| pubmed-article:9048968 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0205464 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0290799 | lld:lifeskim |
| pubmed-article:9048968 | lifeskim:mentions | umls-concept:C0599278 | lld:lifeskim |
| pubmed-article:9048968 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:9048968 | pubmed:dateCreated | 1997-4-1 | lld:pubmed |
| pubmed-article:9048968 | pubmed:abstractText | The ligand binding characteristics of the recombinant human 5-HT1A receptor stably expressed in a Chinese Hamster Ovary (CHO) cell line are described using a selective agonist, [3H]8-OH-DPAT, and a novel antagonist radioligand, [3H]WAY-100635. The association of [3H]WAY-100635 was a time- and temperature-dependent process. Mn2+ > Ca2+ > Mg2+ reduced the specific [3H]WAY-100635 binding in a concentration-dependent manner, whereas Na+ and K+ were ineffective. Scatchard analyses revealed a homogeneous population of [3H]WAY-100635 recognition sites (Kd = 0.32 nM; Bmax = 162 fmol/mg of protein). Addition of divalent cations to the incubation medium produced a two-fold decrease in the binding affinity of [3H]WAY-100635 with no significant change in Bmax; GTP gamma S had no effect on Kd or Bmax parameters. [3H]WAY-100635 displayed a higher affinity (2-3 fold) for the 5-HT1A site when compared with [3H] 8-OH-DPAT binding under similar incubation conditions. Furthermore, [3H] 8-OH-DPAT labelled approximately 53-61% of total 5-HT1A sites recognised by [3H]WAY-100635. The competition binding profiles of [3H]WAY-100635 and [3H]8-OH-DPAT were highly correlated and consistent with the recognition of 5-HT1A receptors. Agonist competition curves with [3H]WAY-100635 were best-resolved into high- and low-affinity binding states, whereas partial agonist and antagonist curves were best-fit to one-site binding models. A significant correlation between the respective affinities of a range of agonists and antagonists at recombinant human and rodent hippocampal 5-HT1A binding sites (previously published) was also observed using [3H]WAY-100635 (r = 0.92; P < 0.0005) and [3H]8-OH-DPAT (r = 0.96; P < 0.0005). The availability of a novel, high-affinity antagonist radioligand, [3H]WAY-100635, will provide a useful tool for the further characterisation of 5-HT1A receptor pharmacology. | lld:pubmed |
| pubmed-article:9048968 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9048968 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9048968 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9048968 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9048968 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9048968 | pubmed:issn | 0024-3205 | lld:pubmed |
| pubmed-article:9048968 | pubmed:author | pubmed-author:EnnioGG | lld:pubmed |
| pubmed-article:9048968 | pubmed:author | pubmed-author:MinchinM CMC | lld:pubmed |
| pubmed-article:9048968 | pubmed:author | pubmed-author:KhawajaXX | lld:pubmed |
| pubmed-article:9048968 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9048968 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:9048968 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9048968 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9048968 | pubmed:pagination | 653-65 | lld:pubmed |
| pubmed-article:9048968 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:9048968 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9048968 | pubmed:articleTitle | Pharmacological characterization of recombinant human 5-hydroxytryptamine1A receptors using a novel antagonist radioligand, [3H]WAY-100635. | lld:pubmed |
| pubmed-article:9048968 | pubmed:affiliation | Wyeth-Ayerst Research, Princeton, New Jersey 08543-8000, USA. khawajx@war.wyeth.com | lld:pubmed |
| pubmed-article:9048968 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9048968 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9048968 | pubmed:publicationType | In Vitro | lld:pubmed |
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