Protease-activated Receptor 2 is Associated with Activation of Human Macrophage Cell Line THP-1.
- Author:
Chon Sik KANG
1
;
Jin TAE
;
Young Mi LEE
;
Byeong Soo KIM
;
Woo Sung MOON
;
Dae Ki KIM
Author Information
- Publication Type:Original Article
- Keywords: Protease-activated receptor 2; macrophage; trypsin; cell proliferation; extracellular regulated kinase
- MeSH: Blotting, Western; Cell Line*; Cell Proliferation; Enzyme-Linked Immunosorbent Assay; Humans*; Macrophages*; Phosphorylation; Phosphotransferases; Receptor, PAR-2*; Serine Proteases; Trypsin; Tumor Necrosis Factor-alpha
- From:Immune Network 2005;5(4):193-198
- CountryRepublic of Korea
- Language:English
- Abstract: BACKGROUND: Protease-activated receptor 2 (PAR2) belongs to a family of G protein- coupled receptors activated by proteolytic cleavage. Trypsin-like serine proteases interact with PAR2 expressed by a variety of tissues and immune cells. The aim of our study was to investigate whether PAR2 stimulation can lead to the activation of human macrophages. METHODS: PAR2-mediated proliferation of human macrophage cell line THP-1 was measured with MTT assay. We also examined the extracellular regulated kinase (ERK) phosphorylation and cytokine production induced by trypsin and PAR2-agonist using western blot and enzyme-linked immunosorbent assay (ELISA), respectively. RESULTS: Treatment of trypsin or PAR2-activating peptide increased cell proliferation in a dose-dependent manner, and induced the activation of ERK1/2 in THP-1 cells. In addition, trypsin-induced cell proliferation was inhibited by pretreatment of an ERK inhibitor (PD98059) or trypsin inhibitor (SBTI). Moreover, PAR2 activation by trypsin increased the secretion of TNF-alpha in THP-1 cells. CONCLUSION: There results suggest that PAR2 activation by trypsin-like serine proteases can induce cell proliferation through the activation of ERK in human macrophage and that PAR2 may play a crucial role in the cell proliferation and cytokine secretion induced by trypsin-like serine proteases.
