Subcellular localization of angiotensin-converting enzyme in cultured neuroblastoma cells.
Angiotensin-converting enzyme (ACE) activity of Neuro-2A mouse neuroblastoma cells was found predominantly in particulate fractions. Density gradient centrifugation of the particulate fractions showed ACE activity in light fractions of the gradient, a result suggesting a plasma membrane localization. This was confirmed using the aqueous two-phase polymer system of plasma membrane isolation. The rapid and energy-independent hydrolysis of exogenous substrate by ACE of intact cells and the sensitivity of the enzyme of intact cells to proteases indicate further that the active site of ACE is oriented extracellularly.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D006868:Hydrolysis; D051379:Mice; D009447:Neuroblastoma / Q000201:enzymology* / Q000648:ultrastructure; D009842:Oligopeptides / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology
D009842:Oligopeptides; C010980:hippuryl-histidyl-leucine; D007703:Peptidyl-Dipeptidase A