Angiotensin I converting enzyme activity in rabbit corneal endothelial cells.
Angiotensin I converting enzyme (ACE) was studied in Vero cells, rabbit corneal fibroblasts, and rabbit corneal endothelial cells. The enzyme activity was determined by means of an assay employing hippuryl-glycyl-glycine as a substrate. The hippuric acid end product was separated from the substrate by reversed phase liquid chromatography and measured spectrophotometrically at 228 nm. The enzyme was further characterized by a captopril inhibition study. Significant ACE activity was found in rabbit corneal endothelial cells but not in other types of cells tested. This is the first report of the presence of this enzyme in a specific ocular cell type and suggests that angiotensin II may play a role in normal ocular physiology.
D000818:Animals; D002460:Cell Line; D002853:Chromatography, Liquid; D003315:Cornea / Q000201:enzymology*; D004727:Endothelium / Q000201:enzymology*; D005347:Fibroblasts / Q000201:enzymology; D066298:In Vitro Techniques; D009842:Oligopeptides / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000032:analysis*; D011817:Rabbits; D013053:Spectrophotometry
D009842:Oligopeptides; C029275:hippuryl-glycyl-glycine; D007703:Peptidyl-Dipeptidase A