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A Human Aminoacyl-tRNA Synthetase as a Regulator of Angiogenesis

Aminoacyl-tRNA synthetases catalyze the first step of protein synthesis. It was shown recently that human tyrosyl-tRNA synthetase (TyrRS) can be split into two fragments having distinct cytokine activities, thereby linking protein synthesis to cytokine signaling pathways. Tryptophanyl-tRNA synthetas...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2002-01, Vol.99 (1), p.173-177
Main Authors: Wakasugi, Keisuke, Slike, Bonnie M., Hood, John, Otani, Atsushi, Ewalt, Karla L., Friedlander, Martin, Cheresh, David A., Schimmel, Paul
Format: Article
Language:English
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Summary:Aminoacyl-tRNA synthetases catalyze the first step of protein synthesis. It was shown recently that human tyrosyl-tRNA synthetase (TyrRS) can be split into two fragments having distinct cytokine activities, thereby linking protein synthesis to cytokine signaling pathways. Tryptophanyl-tRNA synthetase (TrpRS) is a close homologue of TyrRS. A natural fragment, herein designated as mini TrpRS, was shown by others to be produced by alternative splicing. Production of this fragment is reported to be stimulated by IFN-γ, a cytokine that also stimulates production of angiostatic factors. Mini TrpRS is shown here to be angiostatic in a mammalian cell culture system, the chicken embryo, and two independent angiogenesis assays in the mouse. The full-length enzyme is inactive in the same assays. Thus, protein synthesis may be linked to the regulation of angiogenesis by a natural fragment of TrpRS.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.012602099