><name sortKey="Hunting, Darel" sort="Hunting, Darel" uniqKey="Hunting D" first="Darel" last="Hunting">Darel Hunting</name><name sortKey="Lomax, Christopher A" sort="Lomax, Christopher A" uniqKey="Lomax C" first="Christopher A." last="Lomax">Christopher A. Lomax</name><name sortKey="Zombor, George" sort="Zombor, George" uniqKey="Zombor G" first="George" last="Zombor">George Zombor</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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