Cross-talk between Integrin and SMAD Signal Pathway in Articular Chondrocyte.
- Author:
Soo Bong HAHN
1
;
Min Sung PARK
;
Yun Hee KIM
;
Jin Woo LEE
Author Information
1. Department of Orthopaedic Surgery, Yonsei University College of Medicine, Seoul, South Korea. ljwos@yuhs.ac
- Publication Type:Original Article
- Keywords:
Articular chondrocyte;
Signal cross-talk;
Type II collagen;
TGF-beta 1;
FAK;
SMAD 2/3
- MeSH:
Blotting, Western;
Cell Culture Techniques;
Chondrocytes*;
Collagen Type II;
Culture Media, Conditioned;
Phosphorylation;
Protein Kinases;
Signal Transduction*;
Transforming Growth Factor beta;
Tyrosine
- From:Journal of Korean Orthopaedic Research Society
2007;10(2):65-75
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
PURPOSE: Identifying the signal cross-talk between integrin signaling cascade and TGF-beta 1 signaling cascade in articular chondrocytes. MATERIALS AND METHODS: To analyze integrin or TGF-beta 1 mediated signaling pathways from extracellular stimuli, type II collagen was coated on the cell culture plate and TGF-beta 1 was added to cell culture media. Chondrocytes were cultured in the conditioned media with each or both stimuli. Altered activation of signaling proteins detected with western blot technique. RESULTS: More rapid attachment of cells was observed in the type II collagen coated group than non-coated group. The phosphorylated SMAD 2 and 3 were expressed in the type II collagen coated group and synergistically up-regulated phosphorylation in the co-treated group. The phosphorylated FAK at tyrosine 925 was activated by TGF-beta 1 treatment and synergistically up-regulated by both stimuli. But there was no meaningfully changed phosphorylation of extracellular signal regulated protein kinase (ERK) 1/2 and p38, as known downstream molecules of FAK cascade. CONCLUSION: This result means that SMAD 2, SMAD 3 and tyrosine 925 of FAK are involved in this signal cross-talking in articular chondrocytes.
