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Characterisation, Density, and Distribution of Kainate Receptors in Normal and Alzheimer's Diseased Human Brain
Author(s) -
Cowburn Richard F.,
Hardy John A.,
Briggs Roger S.,
Roberts Peter J.
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb10908.x
Subject(s) - kainate receptor , kainic acid , alzheimer's disease , receptor , human brain , glutamate receptor , hippocampal formation , glutamatergic , neuroscience , biology , population , medicine , chemistry , endocrinology , biochemistry , ampa receptor , disease , environmental health
The specific binding of [ 3 H]kainic acid was investigated in membrane preparations from human parietal cortex obtained postmortem. Saturation studies revealed that binding occurred to a single population of sites with a K D of 15 n M and a B max of 110 fmol/mg of protein. The kinetically determined dissociation constant for these sites agreed well with that obtained from saturation analyses. Pharmacological characterisation of these sites gave a profile consistent with those reported for kainate receptor sites in animal brain. The integrity of kainate receptors was studied in several brain regions from six patients who had died of Alzheimer's disease and from six closely matched control subjects. No change in either the affinity or the number of kainate receptors was seen in any of the regions studied, despite the loss of neo‐cortical and hippocampal glutamatergic terminals in the Alzheimer's diseased brains, as previously reported.