N-terminal domain of soluble epoxide hydrolase negatively regulates the VEGF-mediated activation of endothelial nitric oxide synthase
Population
sEH knockout (sEH-/-) mice, wild-type mice, and endothelial cells (ECs)
Comparison
Pharmacological inhibition of sEH phosphatase… vs Wild-type mice or control endothelial cells
Design
Preclinical
Authors
Discussion
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Member takes
Implication
Preclinical sEH phosphatase inhibition enhances endothelial signaling; hypothesis-generating for angiogenesis therapies and requires clinical validation.
Structured PICO
P
Population
sEH knockout (sEH-/-) mice, wild-type mice, and endothelial cells (ECs)
I
Intervention
Pharmacological inhibition of sEH phosphatase, overexpression of sEH with an inactive phosphatase domain, or overexpression of the phosphatase domain of sEH; VEGF treatment
C
Comparator
Wild-type mice or control endothelial cells
O
Outcome
eNOS phosphorylation and NO productionsurrogate
The phosphatase activity of soluble epoxide hydrolase negatively regulates VEGF-mediated eNOS activation and angiogenesis, highlighting a novel mechanistic role in endothelial function.
Cite This Study
Hou et al. (2011) studied this question.