Abstract
The nicotinic acetylcholine receptor (AChR) is a neurotransmitter receptor which, upon acetylcholine binding, undergoes a conformational change which triggers ion permeability by opening a self contained cation channel. AChR is present in muscle end plates, in ganglia and in CNS, with different structural and functional characteristics. The most complete information on structure and function are available for AChR of skeletal muscles and fish electric organs. In these organs AChR is a membrane complex of approximately 300 KDa composed by four protein subunits α, ß, γ, δ, (Conti-Tronconi and Raftery, 1982 Popot and Changeux, 1984). In the functional receptor five subunits (α2, ß, γ, δ) are arranged with pseudo-five-fold symmetry around the central cation conducting channel. Of the five subunits only the two α-subunits bind acetylcholine and cholinergic agents. Nicotinic acetylcholine receptors are found in many areas of the central nervous system (CNS) and pharmacological studies suggest that they could be divided in subtypes (Wonnacott, 1987)- However, the number of AChR subtypes, their relationship to each other, the role they play in the various areas of the CNS are still controversial.
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Sher, E., Gotti, C., Fornasari, D., Chini, B., Ogando, A.E., Clementi, F. (1988). Human Neuroblastoma Cells: An in Vitro Model for the Study of Mammalian Neuronal Nicotinic Receptors. In: Zimmermann, H. (eds) Cellular and Molecular Basis of Synaptic Transmission. NATO ASI Series, vol 21. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73172-3_33
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