Biopolym. Cell. 2010; 26(5):373-377.
Structure and Function of Biopolymers
Identification of autoantibodies to tyrosil-tRNA synthetase in heart disfunctions
1, 2Kondratiuk Iu. Iu., 1Sidorik L. L., 1Bobyk V. I., 3Ryabenko D. V., 1Kornelyuk A. I.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Taras Shevchenko National University of Kyiv
    64, Volodymyrska Str., Kyiv, Ukraine, 01601
  3. National Scientific Center "M. D. Strazhesko Institute of Cardiology, MAS of Ukraine"
    5, Narodnogo Opolchennya Str., Kyiv, Ukraine, 03151


Aim. To investigate the levels of specific autoantibodies against tyrosyl-tRNA synthetase and its individual modules in the blood serum of people with heart failure caused by dilated cardiomyopathy, myocarditis and ischemic heart disease compared with healthy donors. Methods. Recombinant proteins were obtained using bacterial strains transformed with appropriate plasmid vectors and were purified by chromatography on Ni-NTA-agarose. The levels of specific autoantibodies were investigated by ELISA. Results. The increased levels of autoantibodies specific to tyrosyl- tRNA synthetase, its N-terminal catalytic module and non-catalytic C-module, were found in the blood serum of patients, compared with healthy donors. Conclusions. The results obtained demonstrate the possible role of tyrosyl-tRNA synthetase in adaptive changes of the myocardium in response to stress factors.
Keywords: autoantibodies, tyrosyl-tRNA synthetase, heart failure


[1] Cleland J. G. F., Khand A., Clark A. The heart failure epidemic: exactly how big is it? Eur. Heart J 2001 22, N 8:623–626.
[2] Dos Remedios C. G., Liew C. C., Allen P. D., Winslow R. L., Van Eyk J. E., Dunn M. J. Genomics, proteomics and bioinformatics of human heart failure J. Muscle Res. Cell Motil 2003 24, N 4–6:251–260.
[3] Rose N. R., Neumann D. A., Herskowitz A. Autoimmune myocarditis: concepts and questions Immunol. Today 1991 12, N 8:253–255.
[4] Fu M., Matsui S. Is cardiomyopathy an autoimmune disease? Keio J. Med 2002 4, N 51:208–212.
[5] Ibba M., Francklyn Ch., Cusak S. The aminoacyl-tRNA synthetases Georgetown: Landes Biosci., 2005 437 p.
[6] Park S. G., Schimmel P., Kim S. Aminoacyl-tRNA synthetases and their connections to disease Proc. Nat. Acad. Sci. USA 2008 105, N 32:11043–11049.
[7] Schimmel P. Development of tRNA synthetases and connection to genetic code and disease Protein Sci 2008 17, N 10:1643–1652.
[8] Mathews M. B., Bernstein R. M. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity Nature 1983 304, N 5922:177–179.
[9] Howard O. M., Dong H. F., Yang D., Raben N., Rosen A., Casciola-Rosen L., Hartlein M., Kron M., Yang D., Yiadom K., Dwivedi S., Plotz P. H., Oppenheimet J. J. Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells J. Exp. Med 2002 196, N 6:781–791.
[10] Mathews M. B., Reichlin M., Hughes G. R., Bernstein R. M. Anti-threonyl-tRNA synthetase, a second myositis-related autoantibody J. Exp. Med 1984 160, N 2:420–434.
[11] Hirakata M., SuwaA., Nagai S., Kron M. A., Trieu E. P., Mimori T., Akizuki M., Targoff I. N. Anti-KS: Identification of autoantibodies to asparaginyl-tRNA synthetase associated with interstitial lung disease. J. Immunol. 1999; 162, N 4:2315–2320.
[12] Sidorik L. L., Rodnin N. V., Savinskaya L. A., Ribkinskaya T. A., Rozhko O. T., Kornelyuk O. I., Matsuka G. Kh. Autoantibodies directed against tyrosyl-tRNA synthetase modulate its aminoacylating activity. Biopolym. Cell. 1996; 12, N 5:21–28.
[13] Betteridge Z., Gunawardena1 H., North1 J., Slinn J., Mc Hugh1 N. Anti-synthetase syndrome: a new autoantibody to phenylalanyl transfer RNA synthetase (anti-Zo) associated with polymyositis and interstitial pneumonia Rheumatology 2007 46, N 6:1005–1008.
[14] Maniatis T., Fritsch E. F., Sambrook J. Molecular cloning: a laboratory manual New York: Cold Spring Harbor Lab. publ., 1982 545 p.
[15] Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970 277, N 259:680–685.
[16] Ribkinska T. A., Kornelyuk O. I., Beresten S. F., Matsuka G. Kh. The immunochemical approach for studies of structure tyrosyl-tRNA synthetase from bovine liver. Biopolym. Cell. 1991; 7, N 5:33–37.
[17] Sidorik L. L. The protein biosynthesis and autoimmunity. Biopolym. Cell. 1992; 8, N 4:3–19.
[18] Wakasugi K., Schimmel P. Two distinct cytokines released from a human aminoacyl-tRNA synthetase Science 1999 284, N 5411:147-151.
[19] Kornelyuk A. I., Tas M. P., Dubrovsky A., Murray C. J. Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase Biopolym. Cell 1999 15, N 2:168–172.
[20] Ivakhno S. S., Kornelyuk A. I. Cytokine-like activities of some aminoacyl-tRNA synthetases and auxiliary p43 cofactor of aminoacylation reaction and their role in oncogenesis. Exp. Oncol. 2004; 26, N 4. P. 250–255.
[21] Guo M., Schimmel P., Yang X.-L. Functional expansion of human tRNA synthetases achieved by structural inventios FEBS Lett 2009 584, N 2:434–442.