Tryptophanyl-tRNA synthetase as a human autoantigen.
Autoantibodies to highly purified tryptophanyl-tRNA synthetase, consisting of two approximately 60-kDa subunits (6.1.1.2, TrpRS), were detected in some sera of donors and patients with various diagnosis using the newly developed 125I-TrpRS-radiodot, 125I-TrpRS-radioblot, ELISA and Western immunoblotting. The percentage of positive sera appears to be dependent upon the method of sera testing. The autoimmune sera recognized both the native and denatured TrpRS forms. The binding of the human serum to the 60-kDa band of tissue extract was demonstrable by the 125I-TrpRS-blot as well as Western blot techniques. The possible role of infections in the induction of anti-TrpRS antibodies and maintenance of the autoimmune response is discussed.
Paley
E L
EL
George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
Alexandrova
N
N
Smelansky
L
L
D000595:Amino Acid Sequence; D000818:Animals; D001323:Autoantibodies / Q000276:immunology*; D001324:Autoantigens / Q000276:immunology*; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D006801:Humans; D015151:Immunoblotting; D007457:Iodine Radioisotopes; D008969:Molecular Sequence Data; D011247:Pregnancy; D011817:Rabbits; D014369:Tryptophan-tRNA Ligase / Q000276:immunology*
D001323:Autoantibodies; D001324:Autoantigens; D007457:Iodine Radioisotopes; D014369:Tryptophan-tRNA Ligase