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J Neurophysiol 90: 3295-3303, 2003. First published July 23, 2003; doi:10.1152/jn.00512.2003
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Characterization of Neuronal Nicotinic Acetylcholine Receptors in the Membrane of Unmyelinated Human C-Fiber Axons by In Vitro Studies

P. M. Lang1,2, R. Burgstahler1, W. Sippel1, D. Irnich2, B. Schlotter-Weigel3 and P. Grafe1

Departments of 1Physiology and 2Anesthesiology and 3Friedrich-Baur-Institute, Ludwig-Maximilians University, 80336 Munich, Germany

Submitted 28 May 2003; accepted in final form 18 July 2003

Application of acetylcholine to peripheral nerve terminals in the skin is a widely used test in studies of human small-fiber functions. However, a detailed pharmacological profile and the subunit composition of nicotinic acetylcholine receptors in human C-fiber axons are not known. In the present study, we recorded acetylcholine-induced changes of the excitability and of the intracellular Ca2+ concentration in C-fiber axons of isolated human nerve segments. In addition, using immunohistochemistry, an antibody of a subtype of nicotinic acetylcholine receptor was tested. Acetylcholine and agonists reduced the current necessary for the generation of action potentials in C fibers by <=30%. This increase in axonal excitability was accompanied by a rise in the free intracellular Ca2+ concentration. The following rank order of potency for agonists was found: epibatidine >> 5-Iodo-A-85380 > 1,1-dimethyl-4-phenylpiperazinium iodide > nicotine > cytisine > acetylcholine; choline had no effect. The epibatidine-induced increase in axonal excitability was blocked by mecamylamine and, less efficiently, by methyllycacontine and dihydro-{beta}-erythroidine. Many C-fiber axons were labeled by an antibody that recognizes the {alpha}5 subunit of nicotinic acetylcholine receptors. In summary, electrophysiological and immunohistochemical data indicate the functional expression of nicotinic acetylcholine receptors composed of {alpha}3, {alpha}5, and {beta}4 but not of {alpha}4/{beta}2 or of {alpha}7 subunits in the axonal membrane of unmyelinated human C fibers. In addition, the observations suggest that the axonal membrane of C fibers in isolated segments of human sural nerve can be used as a model for presumed cholinergic chemosensitivity of axonal terminals.

Address for reprint requests and other correspondence: P. Grafe, Dept. of Physiology, University of Munich, Pettenkoferstr. 12, 80336 Munich, Germany (E-mail: P.Grafe{at}lrz.uni-muenchen.de).




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