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PMID: 1708821 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

K+ and Cl- currents in enterocytes isolated from guinea-pig small intestinal villi.

The Journal of physiology ·Vol. 434 ·1991-03-00 ·Pages 351-67

Sepúlveda FV, Fargon F, McNaughton PA

Abstract

1. The whole-cell configuration of the patch-clamp technique has been used to investigate the conductance properties of villus enterocytes isolated from guinea-pig small intestinal epithelium. 2. With near physiological ionic gradients inward and outward rectification was observed in the hyperpolarizing and depolarizing voltage domains respectively. 3. Replacement of intra- and extracellular K+ with N-methyl-D-glucamine (NMG) eliminated inward rectification but did not alter outward currents. In symmetrical low Cl- solutions outward currents were reduced but inward rectification was not affected. Under these conditions increases in extracellular K+ shifted both the current-voltage relation and the extrapolated reversal potential as expected for a K(+)-selective current. 4. The inwardly rectifying nature of the K+ current observed here remained unaltered after chelation of internal Mg2+ with ATP or EDTA. 5. Extracellular application of 5 mM-Ba2+ or 50 micrograms ml-1 of the venom of the scorpion Leiurus quinquestriatus abolished the inward K+ current, while 5 mM-extracellular tetraethylammonium (TEA) had little effect. 6. The current remaining in the presence of symmetrical Cl- solutions and in the complete absence of K+ rectified outwardly and reversed at 0 mV. The anionic nature of this current was confirmed by replacing Cl- with different anions. SCN- and Br- carried more current than Cl-, while F- and gluconate were less permeant. 7. Anionic currents of villus guinea-pig enterocytes were not stimulated by cyclic AMP and were strongly and reversibly inhibited by the Cl- channel blocker 5-nitro-2-(3-phenylpropylamino) benzoic acid (NPPB, 10(-5) M). 8. The inwardly rectifying K+ current described here shares some, but not all, characteristics with others previously described. It is postulated that this conductance might function to couple K+ permeability and the Na(+)-K+ pump rate in enterocytes. Absorption of chloride may be mediated by the Cl- channels.

