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Two distinct cytokines released from a human aminoacyl-tRNA synthetase

Academic Article
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Overview

authors

  • Wakasugi, K.
  • Schimmel, Paul

publication date

  • April 1999

journal

  • Science  Journal

abstract

  • Aminoacyl-tRNA synthetases catalyze aminoacylation of transfer RNAs (tRNAs). It is shown that human tyrosyl-tRNA synthetase can be split into two fragments with distinct cytokine activities. The endothelial monocyte-activating polypeptide II-like carboxy-terminal domain has potent leukocyte and monocyte chemotaxis activity and stimulates production of myeloperoxidase, tumor necrosis factor-alpha, and tissue factor. The catalytic amino-terminal domain binds to the interleukin-8 type A receptor and functions as an interleukin-8-like cytokine. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines.

subject areas

  • Amino Acid Sequence
  • Antigens, CD
  • Apoptosis
  • Binding, Competitive
  • Catalytic Domain
  • Chemotaxis, Leukocyte
  • Cytokines
  • Humans
  • Interleukin-8
  • Leukocyte Elastase
  • Molecular Sequence Data
  • Monocytes
  • Neoplasm Proteins
  • Neutrophils
  • RNA-Binding Proteins
  • Receptors, Interleukin
  • Receptors, Interleukin-8A
  • Recombinant Proteins
  • Signal Transduction
  • Tumor Cells, Cultured
  • Tyrosine-tRNA Ligase
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.284.5411.147

PubMed ID

  • 10102815
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Additional Document Info

start page

  • 147

end page

  • 151

volume

  • 284

issue

  • 5411

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