Abstract:
:The aminoacyl-tRNA synthetase interacting multi-functional protein 1 (AIMP1) participates in a variety of cellular processes, including translation, cell proliferation, inflammation and wound healing. Previously, we showed that the N-terminal peptide of AIMP1 (6-46 aa) induced ERK phosphorylation. Liver fibrosis is characterized by excessive deposition of extracellular matrix, which is induced by TGFβ signaling, and activated ERK is known to induce the phosphorylation of SMAD, thereby inhibiting TGFβ signaling. We assessed whether the AIMP1 peptide can inhibit collagen synthesis in hepatic stellate cells (HSCs) by activating ERK. The AIMP1 peptide induced phosphorylation of SMAD2 via ERK activation, and inhibited the nuclear translocation of SMAD, resulting in a reduction of the synthesis of type I collagen. The AIMP1 peptide attenuated liver fibrosis induced by CCl4, in a dose-dependent manner. Masson-Trichrome staining showed that the AIMP1 peptide reduced collagen deposition. Immunohistochemical staining showed that the levels of α-SMA, TGFβ and type I collagen were all reduced by the AIMP1 peptide. Liver toxicity analysis showed that the AIMP1 peptide improved the levels of relevant biological parameters in the blood. These results suggest that AIMP1 peptide may have potential for development as a therapeutic agent to treat liver fibrosis.
journal_name
Int J Oncoljournal_title
International journal of oncologyauthors
Ahn J,Son MK,Jung KH,Kim K,Kim GJ,Lee SH,Hong SS,Park SGdoi
10.3892/ijo.2015.3303subject
Has Abstractpub_date
2016-02-01 00:00:00pages
747-55issue
2eissn
1019-6439issn
1791-2423journal_volume
48pub_type
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