Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase

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...

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Бібліографічні деталі
Дата:1999
Автори: Kornelyuk, A., Tas, M., Dubrovsky, A., Murray, J.C.
Формат: Стаття
Мова:English
Опубліковано: Інститут молекулярної біології і генетики НАН України 1999
Назва видання:Биополимеры и клетка
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Онлайн доступ:http://dspace.nbuv.gov.ua/handle/123456789/156329
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Назва журналу:Digital Library of Periodicals of National Academy of Sciences of Ukraine
Цитувати:Cytokine activity of the non-catalytic EMAP-2-like domain of mammalian tyrosyl-tRNA synthetase / A. Kornelyuk, M. Tas, A. Dubrovsky, J.C. Murray // Биополимеры и клетка. — 1999. — Т. 15, № 2. — С. 168-172. — Бібліогр.: 23 назв. — англ.

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Digital Library of Periodicals of National Academy of Sciences of Ukraine
Опис
Резюме: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.