Analysis of the function and sigial transduction about Discoidin Domain Receptor (DDR)1 as a unique collagen receptor.

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Discoidin Domain Receptor (DDR)1 is a receptor tyrosine kinase activated by collagen that is abundant in extracellular matrix. Previous studies reported human mammary carcinoma tumors expressed DDR1 highly in comparison with normal mammary tissues.In the present study, we detected DDR1 mRNA and protein in human T-47D mammary carcinoma cells in vitro. We used RNA knock down method by vector expressing small hairpin RNA(shRNA) to identify the role of DDR1 in T-47D cells.Suppression of DDR1 in T-47D cells decreased adherence to collagen-coated plates. Morphogically, suppression of DDR1 in T-47D cells decreased exhibition of pseudopod extension on collagen-coated plates. Suppression of DDR1 in T-47D cells decreased migration through collagen lattices. Suppression of DDR1 in T-47D cells decreased activity of cdc-42 in the presence of soluble collagen.Taken together, the interaction of DDR1 with collagen of extracellular matrix results in migration in a stromal tissue microenvironment in mammary carcinoma cells.