Cytochemical localization of Na(+)-K(+)-adenosine triphosphate activity in the proximal convoluted tubule cells of the gerbil Meriones crassus.
The present work describes the cytochemical localization of Na(+)-K(+)-ATPase in the proximal convoluted tubule cells of the gerbil Meriones crassus. By using CeCl3 as capture agent, a fine, uniform reaction product was distributed mainly across the basolateral membranes and at the apical surface. This study provides evidence that the ATPase enzyme studied is actually Na(+)-K(+)-ATPase because acetate buffer (bleaching agent) had no decalcifying effect, nor did the subsequent application of levamisole, an inhibitor of alkaline phosphatase, which can hydrolize ATP. Such findings may serve to provide insights into the regulatory role of the Na(+)-K(+)-ATPase in intra-extra cellular balance in the basolateral membranes of the proximal convoluted tubule cells of this desert animal which show thick basal laminae with their membrane-bound bodies. However, there is a lack of knowledge regarding the transport function of the assayed enzyme and these bodies.
Safer
A M
AM
Department of Zoology, Faculty of Science, Kuwait University, Kuwait.
Abou-Salem
K S
KS
Hussain
S T
ST
D000818:Animals; D005849:Gerbillinae; D006651:Histocytochemistry; D006868:Hydrolysis; D007687:Kidney Tubules, Proximal / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D008871:Microvilli / Q000201:enzymology / Q000648:ultrastructure; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D000254:Sodium-Potassium-Exchanging ATPase