Nilasena D S, Trieu E P, Targoff I N
Veterans Affairs Medical Center, Salt Lake City, Utah.
Arthritis Rheum. 1995 Jan;38(1):123-8. doi: 10.1002/art.1780380119.
To determine the biochemical structure and antigenic components of Mi-2 autoantigen, the target of autoantibodies in 15-20% of dermatomyositis patients.
Immunoprecipitation from 35S-labeled HeLa cell extract, immunoblotting, and purification from bovine thymus by immunoaffinity chromatography.
All 46 sera that had anti-Mi-2 autoantibodies demonstrated by immunodiffusion immunoprecipitated a major protein of approximately 240 kd. Additional proteins of 200, 150, 72, 65, 63, 50, and 34 kd appeared to be part of the antigen. Fractions of purified bovine Mi-2 with antigenic activity showed high molecular weight bands comparable with immunoprecipitated HeLa Mi-2. Twenty-four of 47 anti-Mi-2 positive sera reacted with the 240-kd protein by immunoblot against anti-Mi-2 immunoprecipitates.
Mi-2 antigen consists of multiple proteins, of which the 240-kd protein appears to be the major reactive component.