Immune Netw.
2005 Dec;5(4):193-198. 10.4110/in.2005.5.4.193.
Protease-activated Receptor 2 is Associated with Activation of Human Macrophage Cell Line THP-1
- Affiliations
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- 1Department of Oriental Pharmacy, College of Pharmacy, Wonkwang University, Iksan, Korea.
- 2Department of Companion and Laboratory Animal Science, Kongju National University, Gongju, Korea.
- 3Department of Immunology, Chonbuk National University Medical School, Jeonju, Korea. deakim@chonbuk.ac.kr
- 4Department of Pathology, Chonbuk National University Medical School, Jeonju, Korea.
- KMID: 1846705
- DOI: http://doi.org/10.4110/in.2005.5.4.193
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.
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