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Activation of angiogenic signaling pathways by two human tRNA synthetases

Academic Article
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Overview

authors

  • Ewalt, K. L.
  • Schimmel, Paul

publication date

  • November 2002

journal

  • Biochemistry  Journal

abstract

  • Aminoacyl-tRNA synthetases establish the rules of the genetic code by joining amino acids to tRNAs that bear the anticodon triplets corresponding to the attached amino acids. The enzymes are thought to be among the earliest proteins to appear, in the transition from a putative RNA world to the theater of proteins. Over their long evolution, the enzymes have acquired additional functions that typically require specialized insertions or domain fusions. Recently, fragments of the closely related human tyrosyl- and tryptophanyl-tRNA synthetases were discovered to be active in angiogenesis signaling pathways. One synthetase fragment has proangiogenic activity, while the other is antiangiogenic. Activity was demonstrated in cell-based assays in vitro and in vivo in the chick embryo, and in the neonatal and adult mouse. The full-length, native enzymes are inactive in these same assays. Activation of angiogenesis activity requires fragment production from the native enzymes by protease cleavage or by translation of alternatively spliced pre-mRNA. Thus, these tRNA synthetases link translation to a major cell-signaling pathway in mammalian cells. The results with animals suggest that therapeutic applications are possible with these tRNA synthetases.

subject areas

  • Animals
  • Humans
  • Neovascularization, Physiologic
  • Signal Transduction
  • Tryptophan-tRNA Ligase
  • Tyrosine-tRNA Ligase
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi020537k

PubMed ID

  • 12416978
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Additional Document Info

start page

  • 13344

end page

  • 13349

volume

  • 41

issue

  • 45

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