Localization and characterization of transport-related elements in the plasma membrane of turtle bladder epithelial cells

William A. Brodsky*, Z. I. Cabantchik, N. Davidson, Gerhard Ehrenspeck, Eva Marie Kinne-Saffran, Rolf Kinne

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

A mixed membrane preparation obtained from turtle bladder epithelial cells contains (Na+ + K+)-ATPase, adenylate cyclase and protein kinase, which interact with ouabain, norepinephrine and cyclic AMP, respectively. When such a preparation is obtained from bladders which had been preexposed to serosal fluids containing the tritiated form of 4,4′-diisothiocyano-2,2′-disulfonic stilbene, the subsequently isolated membrane proteins are enriched in tritium as well as in the afore-mentioned enzymes, none of which is inhibited. Freeflow electrophoresis separates the mixed membrane preparation into two distinguishable groups: one, construed as apical membranes, is enriched in norepinephrine-sensitive adenylate cyclase and cyclic AMP-sensitive protein kinase; the other, construed as basal-lateral membranes, is enriched in ouabain-sensitive ATPase and 4,4′-diisothiocyano-2,2′-disulfonic stilbene-binding proteins. The physiological counterparts of these enzymatically defined membrane markers are the mucosal sidedness of the transport effects of norepinephrine and cyclic AMP derivatives and the serosal sidedness of the transport effects of ouabain and disulfonic stilbenes in the intact turtle bladder. The discreteness and ion selectivity of each membrane-bound, transport-related element are discussed in relation to the corresponding characteristics of each transport process in vivo; the possibility of regulation of anion transport by adenylate cyclase-protein kinase system is also discussed.

Original languageEnglish
Pages (from-to)490-508
Number of pages19
JournalBiochimica et Biophysica Acta - Biomembranes
Volume556
Issue number3
DOIs
StatePublished - 5 Oct 1979

Keywords

  • (Na + K)-ATPase
  • (Turtle bladder)
  • Adenylate cyclase
  • DIDS-binding protein
  • Protein kinase
  • Transport

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