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

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.

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 Creators:
Kinne, Rolf1, 2, Author           
Shlatz, Linda J.1, 2, Author           
Kinne-Saffran, Evamaria1, 2, Author           
Schwartz, Irving L.1, 2, Author           
Affiliations:
1Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              
2Department of Physiology and Biophysics, Mount Sinai Medical and Graduate Schools of the City University of New York, 10029, New York, N.Y., ou_persistent22              

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Free keywords: Plasma Membrane; Protein Kinase; Luminal; Proximal Tubule; Brush Border
 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.

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Language(s): eng - English
 Dates: 1975-07-081975-04-241975-11-07
 Publication Status: Published in print
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/BF01868620
PMID: 172638
 Degree: -

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Title: Journal of Membrane Biology
  Other : J. Membr. Biol.
Source Genre: Journal
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Publ. Info: New York : Springer-Verlag New York
Pages: - Volume / Issue: 24 (2) Sequence Number: - Start / End Page: 145 - 159 Identifier: ISSN: 0022-2631
CoNE: https://pure.mpg.de/cone/journals/resource/954925415943