Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Cell Division
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Cell Line
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Cell Movement
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Cells, Cultured
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Chick Embryo
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Chorion / metabolism
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Collagen / pharmacology
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Drug Combinations
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Endothelial Growth Factors / metabolism
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Endothelium, Vascular / cytology
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Humans
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Interferon-gamma / pharmacology
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Laminin / pharmacology
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Lymphokines / metabolism
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Mice
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Neovascularization, Pathologic*
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Protein Structure, Tertiary
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Proteoglycans / pharmacology
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Retinal Vessels / metabolism
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Signal Transduction
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Time Factors
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Tryptophan-tRNA Ligase / chemistry*
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Tryptophan-tRNA Ligase / genetics
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Tryptophan-tRNA Ligase / physiology*
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Umbilical Veins / cytology
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Vascular Endothelial Growth Factor A
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Vascular Endothelial Growth Factors
Substances
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Drug Combinations
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Endothelial Growth Factors
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Laminin
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Lymphokines
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Proteoglycans
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Vascular Endothelial Growth Factor A
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Vascular Endothelial Growth Factors
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matrigel
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Interferon-gamma
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Collagen
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Tryptophan-tRNA Ligase