Evidence for the existence of high affinity binding sites for indomethacin on human blood platelets
Using human blood-washed platelets and [3H]indomethacin, we demonstrated the presence of saturable, time- and temperature-dependent high affinity binding sites for non-steroidal anti-inflammatory drugs. The observed Kd value for indomethacin was 5 nM. Structural specificity of the non-steroidal anti...
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| Veröffentlicht in: | Molecular pharmacology 1986-01, Vol.29 (1), p.39-44 |
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| container_title | Molecular pharmacology |
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| creator | MAGOUS, R BALI, J.-P ESCALE, R GIRARD, J.-P RECHENCQ, E ROSSI, J.-C |
| description | Using human blood-washed platelets and [3H]indomethacin, we demonstrated the presence of saturable, time- and temperature-dependent
high affinity binding sites for non-steroidal anti-inflammatory drugs. The observed Kd value for indomethacin was 5 nM. Structural
specificity of the non-steroidal anti-inflammatory drug site was studied with arylacetic acids, anthranilic acids, and compounds
from other chemical families. Arylacetic acid drugs had affinities which were similar to the affinity of indomethacin. Affinity
differences among the other drugs may be related to the presence or absence of the lipophilic substituent on the central ring.
As expected, anti-inflammatory pyrrazole derivatives, aspirin, bucloxic acid, cortisol, nordihydroguaiaretic acid, and the
chemotactic peptide formyl-Met-Leu-Phe were not recognized by the indomethacin binding site. |
| format | Article |
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high affinity binding sites for non-steroidal anti-inflammatory drugs. The observed Kd value for indomethacin was 5 nM. Structural
specificity of the non-steroidal anti-inflammatory drug site was studied with arylacetic acids, anthranilic acids, and compounds
from other chemical families. Arylacetic acid drugs had affinities which were similar to the affinity of indomethacin. Affinity
differences among the other drugs may be related to the presence or absence of the lipophilic substituent on the central ring.
As expected, anti-inflammatory pyrrazole derivatives, aspirin, bucloxic acid, cortisol, nordihydroguaiaretic acid, and the
chemotactic peptide formyl-Met-Leu-Phe were not recognized by the indomethacin binding site.</description><identifier>ISSN: 0026-895X</identifier><identifier>EISSN: 1521-0111</identifier><identifier>PMID: 3945226</identifier><identifier>CODEN: MOPMA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Pharmacology and Experimental Therapeutics</publisher><subject>Anti-Inflammatory Agents - pharmacology ; Binding Sites ; Binding, Competitive ; Biological and medical sciences ; Blood Platelets - analysis ; Bones, joints and connective tissue. Antiinflammatory agents ; Humans ; In Vitro Techniques ; indomethacin ; Indomethacin - blood ; man ; Medical sciences ; Molecular Conformation ; Pharmacology. Drug treatments ; platelets ; Receptors, Drug - analysis ; Structure-Activity Relationship ; Tritium</subject><ispartof>Molecular pharmacology, 1986-01, Vol.29 (1), p.39-44</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8815675$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3945226$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MAGOUS, R</creatorcontrib><creatorcontrib>BALI, J.-P</creatorcontrib><creatorcontrib>ESCALE, R</creatorcontrib><creatorcontrib>GIRARD, J.-P</creatorcontrib><creatorcontrib>RECHENCQ, E</creatorcontrib><creatorcontrib>ROSSI, J.-C</creatorcontrib><title>Evidence for the existence of high affinity binding sites for indomethacin on human blood platelets</title><title>Molecular pharmacology</title><addtitle>Mol Pharmacol</addtitle><description>Using human blood-washed platelets and [3H]indomethacin, we demonstrated the presence of saturable, time- and temperature-dependent
high affinity binding sites for non-steroidal anti-inflammatory drugs. The observed Kd value for indomethacin was 5 nM. Structural
specificity of the non-steroidal anti-inflammatory drug site was studied with arylacetic acids, anthranilic acids, and compounds
from other chemical families. Arylacetic acid drugs had affinities which were similar to the affinity of indomethacin. Affinity
differences among the other drugs may be related to the presence or absence of the lipophilic substituent on the central ring.
