Induction of monocyte chemoattractant protein-1 secretion from lung epithelial cells by trypsin
- VernacularTitle:胰蛋白酶可诱导肺上皮细胞分泌单核细胞趋化蛋白-1
- Author:
Haiyan WANG
;
Shaoheng HE
- Publication Type:Journal Article
- Keywords:
Trypsin;
Epithelial cells;
Monocyte chemoattr actant protein-1
- From:Chinese Journal of Pathophysiology
1986;0(04):-
- CountryChina
- Language:Chinese
-
Abstract:
AIM: To investigate the actions of trypsi n on the secretion of monocyte chemoattractant protein-1 (MCP-1) from human lung e pithelial cells. METHODS: A549 cells were cultured in a 12-well culture plate. Th e challenge was performed by addition of various concentrations of trypsin or tr ypsin inhibitor into each well, respectively. After 2 h, 8 h or 16 h, the reacti ons were terminated by removal of the supernatant from each well. A sandwich ELI SA was used to determine the levels of MCP-1 in supernatants. RESULTS: Following 16 h incubation, trypsin was able to induce c oncentration-dependent secretion of MCP-1. As low as 3 ?g/L trypsin was able to induce MCP-1 release from epithelial cells, and the maximum of accumulated rele ase of MCP-1 was observed with 100 ?g/L trypsin, which was 3 fold more than bas eline release. However, trypsin at 300 ?g/L did not induce significant MCP-1 se cretion. Soybean trypsin inhibitor (SBTI) inhibited trypsin-induced MCP-1 secret ion, but ? 1-antitrysin (? 1-AT) did not. The time course showed that the actions of trypsin initiated at 2 h and reached their peak at 16 h. CONCLUSION: Trypsin is a potent secretogogue of MCP-1 release fr om cultured human lung epithelial cells, and itself action can be inhibited by S BTI.
