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Distribution of membrane-bound cyclic AMP-dependent protein kinase in plasma membranes of cells of the kidney cortex

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Kinne,  Rolf
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Physiology and Biophysics, Mount Sinai Medical and Graduate Schools of the City University of New York, 10029, New York, N.Y.;

/persons/resource/persons260904

Shlatz,  Linda J.
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Physiology and Biophysics, Mount Sinai Medical and Graduate Schools of the City University of New York, 10029, New York, N.Y.;

/persons/resource/persons257981

Kinne-Saffran,  Evamaria
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Physiology and Biophysics, Mount Sinai Medical and Graduate Schools of the City University of New York, 10029, New York, N.Y.;

/persons/resource/persons260906

Schwartz,  Irving L.
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Physiology and Biophysics, Mount Sinai Medical and Graduate Schools of the City University of New York, 10029, New York, N.Y.;

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Citation

Kinne, R., Shlatz, L. J., Kinne-Saffran, E., & Schwartz, I. L. (1975). Distribution of membrane-bound cyclic AMP-dependent protein kinase in plasma membranes of cells of the kidney cortex. Journal of Membrane Biology, 24(2), 145-159. doi:10.1007/BF01868620.


Cite as: https://hdl.handle.net/21.11116/0000-0008-9E69-1
Abstract
Renal cortical plasms membranes were separated by free flow electrophoresis into luminal (brush border microvilli) and contraluminal (basal-lateral membrane) fractions. These membranes were found to contain an intrinsic, self-phosphorylating system which consists of a cyclic AMP-dependent protein kinase, a phosphorprotein phosphatase and the substrate(s) of these enzymes. The kinase, but not the phosphatase, was stimulated by cyclic AMP; maximal (1.7-fold) stimulation was effected at a cyclic AMP concentration of 0.1 muM. The degree of phosphorylation of the brush borders was six times greater than that of the basal-lateral membranes in the absence of cyclic AMP and 2.3-fold greater in the presence of cyclic AMP. This preferential phosphorylation of the luminal membrane by membrane-associated protein kinase(s) may play a role in the parathyroid hormone-mediated alterations of solute reabsorption in the proximal tubule.