0000000000337299
AUTHOR
G. M. Pacifici
Cytosolic epoxide hydrolase in humans: development and tissue distribution.
Cytosolic epoxide hydrolase activity was measured towards trans-stilbene oxide in 41 human adult livers, in 40 fetal livers, in 17 placentas and in fetal and adult lungs, kidneys and gut. The cytosolic epoxide hydrolase activity was measurable in all specimens investigated. The rate of formation of trans-stilbene glycol (pmol/min per mg protein, mean +/- SD) was 55.2 +/- 89.6 (fetal liver). 303.2 +/- 73.2 (adult liver) and 18.8 +/- 13.1 (placenta) In the fetal extrahepatic tissues, the cytosolic epoxide hydrolase activity was 70.0 +/- 9.4 (adrenals), 47.6 +/- 7.2 (gut), 69.4 +/- 22.5 (kidneys) and 43.2 +/- 19.2 (lungs) pmol/min per mg protein, whereas in the adult tissues it was 131.2 +/- 6…
Valpromide is a poor inhibitor of the cytosolic epoxide hydrolase
The effect of the antiepileptics valpromide and sodium valproate on the cytosolic epoxide hydrolase was studied in human fetal liver, kidneys and adrenals and from human adult liver and kidneys. Trans-stilbene oxide was used as substrate. Valpromide (10 mM) lowered the activity of the epoxide hydrolase to one half of the control in all organs studied. Sodium valproate (10 mM) was less powerful as an inhibitor than valpromide; however, it exerted a significant inhibition in all tissues studied.