Characterisation, density, and distribution of kainate receptors in normal and Alzheimer's diseased human brain.
The specific binding of [3H]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 KD of 15 nM and a Bmax 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 neocortical and hippocampal glutamatergic terminals in the Alzheimer's diseased brains, as previously reported.
Cowburn
R F
RF
Department of Biochemistry and Molecular Genetics, St. Mary's Hospital Medical School, London, England.
Hardy
J A
JA
Briggs
R S
RS
Roberts
P J
PJ
D000328:Adult; D000368:Aged; D000544:Alzheimer Disease / Q000378:metabolism*; D001921:Brain / Q000378:metabolism*; D006801:Humans; D007608:Kainic Acid / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008875:Middle Aged; D018092:Kainic Acid Receptors; D016194:Receptors, N-Methyl-D-Aspartate; D017981:Receptors, Neurotransmitter / Q000378:metabolism*
D007608:Kainic Acid; D018092:Kainic Acid Receptors; D016194:Receptors, N-Methyl-D-Aspartate; D017981:Receptors, Neurotransmitter