Immunostaining of motor nerve terminals by IgM M protein with activity against gangliosides GM1 and GD1b from a patient with motor neuron disease.
We demonstrated the binding of an IgM monoclonal protein, obtained from a patient with motor neuron disease, with known antibody activity against gangliosides GM1, GD1b, and asialo GM1, to neuromuscular junctions in guinea pig gastrocnemius muscle, using an indirect immunofluorescence technique. Staining disappeared after delipidation of muscle sections. Denervated muscle sections showed no labeling at the neuromuscular junction after incubation with the patient's serum. This indicates presynaptic binding of the IgM M protein and supports the concept that IgM monoclonal antibody to nerve terminal determinants may underlie a motor neuron disorder.
Schluep
M
M
Department of Neurology, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.
Steck
A J
AJ
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D005455:Fluorescent Antibody Technique; D005677:G(M1) Ganglioside / Q000276:immunology; D005732:Gangliosides / Q000276:immunology*; D006168:Guinea Pigs; D006801:Humans; D007075:Immunoglobulin M / Q000276:immunology*; D009046:Motor Neurons; D009468:Neuromuscular Diseases / Q000276:immunology*; D009469:Neuromuscular Junction / Q000276:immunology*; D013194:Staining and Labeling
D000911:Antibodies, Monoclonal; D005732:Gangliosides; D007075:Immunoglobulin M; C033851:ganglioside, GD1b; D005677:G(M1) Ganglioside