The target antigen identification at dilated cardiomyopathy

Authors

  • V. I. Bobyk Institute of Molecular Biology and Genetics, NAS of Ukraine 150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 Author
  • T. V. Kovenya Institute of Molecular Biology and Genetics, NAS of Ukraine 150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 Author
  • O. M. Fedorkova Institute of Molecular Biology and Genetics, NAS of Ukraine 150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 Author
  • V. M. Danilova Petr Bogach Institute of Physiology Taras Shevchenko National University of Kyiv 2 corp 12, Academika Glushkova Ave Str., Kyiv, Ukraine, 03022 Author
  • V. S. Tregubov Petr Bogach Institute of Physiology Taras Shevchenko National University of Kyiv 2 corp 12, Academika Glushkova Ave Str., Kyiv, Ukraine, 03022 Author
  • D. V. Ryabenko M. D. Strazhesko Institute of Cardiology, MAS of Ukraine 5, Narodnogo Opolchennya Str., Kyiv, Ukraine, 03151 Author
  • L. L. Sidorik Institute of Molecular Biology and Genetics, NAS of Ukraine 150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680 Author

DOI:

https://doi.org/10.7124/bc.0006BC

Abstract

Identification of target antigen at autoimmune pathologies is based on the use of immunological approaches such as ELISA and Western blot analysis. To determine the antigen at dilated cardiomyopathy (DCM) which is a severe autoimmune cardiospecific pathology of unknown origin we have studied the level of specific antibodies against myosin. The panel of blood sera from healthy donors and DCM patients has been screened in ELISA using as antigen myosins purified from the myocardia of healthy donors and DCM patients. We have observed that the level of antimyosin antibodies in sera of DCM patients is significantly higher then in sera of healthy donors. The comparative analysis of immune response against heavy and light chains of myosins revealed that heavy chain of DCM myosin were the most immunogenic. For the first time we have demonstrated that heavy chain of DCM myosin is a target antigen at dilated cardiomyopathy.

References

Goldman JH, McKenna WJ. Immunopathogenesis of dilated cardiomyopathies. Curr Opin Cardiol. 1995;10(3):306-11.

Limas CJ. Cardiac autoantibodies in dilated cardiomyopathy: a pathogenetic role? Circulation. 1997;95(8):1979-80.

Sidorik L. L., Rodnin N. V., Bobyk V. I., Ryabenko D. V., Veberov A. V., Tkachenko T. Yu., Matsuka G. Kh. Investigation of autoantibodies directed against tissue-specific myocardial antigens in dilated cardiomyopathy. Biopolym. Cell. 1995; 11(1):81-86.

Caforio AL, Grazzini M, Mann JM, Keeling PJ, Bottazzo GF, McKenna WJ, Schiaffino S. Identification of alpha- and beta-cardiac myosin heavy chain isoforms as major autoantigens in dilated cardiomyopathy. Circulation. 1992;85(5):1734-42.

Bobik V. I., Veberov A. V., Ryabenko D. V., Dubrovskaya G. V., Rodnin N. V., Sidorik L. L. The purification of the main tissue-specific antigens from the normal and effected by dilatative cardiomyopathia human heart. Biopolym. Cell. 1993; 9(6):63-66

Practical protein chemistry. Ed. A. Dubro. Moscow, Mir. 1989; 623 p.

Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.

Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-54.

Matsiota P, Druet P, Dosquet P, Guilbert B, Avrameas S. Natural autoantibodies in systemic lupus erythematosus. Clin Exp Immunol. 1987;69(1):79-88.

Knowlton AA, Kapadia S, Torre-Amione G, Durand JB, Bies R, Young J, Mann DL. Differential expression of heat shock proteins in normal and failing human hearts. J Mol Cell Cardiol. 1998;30(4):811-8.

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Published

2004-07-20

Issue

Vol. 20 No. 4 (2004)

Section

Short Communications