Biopolym. Cell. 1999; 15(2):168-172.
Priority Publications
Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase
1Kornelyuk A. I., 2Tas M. P. R., 1Dubrovsky A. L., 2Murray J. C.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. The University of Nottingham
    University ParkNottingham, NG7 2RD, UK


Cytokine activity of the isolated recombinant C-terminal domain of mammalian lyrosyl-tRNA synthetasg (TyrRS), which is homologous to a tumor-derived cytokine, endothelial and monocyte activating polypeptide (EMAP-2) has been studied. It was shown that C-domain induced a ~ 2-fold increase of monocyte chemotaxis. This effect is comparable with the values of chemotaxis induction by EMAP-2 cytokine and proEMAP-2. The truncated catalytic form of bovine TyrRS (2 x 39 kDa) lias no effect on monocyte chemotaxis. C-domain of TyrRS also induced a ~ 3-fold increase in tissue factor activity in cultured human endothelial cells. A hypothesis is forwarded that the isolated C-domain of mammalian TyrRS may be released at proteoiytic cleavage of TyrRS by some protease, activated ui stress conditions, and functions as a mediator via signal transduction through interaction with a putative EMAP-2 receptor.


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