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Medline

PubMed, a service of the National Library of Medicine

World Oncology Network

R.E.Kavetsky Institute of Experimental Pathology, Oncology and Radiobiology



Vol. 26, No. 4, 2004 (December)

Content

CYTOKINE-LIKE ACTIVITIES OF SOME AMINOACYL-tRNA SYNTHETASES AND AUXILIARY p43 COFACTOR OF AMINOACYLATION REACTION AND THEIR ROLE IN ONCOGENESIS

 

Serhiy S. Ivakhno, Alexander I. Kornelyuk

Institute of Molecular Biology and Genetics, NAS of Ukraine, Kyiv, Ukraine

Abstract. Multifunctionality of proteins is among mechanisms accounting for the complexity of interactome networks in higher eukaryotes. During oncogenesis and other pathologic conditions many proteins perform additional functions without changes in three dimensional structures. One family of these moonlighting proteins is represented by enzymes and cofactors of aminoacylation reactions, by means of which tRNAs are attached to their cognate amino acids. Tyrosyl-tRNA synthetase (TyrRS), tryptophanyl-tRNA synthetases (TrpRS) and auxiliary factor of mammalian multi-aminoacyl-tRNA synthetases, p43 (precusor of endothelial monocyte activating polypeptide II — EMAP II) upon their release in intracellular environment become proinflammatory cytokines with multiple activities during apoptosis, angiogenesis and inflammation. In addition, these proteins play important role in cancer progression, modulating tumor angiogenesis and its escape from surveillance by immune system.

Key Words: moonlighting proteins, endothelial-monocyte activating polypeptide II, tyrosyl-tRNA synthetase, tryptophanyl-tRNA synthetase, apoptosis, tumor angiogenesis.

Language:  English

[full text]




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