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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-2-26
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pubmed:abstractText |
[3H]Kainate bound to chick cerebellar membranes with a KD of 0.6 microM and with an exceptionally high Bmax of 165 pmol/mg of protein. In octylglucoside-solubilised extracts, the affinity of [3H]kainate was reduced (KD = 2.7 microM), but the Bmax was relatively unchanged (130 pmol/mg of protein). The rank potency of competitive ligands was domoate greater than kainate greater than 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) greater than glutamate. Binding sites for alpha-[3H]amino-3- hydroxy-5-methylisoxazolepropionate ([3H]AMPA) were much less abundant, with KD and Bmax values in membranes of 86 nM and 1 pmol/mg of protein, respectively. The affinity of [3H]AMPA binding was also reduced on solubilisation (KD = 465 nM), but there was an increase in the Bmax (1.7 pmol/mg of protein). Quisqualate and CNQX were the most effective displacers of [3H]AMPA binding, but kainate was also a relatively potent inhibitor. However, in contrast to the displacement profile for [3H]kainate, domoate was markedly less potent than kainate at displacing [3H]AMPA. These results suggest that [3H]AMPA binds to a small subset of the kainate sites that, unlike the majority of the [3H]kainate binding protein, which has been reported to be located in the Bergmann glia, may represent neuronal unitary non-N-methyl-D-aspartate receptors.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glucosides,
http://linkedlifedata.com/resource/pubmed/chemical/Ibotenic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Kainic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Kainic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Neurotransmitter,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Amino-3-hydroxy-5-methyl-4-iso...,
http://linkedlifedata.com/resource/pubmed/chemical/domoic acid,
http://linkedlifedata.com/resource/pubmed/chemical/octyl-beta-D-glucoside
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
702-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1846403-Animals,
pubmed-meshheading:1846403-Binding, Competitive,
pubmed-meshheading:1846403-Cell Membrane,
pubmed-meshheading:1846403-Cerebellum,
pubmed-meshheading:1846403-Chickens,
pubmed-meshheading:1846403-Glucosides,
pubmed-meshheading:1846403-Ibotenic Acid,
pubmed-meshheading:1846403-Kainic Acid,
pubmed-meshheading:1846403-Receptors, AMPA,
pubmed-meshheading:1846403-Receptors, Kainic Acid,
pubmed-meshheading:1846403-Receptors, Neurotransmitter,
pubmed-meshheading:1846403-Solubility,
pubmed-meshheading:1846403-alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Comparison of solubilised kainate and alpha-amino-3-hydroxy-5- methylisoxazolepropionate binding sites in chick cerebellum.
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pubmed:affiliation |
Molecular Neurobiology Unit, MRC Centre, Cambridge, England.
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pubmed:publicationType |
Journal Article,
Comparative Study
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