( 3H)dipyridamole and ( 3H)nitrobenzylthioinosine binding sites at the human parietal cortex and erythrocyte adenosine transporter: A comparison
We compared the binding sites of the adenosine transport inhibitors ( 3H)dipyridamole (DPR) and ( 3H)nitrobenzylthioinosine (NBI) in human parietal cortex and erythrocytes. In comparison with guinea pig ( 3H)DPR marked only slightly more binding sites than ( 3H)NBI with a Bmax of 1080±29 and 780±7 f...
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| Veröffentlicht in: | Life sciences (1973) 1994, Vol.55 (21), p.1675-1682 |
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| container_title | Life sciences (1973) |
| container_volume | 55 |
| creator | Deckert, Jürgen Hennemann, Anja Bereznai, Benjamin Fritze, Jürgen Vock, Reinhard Marangos, Paul J. Riederer, Peter |
| description | We compared the binding sites of the adenosine transport inhibitors (
3H)dipyridamole (DPR) and (
3H)nitrobenzylthioinosine (NBI) in human parietal cortex and erythrocytes. In comparison with guinea pig (
3H)DPR marked only slightly more binding sites than (
3H)NBI with a Bmax of 1080±29 and 780±7 fmol/mg protein respectively in parietal cortex and 24288±2725 and 20875±1905 fmol/mg protein respectively in erythrocytes. NBI displaced (
3H)DPR binding completely from its binding sites at about K
D/2 concentrations in parietal cortex as well as erythrocytes with inhibition constants comparable to its dissociation constants. Lineweaver-Burke analysis in erythrocytes indicated a competitive inhibition of (
3H)DPR binding by NBI. Pharmacological characterization of (
3H)DPR binding sites in human erythrocytes is consistent with their localization on adenosine transporters. These findings provide evidence that as opposed to guinea pig (
3H)DPR and (
3H)NBI largely label binding sites to the same adenosine transporter in human erythrocytes and parietal cortex. |
| doi_str_mv | 10.1016/0024-3205(94)00276-2 |
| format | Article |
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3H)dipyridamole (DPR) and (
3H)nitrobenzylthioinosine (NBI) in human parietal cortex and erythrocytes. In comparison with guinea pig (
3H)DPR marked only slightly more binding sites than (
3H)NBI with a Bmax of 1080±29 and 780±7 fmol/mg protein respectively in parietal cortex and 24288±2725 and 20875±1905 fmol/mg protein respectively in erythrocytes. NBI displaced (
3H)DPR binding completely from its binding sites at about K
D/2 concentrations in parietal cortex as well as erythrocytes with inhibition constants comparable to its dissociation constants. Lineweaver-Burke analysis in erythrocytes indicated a competitive inhibition of (
3H)DPR binding by NBI. Pharmacological characterization of (
3H)DPR binding sites in human erythrocytes is consistent with their localization on adenosine transporters. These findings provide evidence that as opposed to guinea pig (
3H)DPR and (
3H)NBI largely label binding sites to the same adenosine transporter in human erythrocytes and parietal cortex.</description><identifier>ISSN: 0024-3205</identifier><identifier>EISSN: 1879-0631</identifier><identifier>DOI: 10.1016/0024-3205(94)00276-2</identifier><identifier>PMID: 7968243</identifier><language>eng</language><publisher>Netherlands: Elsevier Inc</publisher><subject>( 3H)dipyridamole ; ( 3H)nitrobenzylthioinosine ; Adenosine - metabolism ; adenosine transporter ; Binding Sites ; Binding, Competitive ; Biological Transport ; Dipyridamole - metabolism ; erythrocyte ; Erythrocytes - metabolism ; Humans ; parietal cortex ; Parietal Lobe - metabolism ; Thioinosine - analogs & derivatives ; Thioinosine - metabolism</subject><ispartof>Life sciences (1973), 1994, Vol.55 (21), p.1675-1682</ispartof><rights>1994</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-748b7b3379238b32d02b0bf56d5240588f57a39550b3b27870fc4bf31cb38fc53</citedby><cites>FETCH-LOGICAL-c357t-748b7b3379238b32d02b0bf56d5240588f57a39550b3b27870fc4bf31cb38fc53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0024320594002762$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27900,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7968243$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Deckert, Jürgen</creatorcontrib><creatorcontrib>Hennemann, Anja</creatorcontrib><creatorcontrib>Bereznai, Benjamin</creatorcontrib><creatorcontrib>Fritze, Jürgen</creatorcontrib><creatorcontrib>Vock, Reinhard</creatorcontrib><creatorcontrib>Marangos, Paul J.</creatorcontrib><creatorcontrib>Riederer, Peter</creatorcontrib><title>( 3H)dipyridamole and ( 3H)nitrobenzylthioinosine binding sites at the human parietal cortex and erythrocyte adenosine transporter: A comparison</title><title>Life sciences (1973)</title><addtitle>Life Sci</addtitle><description>We compared the binding sites of the adenosine transport inhibitors (
3H)dipyridamole (DPR) and (
3H)nitrobenzylthioinosine (NBI) in human parietal cortex and erythrocytes. In comparison with guinea pig (
3H)DPR marked only slightly more binding sites than (
3H)NBI with a Bmax of 1080±29 and 780±7 fmol/mg protein respectively in parietal cortex and 24288±2725 and 20875±1905 fmol/mg protein respectively in erythrocytes. NBI displaced (
3H)DPR binding completely from its binding sites at about K
D/2 concentrations in parietal cortex as well as erythrocytes with inhibition constants comparable to its dissociation constants. Lineweaver-Burke analysis in erythrocytes indicated a competitive inhibition of (
3H)DPR binding by NBI. Pharmacological characterization of (
3H)DPR binding sites in human erythrocytes is consistent with their localization on adenosine transporters. These findings provide evidence that as opposed to guinea pig (
3H)DPR and (
3H)NBI largely label binding sites to the same adenosine transporter in human erythrocytes and parietal cortex.</description><subject>( 3H)dipyridamole</subject><subject>( 3H)nitrobenzylthioinosine</subject><subject>Adenosine - metabolism</subject><subject>adenosine transporter</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Biological Transport</subject><subject>Dipyridamole - metabolism</subject><subject>erythrocyte</subject><subject>Erythrocytes - metabolism</subject><subject>Humans</subject><subject>parietal cortex</subject><subject>Parietal Lobe - metabolism</subject><subject>Thioinosine - analogs & derivatives</subject><subject>Thioinosine - metabolism</subject><issn>0024-3205</issn><issn>1879-0631</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1q3DAUhUVpSSbTvkEDWpVk4UaWLMvuohBC_iCQTbIW-rnuqNiSK2lKnafoI8eeGbLM6qJ7zzkXfRehryX5XpKyviCEVgWjhJ-11fn8EHVBP6BV2Yi2IDUrP6LVm-QYnaT0mxDCuWBH6Ei0dUMrtkL_zzC7O7dunKKzagg9YOUt3nW9yzFo8C9TnzcuOB-S84C189b5Xzi5DAmrjPMG8GY7KI9HFR1k1WMTYoZ_uyiIU97EYKY8R1s4hOSofBoXVfyBL2f9sHhT8J_Rp071Cb4c6ho931w_Xd0VD4-391eXD4VhXORCVI0WmjHRUtZoRi2hmuiO15bTivCm6bhQrOWcaKapaATpTKU7VhrNms5wtkbf9rljDH-2kLIcXDLQ98pD2CYpZkAtnzmuUbUXmhhSitDJMbpBxUmWRC6HkAtluVCWbSV3h5B0tp0e8rd6APtmOpCf5z_3c5g_-ddBlMk48Aasi2CytMG9v-AVns-ZBQ</recordid><startdate>1994</startdate><enddate>1994</enddate><creator>Deckert, Jürgen</creator><creator>Hennemann, Anja</creator><creator>Bereznai, Benjamin</creator><creator>Fritze, Jürgen</creator><creator>Vock, Reinhard</creator><creator>Marangos, Paul J.