The relationship between localization of Na+, K+-ATPase and cellular fine structure in the rat parotid gland.
A method for the ultrastructural localization of the Na+-pump enzyme, Na+, K+-ATPase has been applied to the rat parotid gland. A ouabain-sensitive final reaction product, dependent on the presence of K+ and Mg2+, was found to be evenly distributed along the basal and basolateral plasma membranes of acinar and striated duct cells. In both cases, it was localized predominantly in the cytoplasm of the extensive foldings of these membranes. It is concluded that the reaction product meets the criteria for valid localization of this enzyme and that potential Na+-pump sites have been demonstrated. This study supports previous findings in salivary glands and contributes to an increasing body of evidence that contraluminal Na+-pumps are common to both reabsorbing and secreting epithelial cells.
D000818:Animals; D003470:Culture Media; D007978:Levamisole / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D008854:Microscopy, Electron; D010042:Ouabain / Q000494:pharmacology; D010306:Parotid Gland / Q000201:enzymology / Q000648:ultrastructure*; D011188:Potassium / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D012964:Sodium / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis*
D003470:Culture Media; D007978:Levamisole; D010042:Ouabain; D012964:Sodium; D000254:Sodium-Potassium-Exchanging ATPase; D008274:Magnesium; D011188:Potassium