Abstract:
: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-alpha. The secreted KRS bound to macrophages and peripheral blood mononuclear cells to enhance the TNF-alpha production and their migration. The mitogen-activated protein kinases, extracellular signal-regulated kinase and p38 mitogen-activated protein kinase, and Galphai 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Park SG,Kim HJ,Min YH,Choi EC,Shin YK,Park BJ,Lee SW,Kim Sdoi
10.1073/pnas.0500226102keywords:
subject
Has Abstractpub_date
2005-05-03 00:00:00pages
6356-61issue
18eissn
0027-8424issn
1091-6490pii
0500226102journal_volume
102pub_type
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