</creator><creator>Riederer, Peter</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1994</creationdate><title>( 3H)dipyridamole and ( 3H)nitrobenzylthioinosine binding sites at the human parietal cortex and erythrocyte adenosine transporter: A comparison</title><author>Deckert, Jürgen ; Hennemann, Anja ; Bereznai, Benjamin ; Fritze, Jürgen ; Vock, Reinhard ; Marangos, Paul J. ; Riederer, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-748b7b3379238b32d02b0bf56d5240588f57a39550b3b27870fc4bf31cb38fc53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>( 3H)dipyridamole</topic><topic>( 3H)nitrobenzylthioinosine</topic><topic>Adenosine - metabolism</topic><topic>adenosine transporter</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Biological Transport</topic><topic>Dipyridamole - metabolism</topic><topic>erythrocyte</topic><topic>Erythrocytes - metabolism</topic><topic>Humans</topic><topic>parietal cortex</topic><topic>Parietal Lobe - metabolism</topic><topic>Thioinosine - analogs & derivatives</topic><topic>Thioinosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Deckert, Jürgen</creatorcontrib><creatorcontrib>Hennemann, Anja</creatorcontrib><creatorcontrib>Bereznai, Benjamin</creatorcontrib><creatorcontrib>Fritze, Jürgen</creatorcontrib><creatorcontrib>Vock, Reinhard</creatorcontrib><creatorcontrib>Marangos, Paul J.</creatorcontrib><creatorcontrib>Riederer, Peter</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Life sciences (1973)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Deckert, Jürgen</au><au>Hennemann, Anja</au><au>Bereznai, Benjamin</au><au>Fritze, Jürgen</au><au>Vock, Reinhard</au><au>Marangos, Paul J.</au><au>Riederer, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>( 3H)dipyridamole and ( 3H)nitrobenzylthioinosine binding sites at the human parietal cortex and erythrocyte adenosine transporter: A comparison</atitle><jtitle>Life sciences (1973)</jtitle><addtitle>Life Sci</addtitle><date>1994</date><risdate>1994</risdate><volume>55</volume><issue>21</issue><spage>1675</spage><epage>1682</epage><pages>1675-1682</pages><issn>0024-3205</issn><eissn>1879-0631</eissn><abstract>We compared the binding sites of the adenosine transport inhibitors (
3H)dipyridamole (DPR) and (
3H)nitrobenzylthioinosine (NBI) in human parietal cortex and erythrocytes. In comparison with guinea pig (
3H)DPR marked only slightly more binding sites than (
3H)NBI with a Bmax of 1080±29 and 780±7 fmol/mg protein respectively in parietal cortex and 24288±2725 and 20875±1905 fmol/mg protein respectively in erythrocytes. NBI displaced (
3H)DPR binding completely from its binding sites at about K
D/2 concentrations in parietal cortex as well as erythrocytes with inhibition constants comparable to its dissociation constants. Lineweaver-Burke analysis in erythrocytes indicated a competitive inhibition of (
3H)DPR binding by NBI. Pharmacological characterization of (
3H)DPR binding sites in human erythrocytes is consistent with their localization on adenosine transporters. These findings provide evidence that as opposed to guinea pig (
3H)DPR and (
3H)NBI largely label binding sites to the same adenosine transporter in human erythrocytes and parietal cortex.</abstract><cop>Netherlands</cop><pub>Elsevier Inc</pub><pmid>7968243</pmid><doi>10.1016/0024-3205(94)00276-2</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0024-3205 |
| ispartof | Life sciences (1973), 1994, Vol.55 (21), p.1675-1682 |
| issn | 0024-3205 1879-0631 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76829506 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | ( 3H)dipyridamole ( 3H)nitrobenzylthioinosine Adenosine - metabolism adenosine transporter Binding Sites Binding, Competitive Biological Transport Dipyridamole - metabolism erythrocyte Erythrocytes - metabolism Humans parietal cortex Parietal Lobe - metabolism Thioinosine - analogs & derivatives Thioinosine - metabolism |
| title | ( 3H)dipyridamole and ( 3H)nitrobenzylthioinosine binding sites at the human parietal cortex and erythrocyte adenosine transporter: A comparison |
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