Immunological and pharmacological heterogeneity of alpha-bungarotoxin binding sites extracted from TE671 cells

J Neuroimmunol. 1988 Aug;19(1-2):149-57. doi: 10.1016/0165-5728(88)90044-6.

Abstract

A proportion of the acetylcholine receptors (AChR) extracted from the human medulloblastoma cell line, TE671, differed pharmacologically and immunologically from AChR extracted from ischaemic human calf muscle (HCM). 29.6% (mean value) of the total 125I-alpha-bungarotoxin (alpha-BuTx) binding sites in the TE671 extracts was not inhibited by d-tubocurarine (dTC). Three of five monoclonal antibodies (m.abs), all of which precipitated greater than 80% of HCM AChRs, precipitated less than 55% of the total TE671 AChR. However, myasthenia gravis sera bound to TE671, and TE671 cell surface AChRs appeared to be similar to that of HCM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / immunology
  • Autoantibodies / immunology
  • Binding Sites
  • Binding, Competitive
  • Bungarotoxins / metabolism*
  • Chemical Precipitation
  • Humans
  • Myasthenia Gravis / immunology*
  • Receptors, Nicotinic / drug effects
  • Receptors, Nicotinic / immunology*
  • Tubocurarine / metabolism
  • Tumor Cells, Cultured

Substances

  • Antibodies, Monoclonal
  • Autoantibodies
  • Bungarotoxins
  • Receptors, Nicotinic
  • Tubocurarine