The integrin ?v?6 is a fibronectin receptor that is undetectable on normal keratinocytes in situ, but is increased significantly in wound healing and in culture-established keratinocytes, suggesting that it may promote changes associated with cell motility. Using normal human oral keratinocytes we have shown that cultured cells express relatively high levels of ?v?6 and this integrin has a functional role in both cell adhesion and migration towards fibronectin. We provide experimental evidence that the increased expression of ?v?6 by normal human oral keratinocytes results in coordinate changes, which promote a more migratory phenotype. Thus increased expression of ?v?6 results in a fibronectin-dependent increase in pro-matrix metalloproteinase 9, matrix metalloproteinase 9 activity increases normal human oral keratinocyte migration, and this may be further dependent on plasmin activation. The results suggest a key role for ?v?6 in these processes and indicate a coordinated link between ?v?6 expression and upregulation of matrix metalloproteinase 9. It appears that ?v?6 may function in normal human oral keratinocyte migration through matrix-metalloproteinase-9-dependent and -independent mechanisms
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