PMID: 6167329Jul 27, 1981Paper

Immunochemical properties of junctional and extrajunctional acetylcholine receptor

Brain Research
D S DwyerG E Kemp

Abstract

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.

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Citations

Nov 1, 1988·Journal of the Neurological Sciences·S KawanamiM A Raftery
Jun 1, 1988·Journal of Neuroimmunology·J P O'MalleyJ J Bray
Sep 1, 1990·Journal of Neuroimmunology·S Nelson, B M Conti-Tronconi
Jan 1, 1984·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·B HoltonJ P Changeux
Jan 1, 1985·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·G M TurnbullG G Lunt
Apr 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·S M SchuetzeZ W Hall
Jul 21, 1998·Annals of the New York Academy of Sciences·H J Kaminski
Apr 13, 2000·Annual Review of Entomology·R F Chapman
Aug 1, 1994·The Journal of Clinical Investigation·B Vernet-der GarabedianJ F Bach
Mar 10, 2015·Developmental Biology·Hwee Li YeoChi Wai Lee
Jan 1, 1987·Annals of the New York Academy of Sciences·Z W HallS M Schuetze

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