Nicotinic acetylcholine receptor subtypes in rat superior cervical ganglion neurons as studied by sequential application of two α-subunit-specific antibodies

• Published in: Neuroscience letters Vol. 303; no. 1; pp. 37 - 40
• Main Authors: Voitenko, Larisa P., Voitenko, Sergey V., Skok, Marina V., Purnyn, Helen E., Skok, Vladimir I.
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier Ireland Ltd 27.04.2001; Elsevier
• Subjects: Acetylcholine - pharmacology; alpha7 Nicotinic Acetylcholine Receptor; Animals; Antibodies - metabolism; Antibodies, Monoclonal - metabolism; Biological and medical sciences; Cells, Cultured; Double immunostaining; Fundamental and applied biological sciences. Psychology; Medicin och hälsovetenskap; Neurons - drug effects; Neurons - metabolism; Nicotinic acetylcholine receptor; Peripheral nervous system. Autonomic nervous system. Neuromuscular transmission. Ganglionic transmission. Electric organ; Rats; Receptors, Nicotinic - drug effects; Receptors, Nicotinic - metabolism; Subunit-specific antibodies; Superior Cervical Ganglion - drug effects; Superior Cervical Ganglion - metabolism; Sympathetic ganglia; Vasodilator Agents - pharmacology; Vertebrates: nervous system and sense organs; Double immunostaining; Sympathetic ganglia; Nicotinic acetylcholine receptor; Subunit-specific antibodies; Cholinergic receptor; Vertebrata; Mammalia; Rat; Autonomic nervous system; Antibody; Rodentia; Superior cervical ganglion; Sympathetic nervous system; Subunit; In vitro; Nicotinic receptor
• ISSN: 0304-3940; 1872-7972
• DOI: 10.1016/S0304-3940(01)01705-0

All cultured neurons of rat superior cervical ganglion (SCG) were stained with nicotinic acetylcholine receptor (nAChR) α5- or α7-subunit-specific oligoclonal antibodies (Abs) and could additionally bind α3-subunit-specific monoclonal antibody (mAb). About 60% of the neurons were stained with α4-specific Ab and could not bind α3-specific mAb. The acetylcholine-induced membrane currents recorded with the whole-cell patch clamp method and partially blocked with α3-specific mAbs, could be additionally blocked with α5- and α7- specific Abs, and vice versa. The results suggest that: (1) each neuron of rat SCG expresses several nAChR subtypes with different α-subunits; (2) the α3-, α5- and α7-subunit-containing nAChRs are probably located far enough from each other thus enabling joint binding to the cell of the corresponding α-subunit specific Abs, in contrast to the α4-subunit-containing nAChRs which are probably located too close to the α3-containing ones to allow their joint binding.