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자료유형
학술저널
저자정보
이은영 (한국생명공학연구원) 김현관 (한국생명공학연구원) 이종수 (충남대학교) 김명희 (한국생명공학연구원)
저널정보
충북대학교 동물의학연구소 Journal of Biomedical and Translational Research Journal of Biomedical and Translational Research 제17권 제4호
발행연도
2016.12
수록면
126 - 131 (6page)

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The aminoacyl-tRNA synthetases (ARSs) are ancient house-keeping enzymes that catalyze the ligation of tRNAs to their cognate amino acids in the first step of protein synthesis. During the evolution of higher eukaryotes, cytoplasmic ARSs have undergone significant changes including the addition of new domains that are not part of the enzymatic core. These additional regions have been found to be associated with a broad range of biological functions beyond protein synthesis. The non-translational functions of ARSs appear to be regulated by their presence within a cytoplasmic multi-tRNA synthetase complex (MSC), which is assembled through the appended domains. We recently reported that the MSC member glutamyl-prolyl-tRNA synthetase (EPRS) promotes antiviral gene expression through its infection-specific phosphorylation and release from the MSC. Here, we conducted transcriptome analysis of influenza A virus-infected cells. We particularly focused on the analysis of chemokine-related gene expression, in combination with chemokine array analysis against virus infection. Moreover, the correlation between chemokine expression pattern and EPRS function in response to different stimuli was assessed. The results showed that viral infection increases interferon-response and pro-inflammatory chemokine expression. In contrast, the level of chemokine expression was suppressed in interferon-γ treated cells. Thus, these results further demonstrate the previously reported stimulus-specific EPRS functions in immune responses.

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