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• W1985959968 abstract "M1 muscarinic acetylcholine receptor (M1AchR)–G protein coupling, as measured by high-affinity agonist binding, was examined in membranes prepared from postmortem human temporal cortex (Brodmann area 38) from individuals with Alzheimer's disease (AD, n = 8) and age-matched controls (n = 6). Binding competitions between the M1AchR-selective antagonist [3H]pirenzepine ([3H]PZ) and muscarinic agonists carbachol, acetylcholine, oxotremorine, and oxotremorine M were conducted. In the presence of 1 mM MgCl2, the inhibition of [3H]PZ binding by carbachol, acetylcholine, or oxotremorine M was best described by a two-affinity state model for control and AD cases, while oxotremorine binding affinity was best fit to a single-state model. Although both control and AD groups had similar KD values for the high- and low-affinity agonist binding sites, the proportion of M1AchRs exhibiting high affinity for carbachol and acetylcholine was reduced by 48 and 33%, respectively, in AD membranes relative to controls (P < 0.05). No changes in the binding of the oxotremorine M or oxotremorine were noted. The nonhydrolyzable guanine nucleotide GppNHp (100μM) reduced the proportion of M1AchRs with high affinity for agonists in both control and AD membranes. Substitution of 1 mM MnCl2 for MgCl2 restored high-affinity carbachol binding at the M1AchR in AD membranes similar to that seen in controls. In the presence of 1 mM MnCl2, agonist binding in controls did not differ from 1 mM MgCl2. In the absence of cations (1 mM EDTA), no differences between control and AD M1AchR carbachol binding were observed. Thus, the loss of high-affinity agonist binding at the M1AchR in AD is dependent on the agonist and cation studied." @default.
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• W1985959968 date "1999-08-01" @default.
• W1985959968 modified "2023-10-16" @default.
• W1985959968 title "Reduced High-Affinity Agonist Binding at the M1 Muscarinic Receptor in Alzheimer's Disease Brain: Differential Sensitivity to Agonists and Divalent Cations" @default.
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• W1985959968 doi "https://doi.org/10.1006/exnr.1999.7116" @default.
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