Journal
EUROPEAN JOURNAL OF PHARMACOLOGY
Volume 445, Issue 3, Pages 153-161Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-2999(02)01750-8
Keywords
nicotinic acetylcholine receptor; alpha 7 subunit; perforated patch-clamp; PC12 cell; GH4C1 cell; recombinant expression
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The pharmacological properties of the rat alpha7 nicotinic acetylcholine receptor endogenously expressed in PC12 cells and recombinantly expressed in GH4Cl cells (alpha7-GH4C1 cells) were characterized and compared. Patch-clamp recordings demonstrated that activation by choline and block by methyllycaconitine and dihydro-beta-erythroidine were similar, but block by mecamylamine was different. Whereas in alpha7-GH4C1 cells the inhibition curve for mecamylamine was monophasic (IC50 of 1.6 muM), it was biphasic in PC12 cells (IC50 values of 341 nM and 9.6 muM). The same rank order of potency was obtained for various nicotinic agonists, while acetylcholine was 3.7-fold less potent and 1.5-fold more effective in PC12 cells. Dihydro-beta-erythroidine differentially blocked acetylcholine-evoked cur-rents in both systems. Since reverse transcriptase polymerase chain reaction (RT-PCR) experiments revealed expression of alpha3, alpha4, alpha5, alpha7 and beta4 subunits in PC12 cells, whereas GH4C1 cells express only the beta4 subunit, our results suggest that more than one form of alpha7 containing heteromeric nicotinic receptors might be functionally expressed in PC12 cells. (C) 2002 Elsevier Science B.V. All rights reserved.
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