@article{oai:yamanashi.repo.nii.ac.jp:00002795,
 author = {Okamoto, Hirotaka and Yatomi, Yutaka and Satoh, Kaneo and Yamane, Tetsu and Mitsumata, Masako and Chen, Wen-Tien and Ozaki, Yukio and Fujii, Hideki},
 issue = {1},
 journal = {山梨医科学雑誌, Yamanashi medical journal},
 month = {},
 note = {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.},
 pages = {31--41},
 title = {<Original article> Sphingosine 1-phosphate stimulates cell migration and active seprase expression in human endothelial cells},
 volume = {27},
 year = {2013}
}