Autoantibodies to the heat-shock protein hsp90 in systemic lupus erythematosus.
Patients with systemic lupus erythematosus (SLE) develop multiple autoantibodies to self-antigens. Analysis of autoantibody systems in this and related autoimmune disorders can provide information of etiologic and pathogenetic significance. We report here a previously unrecognized autoantibody to the 90,000-D heat-shock protein, hsp90, a molecule thought to have important functions in the cellular response to stress, virus-induced transformation, steroid hormone receptor action, and cellular activation. Autoantibodies to hsp90 were exclusively of the IgG class, and were detected in approximately 50% of unselected patients with SLE and 2/6 patients with idiopathic polymyositis. Anti-hsp90 antibodies were not detected in sera from 10 normal subjects, 10 patients with rheumatoid arthritis, or 7 patients with scleroderma. The identity of this major intracytoplasmic antigen was established by its specific removal from nonionic detergent cell lysates following immunoabsorption with monospecific rabbit anti-hsp90, and by demonstration of increased synthesis following a 10-min 45 degrees C heat shock. These data define the frequent occurrence of a novel autoantibody to a major heat-shock protein in patients with SLE.
Minota
S
S
Division of Rheumatology and Immunology, University of North Carolina, Chapel Hill 27514.
Koyasu
S
S
Yahara
I
I
Winfield
J
J
D001323:Autoantibodies / Q000032:analysis*; D001324:Autoantigens / Q000032:analysis* / Q000276:immunology; D006360:Heat-Shock Proteins / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000032:analysis; D008180:Lupus Erythematosus, Systemic / Q000276:immunology*; D008970:Molecular Weight
D001323:Autoantibodies; D001324:Autoantigens; D006360:Heat-Shock Proteins; D007074:Immunoglobulin G