MeSH Terms
Animals Barium/pharmacology Cell Separation/methods Chlorides/metabolism Epithelium/metabolism Female Gluconates/pharmacology Guinea Pigs Intestine, Small/metabolism Ion Channels/drug effects,metabolism Male Potassium/metabolism Potassium Channels/drug effects,metabolism Scorpion Venoms/pharmacology
Chemicals
Chlorides Gluconates Ion Channels Potassium Channels Scorpion Venoms Barium Potassium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sepúlveda F V
AFRC Institute of Animal Physiology and Genetics Research, Babraham, Cambridge.
Fargon F
McNaughton P A
References (29)
29 references, click to expand
  1. Potassium currents of isolated Necturus enterocytes: a whole-cell patch-clamp study.
    J Physiol. 1991 Feb;433:663-76 PMID: 1841962
  2. Conductance properties of single inwardly rectifying potassium channels in ventricular cells from guinea-pig heart.
    J Physiol. 1984 Feb;347:641-57 PMID: 6323703
  3. Possible involvement of GTP-binding proteins in the deactivation of an inwardly rectifying K+ current in enterocytes isolated from guinea-pig small intestine.
    Pflugers Arch. 1990 Oct;417(2):240-2 PMID: 1707517
  4. A chloride conductance activated by adenosine 3',5'-cyclic monophosphate in the apical membrane of Necturus enterocytes.
    J Physiol. 1988 Jan;395:597-623 PMID: 2457684
  5. Characterization of a phosphorylation-activated Cl-selective channel in isolated Necturus enterocytes.
    J Physiol. 1989 Sep;416:517-37 PMID: 2481731
  6. A rabbit jejunal isolated enterocyte preparation suitable for transport studies.
    J Physiol. 1985 Jun;363:257-70 PMID: 2862277
  7. Mechanism of anion permeation through channels gated by glycine and gamma-aminobutyric acid in mouse cultured spinal neurones.
    J Physiol. 1987 Apr;385:243-86 PMID: 2443667
  8. Anion and cation channels in the basolateral membrane of rabbit parietal cells.
    Pflugers Arch. 1989 Jun;414(2):185-92 PMID: 2474146
  9. An emerging pharmacology of peptide toxins targeted against potassium channels.
    J Membr Biol. 1988 Oct;105(2):95-111 PMID: 2464066
  10. Characterization of the inward-rectifying potassium current in cat ventricular myocytes.
    J Gen Physiol. 1988 Apr;91(4):593-615 PMID: 2455768
  11. K+ channels activated by L-alanine transport in isolated Necturus enterocytes.
    FEBS Lett. 1988 Jul 18;234(2):446-8 PMID: 2455660
  12. Potassium channels in Necturus proximal tubule.
    Am J Physiol. 1987 Sep;253(3 Pt 2):F488-94 PMID: 2443020
  13. Basolateral potassium channels in renal proximal tubule.
    Am J Physiol. 1987 Sep;253(3 Pt 2):F476-87 PMID: 2443019
  14. Inward rectification of a potassium channel in cardiac ventricular cells depends on internal magnesium ions.
    Proc Natl Acad Sci U S A. 1987 Apr;84(8):2560-4 PMID: 2436236
  15. Ohmic conductance through the inwardly rectifying K channel and blocking by internal Mg2+.
    Nature. 1987 Jan 8-14;325(7000):156-9 PMID: 2433601
  16. Leiurus quinquestriatus venom inhibits different kinds of Ca2+-dependent K+ channels.
    Biochim Biophys Acta. 1986 Apr 14;856(2):403-7 PMID: 2420362
  17. Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle.
    Nature. 1985 Jan 24-30;313(6000):316-8 PMID: 2578618
  18. Electroneutral, HCO3(-)-independent, pH gradient-dependent uphill transport of Cl- by ileal brush-border membrane vesicles. Possible role in the pathogenesis of chloridorrhea.
    Biochem J. 1989 Nov 1;263(3):775-84 PMID: 2597129
  19. Reconstitution of an inwardly rectifying potassium channel from the basolateral membranes of Necturus enterocytes into planar lipid bilayers.
    Proc Natl Acad Sci U S A. 1989 Jul;86(13):5212-6 PMID: 2740353
  20. Whole-cell potassium currents in single early distal tubule cells.
    Am J Physiol. 1988 Oct;255(4 Pt 2):F699-703 PMID: 3263054
  21. Kinetics of voltage- and Ca2+ activation and Ba2+ blockade of a large-conductance K+ channel from Necturus enterocytes.
    J Membr Biol. 1988 Oct;105(1):65-75 PMID: 3225837
  22. Catalytic subunit of cAMP-dependent protein kinase.
    Methods Enzymol. 1983;99:51-5 PMID: 6316099
  23. Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches.
    Pflugers Arch. 1981 Aug;391(2):85-100 PMID: 6270629
  24. A potential- and time-dependent blockade of inward rectification in frog skeletal muscle fibres by barium and strontium ions.
    J Physiol. 1978 Jul;280:169-91 PMID: 308537
  25. Blocking effects of barium and hydrogen ions on the potassium current during anomalous rectification in the starfish egg.
    J Physiol. 1978 Jun;279:167-85 PMID: 566793
  26. Anion selectivity in biological systems.
    Physiol Rev. 1977 Jan;57(1):109-56 PMID: 834775
  27. Na+, K+ and Cl- transport in isolated small intestinal cells from guinea pig. Evidences for the existence of a second Na+ pump.
    Biochim Biophys Acta. 1987 Jul 23;901(2):209-16 PMID: 3607047
  28. The use of hyperosmolar, intracellular-like solutions for the isolation of epithelial cells from guinea-pig small intestine.
    Biochim Biophys Acta. 1987 Jul 23;901(2):201-8 PMID: 3607046
  29. Two types of potassium currents seen in isolated Necturus enterocytes with the single-electrode voltage-clamp technique.
    J Physiol. 1991 Feb;433:645-61 PMID: 1841961
Article Info
Journal
The Journal of physiology
Abbr.
J Physiol
ISSN
0022-3751
Published
1991-03-00
Pages
351-67
Language
English
Region
England
NLM ID
0266262
PMCID
PMC1181422
Subset
IM
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