Ultracytochemical localization of ouabain-sensitive K+-dependent, p-nitrophenyl phosphatase in myelin.
Ouabain-sensitive, K+-dependent p-nitrophenyl phosphatase (K-NPPase) activity was demonstrated ultracytochemically in the myelin of nerve fibers in peripheral and central white matter. Enzyme activity was more prominent in paranodal than compact myelin, and it was absent from nodal and interparanodal axolemma. Since K-NPPase is part of the Na-KATPase complex, we consider myelin as an important site of the sodium pump and believe that myelin participates in cationic regulation of the nervous tissue.
D009597:4-Nitrophenylphosphatase / Q000378:metabolism*; D000818:Animals; D006651:Histocytochemistry; D008854:Microscopy, Electron; D009186:Myelin Sheath / Q000201:enzymology*; D010042:Ouabain / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011188:Potassium / Q000494:pharmacology; D011901:Ranvier's Nodes / Q000201:enzymology; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism
D010042:Ouabain; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium