rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
4
|
pubmed:dateCreated |
1990-3-14
|
pubmed:abstractText |
1. [3H]-idazoxan labels a single population of high affinity sites (Kd 2.26 +/- 0.02 nM; Bmax 372 +/- 25 fmol mg-1 protein) in hamster adipocyte membranes. In the presence of 1 microM yohimbine to preclude binding to alpha 2-adrenoceptors, the density of [3H]-idazoxan binding sites was reduced (287 +/- 18 fmol mg-1 protein) without an apparent decrease in the affinity (Kd 2.19 +/- 0.24 nM) of the radioligand. 2. Displacement studies indicate that alpha-adrenoceptor ligands with an imidazoline side chain completely inhibit [3H]-idazoxan binding to hamster adipocyte membranes; in contrast, the alpha 2-adrenoceptor antagonists yohimbine, rauwolscine, BDF 6143 and phentolamine inhibited only 20-30% of the specific binding with affinity values consistent with an interaction at alpha 2-adrenoceptors. 3. The low potency of noradrenaline and adrenaline in displacing [3H]-idazoxan binding to the second site on hamster adipocyte membranes indicates that it is unlikely that this site is a type of adrenoceptor. 4. These results suggest that [3H]-idazoxan binds with high affinity to two sites in hamster adipocytes: an alpha 2-adrenoceptor and a non-adrenoceptor imidazoline site.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-14169133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-189821,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-2885406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-2889454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-2906613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-2987483,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2558757-7401933
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0007-1188
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
98
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1143-50
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2558757-Adipose Tissue,
pubmed-meshheading:2558757-Animals,
pubmed-meshheading:2558757-Binding, Competitive,
pubmed-meshheading:2558757-Cerebral Cortex,
pubmed-meshheading:2558757-Cricetinae,
pubmed-meshheading:2558757-Dioxanes,
pubmed-meshheading:2558757-Dioxins,
pubmed-meshheading:2558757-Idazoxan,
pubmed-meshheading:2558757-Imidazoline Receptors,
pubmed-meshheading:2558757-Kinetics,
pubmed-meshheading:2558757-Male,
pubmed-meshheading:2558757-Mesocricetus,
pubmed-meshheading:2558757-Rats,
pubmed-meshheading:2558757-Rats, Inbred Strains,
pubmed-meshheading:2558757-Receptors, Adrenergic, alpha,
pubmed-meshheading:2558757-Receptors, Drug
|
pubmed:year |
1989
|
pubmed:articleTitle |
[3H]-idazoxan binds with high affinity to two sites on hamster adipocytes: an alpha 2-adrenoceptor and a non-adrenoceptor site.
|
pubmed:affiliation |
Department of Pharmacology, Syntex Research Centre, Heriot-Watt University Research Park, Riccarton, Edinburgh.
|
pubmed:publicationType |
Journal Article,
In Vitro
|