Cytochemical localization of alkaline phosphatase and ouabain-sensitive K+-dependent p-nitrophenylphosphatase activities in brain capillaries of the newt.
The ultrastructural localization of alkaline phosphatase and K+-NPPase was investigated in brain capillaries of newt by a cytochemical study using whole brain perfusion. The alkaline phosphatase activity was present in both luminal and antiluminal membranes of the endothelial cells. By contrast, the K+-NPPase was located only in antiluminal membranes of the brain capillaries. This distinct enzymatic distribution suggested that the luminal and antiluminal membranes are functionally different. The role of alkaline phosphatase and K+-NPPase in the blood brain barrier is discussed.
D009597:4-Nitrophenylphosphatase / Q000032:analysis*; D000469:Alkaline Phosphatase / Q000032:analysis*; D000818:Animals; D001921:Brain / Q000648:ultrastructure; D002196:Capillaries / Q000201:enzymology* / Q000648:ultrastructure; D002560:Cerebrovascular Circulation; D006651:Histocytochemistry; D008854:Microscopy, Electron; D010042:Ouabain / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D012455:Salamandridae; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis
D010042:Ouabain; D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D000254:Sodium-Potassium-Exchanging ATPase