Abstract: Objective：To explore the possible mechanism of protein kinase C α(PKCα) involved in the migration of SW620 cells promoted by Ⅶa/tissue factor (TF) activated proteaseactivated receptor 2 (PAR2). Methods：After SW620 cells were treated by PAR2 agonist (PAR2-AP), coagulation factor Ⅶa, PKCagonist (PMA), anti-TF antibody (α-TF), anti-PAR2 antibody (α-PAR2) and isotype control antibody (mopc-21) respectively, the expressions of PKCα and p-PKCα in SW620 cells were detected by Western blot, and the distribution of PKCα by immunofluorescence assay. After SW620 cells were pretreated with PMA (100 nmol/L), factor Ⅶa (10 nmol/L) and PKCα inhibitor(safingol, 10 μmol/L) respectively, the migration of SW620 cells was detected by Transwell test, and the expression level of MMP-9 mRNA by quantitative real-time PCR (q-PCR). Results：PMA (100 nmol/L), factor Ⅶa (10 nmol/L) and PAR2AP (100 μmol/L) were able to increase the phosphorylation of PKCα obviously (P<0.05), but did not show significant effect on the expression of PKCα (P＞0.05). Immunofluorescence assay indicated the translocation of PKCα from cytoplasm into nuclear membrane and nucleus of SW620 cells. In the meanwhile, both α-TF and α-PAR2 were able to obviously inhibit the activation of PKCα by factor Ⅶa, while mopc-21 did not show the inhibitory effect. In addition, Transwell test and q-PCR demonstrated that safingol could obviously block the migration of SW620 cells and the expression of MMP-9 mRNA in SW620 cells caused by factor Ⅶa. Conclusion：Factor Ⅶa could activate PAR2 based on TF, then upregulate the expression of MMP-9 and promote the migration of SW620 cells via the action of PKCα.