Suppression of E3 ubiquitin ligase Cbl-b in interleukin-1 signaling.
- Author:
Jiang-Tian YU
1
;
Xin BU
1
;
Hu ZHAO
1
;
Jin SU
2
Author Information
1. Department of Biochemistry and Molecular Biology, The Fourth Military Medical University, Xi'an 710032, China.
2. Department of Biochemistry and Molecular Biology, The Fourth Military Medical University, Xi'an 710032, China. sujin923@fmmu.edu.cn.
- Publication Type:Journal Article
- MeSH:
Collagen;
metabolism;
Epithelial Cells;
enzymology;
Humans;
Interleukin-1;
metabolism;
Matrix Metalloproteinase 13;
metabolism;
Proto-Oncogene Proteins c-cbl;
metabolism;
Signal Transduction
- From:
Acta Physiologica Sinica
2015;67(4):409-412
- CountryChina
- Language:Chinese
-
Abstract:
The present study aims to investigate the effect of Cbl-b, a member of E3 ubiquitin ligase family, on interleukin-1 (IL-1) pathway in synoviocytes. The protein expression levels of Cbl-b and IL-1-induced matrix metalloproteinase 13 (MMP-13) in synoviocytes were analyzed by Western blot. Collagen substrates were incubated with the conditioned medium collected from synoviocytes cultures and then subjected to SDS-PAGE for analysis of collagen degradation. The results showed that compared with wild-type cells, Cbl-b-deficient cells expressed more MMP-13 protein and had enhanced ability to degrade collagens under IL-1 stimulation. These data suggest that Cbl-b may negatively regulate IL-1-triggered degradation of collagen matrix in synoviocytes.
