Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response

Gyu Park Sang, Jin Kim Hye, Hong Min You, Eung Chil Choi, Kee Shin Young, Bum Joon Park, Won Lee Sang, Sunghoon Kim

Research output: Contribution to journalArticlepeer-review

150 Citations (Scopus)


Although aminoacyl-tRNA synthetases (ARSs) are essential for protein synthesis, they also function as regulators and signaling molecules in diverse biological processes. Here, we screened 11 different human ARSs to identify the enzyme that is secreted as a signaling molecule. Among them, we found that lysyl-tRNA synthetase (KRS) was secreted from intact human cells, and its secretion was induced by TNF-α. The secreted KRS bound to macrophages and peripheral blood mononuclear cells to enhance the TNF-α production and their migration. The mitogen-activated protein kinases, extracellular signal-regulated kinase and p38 mitogen-activated protein kinase, and Gαai were determined to be involved in the signal transduction triggered by KRS. All of these activities demonstrate that human KRS may work as a previously uncharacterized signaling molecule, inducing immune response through the activation of monocyte/macrophages.

Original languageEnglish
Pages (from-to)6356-6361
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number18
Publication statusPublished - 2005 May 3

All Science Journal Classification (ASJC) codes

  • General


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