Serum Protein Electrophoretic Pattern in Experimental Myasthenia Gravis

Abstract

Myasthenia gravis (MG) is an antibody-mediated autoimmune neuromuscular disease, leading to skeletal muscle weakness. The autoantibodies are against acetylcholine receptor (AChR) of the muscle membrane localized at the neuromuscular junction. The early diagnosis of MG is a key factorfor the advanced medical practice, but, it still remains challenging. The objective of this pilot study was to examine the pattern of serum protein electrophoresis in the animal experimental model of MG. Acetylcholine receptor (AChR) was purified from rat (mail Wistar) leg muscle by affinity chromatography. Four rabbits were immunized on day 1, week 4 and week 8 with purified rat leg muscle AChR and assayed for serum anti-AChR antibody titer on blood samples taken on week 2, week 5 and week 9. Control rabbits received an emulsion of phosphate bufferded saline in the adjuant. The serum anti-AChR anybodies were tittered using quenching fluoroimmunoassay. Electrophoresis separation of the serum proteins was performed on a cellulose acetate membrane. Results showed that Immunizations of rabbits induced muscle weakness in the animals together with elevation of serum anti-AChR antibody. During the course of immunizations, percentage of beta-globulin fraction increased gradually from 15.8% to 41.2% whereas, albumin decreased from 68.3% to 43.8%. As determined by cellulose acetate electrophoresis. These results represent proof-of principle data for diagnosis of the acetylcholine receptor-MG subtypes and severity.