Immunochemical properties of junctional and extrajunctional acetylcholine receptor.
Immunological assays were performed to compare two distinct forms of the nicotinic acetylcholine receptor (AChR): junctional (JR) and extrajunctional receptor (EJR). Antibodies from myasthenia gravis patients' sera inhibited the binding of [125I]alpha-bungarotoxin (BGT), to EJR more effectively than binding to JR. Immunological differences between JR and EJR were confirmed by other assay methods. In all cases, EJR appeared to have antigenic determinants not found on JR. It was established that enzymatic removal of carbohydrates from EJR caused it to more closely resemble JR. Thus differences between JR and EJR may be due, in part, to carbohydrate residues found on EJR that are absent on JR. The extent of antibody binding to EJR was examined by gel filtration methods. Immunochemical studies of bands from SDS gels showed that antibodies are present in myasthenic serum which react with the 3 subunits (42, 53, 64 kdaltons) of AChR to varying degrees.
D000109:Acetylcholine / Q000276:immunology*; D000818:Animals; D000906:Antibodies / Q000276:immunology; D002038:Bungarotoxins / Q000378:metabolism; D000939:Epitopes; D006801:Humans; D007074:Immunoglobulin G / Q000032:analysis; D009045:Motor Endplate / Q000276:immunology*; D009121:Muscle Denervation; D009132:Muscles / Q000294:innervation; D009157:Myasthenia Gravis / Q000276:immunology; D009469:Neuromuscular Junction / Q000276:immunology*; D051381:Rats; D011950:Receptors, Cholinergic / Q000276:immunology*; D011978:Receptors, Nicotinic / Q000276:immunology*; D013570:Synaptic Membranes / Q000276:immunology*
D000906:Antibodies; D002038:Bungarotoxins; D000939:Epitopes; D007074:Immunoglobulin G; D011950:Receptors, Cholinergic; D011978:Receptors, Nicotinic; D000109:Acetylcholine