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AJP - Renal Physiology, Vol 265, Issue 6 743-F755, Copyright © 1993 by American Physiological Society
ARTICLES |
A. M. Bertorello and A. I. Katz
Rolf Luft Center for Diabetes Research, Department of Endocrinology, Karolinska Institutet, Karolinska Hospital, Stockholm, Sweden.
Sodium-potassium-activated adenosinetriphosphatase (Na-K-ATPase; the Na:K pump), located at the basolateral domain of epithelial cells, provides the driving force for active sodium and potassium translocation and for the secondary active transport of other solutes across the renal tubules. Short-term regulation of renal Na-K-ATPase activity (i.e., not reflecting changes in its biosynthesis rate) provides an important mechanism of modulating tubule transport and thus the final Na and K urinary excretion. Recent studies have provided abundant evidence that such regulation is effected by complex functional networks that are specific for different nephron segments and involve distinct and often mutually interacting intracellular signal transduction pathways. The effects of hormones and autacoids linked to alterations in cell adenosine 3',5'-cyclic monophosphate and consequently of protein kinase A, in the levels and distribution of protein kinase C, or in the generation of various eicosanoids provide examples of rapid Na:K pump activity modulation by the mechanisms mentioned above. In this review we assess the roles of specific intracellular messengers and the manner in which they, and especially protein kinases, might interact with the pump in the short-term regulation of its activity; also, we examine the emerging evidence supporting the participation of the cytoskeleton in this process.
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A. V. Chibalin, J. R. Zierath, A. I. Katz, P.-O. Berggren, and A. M. Bertorello Phosphatidylinositol 3-Kinase-mediated Endocytosis of Renal Na+,K+-ATPase alpha Subunit in Response to Dopamine Mol. Biol. Cell, May 1, 1998; 9(5): 1209 - 1220. [Abstract] [Full Text]
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A. V. Chibalin, A. I. Katz, P.-O. Berggren, and A. M. Bertorello Receptor-mediated inhibition of renal Na+-K+-ATPase is associated with endocytosis of its alpha - and beta -subunits Am J Physiol Cell Physiol, November 1, 1997; 273(5): C1458 - C1465. [Abstract] [Full Text] [PDF]
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L. Ragolia, B. Cherpalis, M. Srinivasan, and N. Begum Role of Serine/Threonine Protein Phosphatases in Insulin Regulation of Na+/K+-ATPase Activity in Cultured Rat Skeletal Muscle Cells J. Biol. Chem., September 19, 1997; 272(38): 23653 - 23658. [Abstract] [Full Text] [PDF]
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M. L. BARNARD, W. G. OLIVERA, D. M. RUTSCHMAN, A. M. BERTORELLO, A. I. KATZ, and J. I. SZNAJDER Dopamine Stimulates Sodium Transport and Liquid Clearance in Rat Lung Epithelium Am. J. Respir. Crit. Care Med., September 1, 1997; 156(3): 709 - 714. [Abstract] [Full Text] [PDF]
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 C. H. Pedemonte, T. A. Pressley, A. R. Cinelli, and M. F. Lokhandwala Stimulation of Protein Kinase C Rapidly Reduces Intracellular Na+ Concentration via Activation of the Na+ Pump in OK Cells Mol. Pharmacol., July 1, 1997; 52(1): 88 - 97. [Abstract] [Full Text]
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 G. Ogimoto, G. A. Yudowski, C. J. Barker, M. Kohler, A. I. Katz, E. Feraille, C. H. Pedemonte, P.-O. Berggren, and A. M. Bertorello G protein-coupled receptors regulate Na+,K+-ATPase activity and endocytosis by modulating the recruitment of adaptor protein 2 and clathrin PNAS, March 28, 2000; 97(7): 3242 - 3247. [Abstract] [Full Text] [PDF]
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G. A. Yudowski, R. Efendiev, C. H. Pedemonte, A. I. Katz, P.-O. Berggren, and A. M. Bertorello Phosphoinositide-3 kinase binds to a proline-rich motif in the Na+,K+-ATPase alpha subunit and regulates its trafficking PNAS, June 6, 2000; 97(12): 6556 - 6561. [Abstract] [Full Text] [PDF]
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