Bradykinin enhances cell migration in human chondrosarcoma cells through BK receptor signaling pathways

Bradykinin (BK) is an inflammatory mediator, and shows elevated levels in regions of severe injury and inflammatory diseases. BK has recently been shown to be involved in carcinogenesis and cancer progression. In this study, we found that BK increased the migration and the expression of α2β1 integri...

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Bibliographic Details
Published in:Journal of cellular biochemistry 2010-01, Vol.109 (1), p.82-92
Main Authors: Yang, Wei-Hung, Chang, Jung-Tzu, Hsu, Sheng-Feng, Li, Te-Mao, Cho, Der-Yang, Huang, Chun-Yin, Fong, Yi-Chin, Tang, Chih-Hsin
Format: Article
Language:English
Subjects:
BK receptor
Blotting, Western
Bone Neoplasms - metabolism
Bradykinin
Bradykinin - metabolism
Cancer
Carcinogenesis
Cartilage
Cell Line, Tumor
Cell migration
Cell Movement - physiology
Cell Separation
Chondrosarcoma
Chondrosarcoma - metabolism
Flow Cytometry
Humans
Inflammation
Inflammatory diseases
Injuries
integirn
Integrin alpha2beta1 - metabolism
Integrins
NF-kappa B - metabolism
Phospholipase C
Protein kinase C
Protein Kinase C-delta - metabolism
Receptors, Bradykinin - metabolism
Reverse Transcriptase Polymerase Chain Reaction
Signal transduction
Signal Transduction - physiology
siRNA
Type C Phospholipases - metabolism
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Summary:Bradykinin (BK) is an inflammatory mediator, and shows elevated levels in regions of severe injury and inflammatory diseases. BK has recently been shown to be involved in carcinogenesis and cancer progression. In this study, we found that BK increased the migration and the expression of α2β1 integrin in human chondrosarcoma cells. We also found that human chondrosarcoma tissues had significantly higher expression of the B1 and B2 receptors comparing to normal cartilage. BK‐mediated migration and integrin up‐regulation was attenuated by B1 and B2 BK receptor siRNA or antagonist. Activations of phospholipase C (PLC), protein kinase Cδ (PKCδ), and NF‐κB pathways after BK treatment was demonstrated, and BK‐induced integrin expression and migration activity was inhibited by the specific inhibitor of PLC, PKCδ, and NF‐κB cascades. Taken together, our results indicated that BK enhances the migration of chondrosarcoma cells by increasing α2β1 integrin expression through the BK receptors/PLC/PKCδ/NF‐κB signal transduction pathway. J. Cell. Biochem. 109: 82–92, 2010. © 2009 Wiley‐Liss, Inc.
ISSN:0730-2312
1097-4644
1097-4644
DOI:10.1002/jcb.22383