Identification of beta-actin as a candidate autoantigen in autoimmune inner ear disease.
(2000) Clinical Otolaryngology and Allied Sciences — Vol. 25, n° 6, p. 535-541 (2000)
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- Abstract
- It has been shown that sera from patients with autoimmune inner ear disease contain antibodies to several inner ear antigens. We report here the characterization of the 42-43 kDa protein against which a significant number of patients' sera react strongly. After separation of inner ear proteins from guinea-pig cochleas by SDS-PAGE, the band corresponding to the 42-43 kDa protein was digested with trypsin and the peptide fragments were separated by high-performance liquid chromatography. Two fractions were then subjected to amino acid sequencing by the classical automated Edman degradation. The sequence of a stretch of 15 amino acids of the first fragment was identical to that of amino acids 148-162 of beta-actin. The sequence of the 10 amino acids of the second fragment was also identical to beta-actin. On Western blots, monoclonal antibody directed against beta-actin reacted with the inner ear 42-43 kDa proteins. The serum samples from the patients and the monoclonal antibody reacted with the non-muscle actin used as antigen in Western blotting. Immunoblot analysis of inner ear proteins after two-dimensional gel electrophoresis showed a spot, corresponding to the region of the 43 kDa as compared to the protein standards. On the basis of these data it is concluded that the target 42-43 kDa protein for antibodies in sera of patients with autoimmune inner ear disease is beta-actin, a molecule, which has important and numerous functions inside cells. This is the first report to identify the cytoskeletal protein beta-actin as a candidate autoantigen in autoimmune inner ear disease.
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Boulassel, M. R., Tomasi, JP., Deggouj, N., & Gersdorff, M. (2000). Identification of beta-actin as a candidate autoantigen in autoimmune inner ear disease. Clinical Otolaryngology and Allied Sciences, 25(6), 535-541. https://doi.org/10.1046/j.1365-2273.2000.00416.x (Original work published 2000)