<Original article> Sphingosine 1-phosphate stimulates cell migration and active seprase expression in human endothelial cells

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Objective: Sphingosine 1-phosphate (Sph-1-P), a bioactive lysophospholipid present in the plasma, is released from activated platelets. Our previous study demonstrated that Sph-1-P promoted the spreading on and migration of human umbilical vein endothelial cells (HUVEC) through the extracellular matrix (ECM), suggesting a possible induction of cell surface proteases in the Sph-1-P activated endothelial cells. In the present study, we examined whether seprase, a type II transmembrane serine protease (TTSP) usually absent in tissue cells, can be induced in endothelial cells activated by Sph-1-P. Methods: HUVEC migration through ECM was examined by modifi ed Boyden chamber assay. Western blotting and immunoprecipitation, using anti-seprase monoclonal antibodies (mAbs), were used to confi rm the seprase expression of HUVEC. Results: We show that Sph-1-P enhanced expression of active form seprase in a time- and dose-dependent manner in HUVEC. The Sph-1-P inducible active form seprase could be blocked by pertussis toxin and by C3 transferase, which inactivate Gi-type heterotrimetric G proteins and Rho, respectively. Conclusion: These results show that Sph-1-P can regulate migration of endothelial cells by inducing active form seprase expression, which, in turn, is mediated through a Gi-coupled cell surface receptor and the Rho protein.

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