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Distribution of parathyroid hormone-stimulated adenylate cyclase in plasma membranes of cells of the kidney cortex

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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.; USA;

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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.; USA;

/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.; USA;

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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.; USA;

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Citation

Shlatz, L. J., Schwartz, I. L., Kinne-Saffran, E., & Kinne, R. (1975). Distribution of parathyroid hormone-stimulated adenylate cyclase in plasma membranes of cells of the kidney cortex. Journal of Membrane Biology, 24(2), 131-144. doi:10.1007/BF01868619.


Cite as: http://hdl.handle.net/21.11116/0000-0008-BB2C-5
Abstract
Free flow electrophoresis was employed to separate renal cortical plasma membranes into luminal (brush border microvilli) and contraluminal (basal-lateral membrane) fractions. During the separation adenylate cyclase activity was found to parallel the activity of Na+-K+-activated ATPase, an enzyme which is present in contraluminal but not in luminal membranes. In the basal-lateral membrane fraction the specific activities of adenylate cyclase and Na+-K+-activated ATPase were 4.4 and 4.6 times greater, respectively, than in the brush border fraction. The adenylate cyclase of the basal-lateral membrane fraction was specifically stimulated by parathyroid hormone which maximally increased enzyme activity eightfold. The biologically active (1-34) peptide fragment of paratyhroid hormone produced a 350% increase in adenylate cyclase activity. In contrast, calcitonin, epinephrine and vasopressin maximally stimulated the enzyme by only 55, 35 and 30%, respectively. These results indicate that adenylate cyclase, specifically stimulated by parathyroid hormone, is distributed preferentially in the contraluminal region of the plasma membrane of renal cortical epithelial cells.