N-terminal domain of soluble epoxide hydrolase negatively regulates the VEGF-mediated activation of endothelial nitric oxide synthase Article (Faculty180)

cited authors

  • Hou, Hsin-Han H; Hammock, Bruce D; Su, Kou- H; Morisseau, Christophe; Kou, Yu R; Imaoka, Susumu; Oguro, Ami; Shyue, Song- K; Zhao, Jin- F; Lee, Tzong- S


  • The mammalian soluble epoxide hydrolase (sEH) has both an epoxide hydrolase and a phosphatase domain. The role of sEH hydrolase activity in the metabolism of epoxyeicosatrienoic acids (EETs) and the activation of endothelial nitric oxide synthase (eNOS) in endothelial cells (ECs) has been well defined. However, far less is known about the role of sEH phosphatase activity in eNOS activation. In the present study, we investigated whether the phosphatase domain of sEH was involved in the eNOS activation in ECs.


publication date

  • 2012

published in

start page

  • 120

end page

  • 9


  • 93