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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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 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-gamma, 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.[1]

References

  1. A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Wakasugi, K., Slike, B.M., Hood, J., Otani, A., Ewalt, K.L., Friedlander, M., Cheresh, D.A., Schimmel, P. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
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