Presence of two isoforms of Na, K-ATPase with different pharmacological and immunological properties in the rat kidney

• Published in: Pflügers Archiv Vol. 430; no. 2; p. 205
• Main Authors: Féraille, E, Barlet-Bas, C, Cheval, L, Rousselot, M, Carranza, M L, Dreher, D, Arystarkhova, E, Doucet, A, Favre, H
• Format: Journal Article
• Language: English
• Published: Germany 01.06.1995
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibody Specificity; Isoenzymes - analysis; Isoenzymes - antagonists & inhibitors; Isoenzymes - chemistry; Kidney - enzymology; Kidney Tubules - enzymology; Kidney Tubules, Collecting - enzymology; Kidney Tubules, Proximal - enzymology; Male; Molecular Sequence Data; Nephrons - enzymology; Ouabain - pharmacology; Rats; Rats, Wistar; Sodium-Potassium-Exchanging ATPase - analysis; Sodium-Potassium-Exchanging ATPase - antagonists & inhibitors; Sodium-Potassium-Exchanging ATPase - chemistry
• ISSN: 0031-6768
• DOI: 10.1007/BF00374651

Previous studies have demonstrated the presence of two populations of Na,K-ATPase with distinct kinetic, pharmacological and immunological characteristics along the rabbit nephron, indicating that the proximal segments of the nephron express exclusively the alpha 1 isoform of the catalytic subunit, whereas the collecting duct expresses an alpha 3-like isoform. Because pharmacological studies have shown the existence of two populations of Na,K-ATPase with different sensitivities to ouabain in the rat cortical collecting duct, which may result from the presence in the same nephron segment of the two isoforms demonstrated in the different segments of the rabbit nephron, the present study was undertaken to characterize the properties of Na,K-ATPase along the rat nephron. Results indicate that each segment of the rat nephron contains two subpopulations of Na,K-ATPase: a component highly sensitive to ouabain (IC50 approximately 5.10(-6) M) which is recognized by an anti-alpha 3 antibody and another moiety of lower affinity for ouabain (IC50 approximately 5.10(-4) M) which is recognized by an anti-alpha 1 antibody. Whether these two subpopulations correspond to different isoforms of the alpha subunit of Na,K-ATPase (alpha 1 and alpha 3-like) remains to be determined.