Protease-activated Receptor 2 is Associated with Activation of Human Macrophage Cell Line THP-1
Immune Network
;
: 193-198, 2005.
Article
in English
| WPRIM
| ID: wpr-85875
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phosphorylation
/
Phosphotransferases
/
Enzyme-Linked Immunosorbent Assay
/
Trypsin
/
Cell Line
/
Blotting, Western
/
Tumor Necrosis Factor-alpha
/
Receptor, PAR-2
/
Cell Proliferation
/
Serine Proteases
Limits:
Humans
Language:
English
Journal:
Immune Network
Year:
2005
Type:
Article
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