As expected, anti-inflammatory pyrrazole derivatives, aspirin, bucloxic acid, cortisol, nordihydroguaiaretic acid, and the
chemotactic peptide formyl-Met-Leu-Phe were not recognized by the indomethacin binding site.</description><subject>Anti-Inflammatory Agents - pharmacology</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Blood Platelets - analysis</subject><subject>Bones, joints and connective tissue. Antiinflammatory agents</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>indomethacin</subject><subject>Indomethacin - blood</subject><subject>man</subject><subject>Medical sciences</subject><subject>Molecular Conformation</subject><subject>Pharmacology. Drug treatments</subject><subject>platelets</subject><subject>Receptors, Drug - analysis</subject><subject>Structure-Activity Relationship</subject><subject>Tritium</subject><issn>0026-895X</issn><issn>1521-0111</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAYhIso67r6E4QcxFshSZsmOcqyfsCCFwVv5W36dhtpk9pk1f33rmvRo6eBmWfmMEfJnAnOUsoYO07mlPIiVVq8nCZnIbxSynKh6CyZZToXnBfzxKzebY3OIGn8SGKLBD9tiAfHN6S1m5ZA01hn445U1tXWbUiwEcOhsDd8j7EFYx3xjrTbHhypOu9rMnQQscMYzpOTBrqAF5Mukufb1dPyPl0_3j0sb9Zpy7WIqRHSsMaoGhQwZEpqwysj0GRQSACFolKyQiMNlZqLvJIKdQVCZbkUDepskVz_7A6jf9tiiGVvg8GuA4d-G0pZFJpyxf4FWZ5lNGdyD15O4LbqsS6H0fYw7srpvn1-NeUQDHTNCM7Y8IspxUQhxR_2feeHHbEcWhh7ML7zm13Jdcn2k9kXM3iHwQ</recordid><startdate>19860101</startdate><enddate>19860101</enddate><creator>MAGOUS, R</creator><creator>BALI, J.-P</creator><creator>ESCALE, R</creator><creator>GIRARD, J.-P</creator><creator>RECHENCQ, E</creator><creator>ROSSI, J.-C</creator><general>American Society for Pharmacology and Experimental Therapeutics</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19860101</creationdate><title>Evidence for the existence of high affinity binding sites for indomethacin on human blood platelets</title><author>MAGOUS, R ; BALI, J.-P ; ESCALE, R ; GIRARD, J.-P ; RECHENCQ, E ; ROSSI, J.-C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h295t-c57c1fc8da8a1e1879c2bc5ec3a67aa8e5b87bec7c079254b78e9ba583475fe93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Anti-Inflammatory Agents - pharmacology</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Blood Platelets - analysis</topic><topic>Bones, joints and connective tissue. Antiinflammatory agents</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>indomethacin</topic><topic>Indomethacin - blood</topic><topic>man</topic><topic>Medical sciences</topic><topic>Molecular Conformation</topic><topic>Pharmacology. Drug treatments</topic><topic>platelets</topic><topic>Receptors, Drug - analysis</topic><topic>Structure-Activity Relationship</topic><topic>Tritium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MAGOUS, R</creatorcontrib><creatorcontrib>BALI, J.-P</creatorcontrib><creatorcontrib>ESCALE, R</creatorcontrib><creatorcontrib>GIRARD, J.-P</creatorcontrib><creatorcontrib>RECHENCQ, E</creatorcontrib><creatorcontrib>ROSSI, J.-C</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MAGOUS, R</au><au>BALI, J.-P</au><au>ESCALE, R</au><au>GIRARD, J.-P</au><au>RECHENCQ, E</au><au>ROSSI, J.-C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence for the existence of high affinity binding sites for indomethacin on human blood platelets</atitle><jtitle>Molecular pharmacology</jtitle><addtitle>Mol Pharmacol</addtitle><date>1986-01-01</date><risdate>1986</risdate><volume>29</volume><issue>1</issue><spage>39</spage><epage>44</epage><pages>39-44</pages><issn>0026-895X</issn><eissn>1521-0111</eissn><coden>MOPMA3</coden><abstract>Using human blood-washed platelets and [3H]indomethacin, we demonstrated the presence of saturable, time- and temperature-dependent
high affinity binding sites for non-steroidal anti-inflammatory drugs. The observed Kd value for indomethacin was 5 nM. Structural
specificity of the non-steroidal anti-inflammatory drug site was studied with arylacetic acids, anthranilic acids, and compounds
from other chemical families. Arylacetic acid drugs had affinities which were similar to the affinity of indomethacin. Affinity
differences among the other drugs may be related to the presence or absence of the lipophilic substituent on the central ring.
As expected, anti-inflammatory pyrrazole derivatives, aspirin, bucloxic acid, cortisol, nordihydroguaiaretic acid, and the
chemotactic peptide formyl-Met-Leu-Phe were not recognized by the indomethacin binding site.</abstract><cop>Bethesda, MD</cop><pub>American Society for Pharmacology and Experimental Therapeutics</pub><pmid>3945226</pmid><tpages>6</tpages></addata></record> |
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| ispartof | Molecular pharmacology, 1986-01, Vol.29 (1), p.39-44 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Anti-Inflammatory Agents - pharmacology Binding Sites Binding, Competitive Biological and medical sciences Blood Platelets - analysis Bones, joints and connective tissue. Antiinflammatory agents Humans In Vitro Techniques indomethacin Indomethacin - blood man Medical sciences Molecular Conformation Pharmacology. Drug treatments platelets Receptors, Drug - analysis Structure-Activity Relationship Tritium |
| title | Evidence for the existence of high affinity binding sites for indomethacin on human blood platelets |
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