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PMID: 8519990 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Induction of endogenous channels by high levels of heterologous membrane proteins in Xenopus oocytes.

Biophysical journal ·Vol. 69 ·No. 3 ·1995-09-00 ·Pages 904-8

Tzounopoulos T, Maylie J, Adelman JP

Abstract

Xenopus oocytes are widely employed for heterologous expression of cloned proteins, particularly electrogenic molecules such as ion channels and transporters. The high levels of expression readily obtained permit detailed investigations without interference from endogenous conductances. Injection of min K mRNA into Xenopus oocytes results in expression of voltage-dependent potassium-selective channels. Recent data show that injections of high concentrations of min K mRNA also induce a chloride current with very different biophysical, pharmacological, and regulatory properties from the min K potassium current. This led to the suggestion that the min K protein acts as an inducer of endogenous, normally silent oocyte ion channels. We now report that high levels of heterologous expression of many membrane proteins in Xenopus oocytes specifically induce this chloride current and a hyperpolarization-activated cation-selective current. The current is blocked by 4,4'-diisothiocyanostilbene-2-2'-disulphonic acid and tetraethylammonium, enhanced by clofilium, and is pH-sensitive. Criteria are presented that distinguish this endogenous current from those due to heterologous expression of electrogenic proteins in Xenopus oocytes. Together with structure-function studies, these results support the hypothesis that the min K protein comprises a potassium-selective channel.

MeSH Terms
4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid/analogs & derivatives,pharmacology Animals Calcium/pharmacology Chloride Channels/antagonists & inhibitors,biosynthesis,physiology Cloning, Molecular Cross-Linking Reagents/pharmacology Female Gene Expression Membrane Potentials Membrane Proteins/biosynthesis Oocytes/physiology Potassium Channels/biosynthesis,physiology Recombinant Proteins/biosynthesis Xenopus
Chemicals
Chloride Channels Cross-Linking Reagents Membrane Proteins Potassium Channels Recombinant Proteins dihydro-DIDS 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tzounopoulos T
Vollum Institute, Department of Molecular and Medical Genetics, Oregon Health Sciences University, Portland 97201, USA.
Maylie J
Adelman J P
References (20)
20 references, click to expand
  1. Chloride current induced by injection of calcium into Xenopus oocytes.
    J Physiol. 1984 Dec;357:173-83 PMID: 6096530
  2. Cloning and expression of a family of inward rectifier potassium channels.
    Receptors Channels. 1994;2(3):183-91 PMID: 7874445
  3. A calcium-independent chloride current activated by hyperpolarization in Xenopus oocytes.
    Proc R Soc Lond B Biol Sci. 1988 Mar 22;233(1271):191-9 PMID: 2454476
  4. Cloning of a membrane protein that induces a slow voltage-gated potassium current.
    Science. 1988 Nov 18;242(4881):1042-5 PMID: 3194754
  5. Cloning and expression of a rat D2 dopamine receptor cDNA.
    Nature. 1988 Dec 22-29;336(6201):783-7 PMID: 2974511
  6. Expression of a cloned rat brain potassium channel in Xenopus oocytes.
    Science. 1989 Apr 14;244(4901):221-4 PMID: 2539643
  7. Molecular basis of potassium channel diversity.
    Pflugers Arch. 1989;414 Suppl 1:S71-5 PMID: 2674893
  8. Site-specific mutations in a minimal voltage-dependent K+ channel alter ion selectivity and open-channel block.
    Neuron. 1991 Sep;7(3):403-8 PMID: 1910787
  9. Alteration of channel activities and gating by mutations of slow ISK potassium channel.
    J Biol Chem. 1991 Nov 25;266(33):22192-8 PMID: 1939241
  10. Novel voltage clamp to record small, fast currents from ion channels expressed in Xenopus oocytes.
    Biophys J. 1992 Jan;61(1):78-82 PMID: 1311612
  11. Calcium-activated potassium channels expressed from cloned complementary DNAs.
    Neuron. 1992 Aug;9(2):209-16 PMID: 1497890
  12. Cloning and expression of an inwardly rectifying ATP-regulated potassium channel.
    Nature. 1993 Mar 4;362(6415):31-8 PMID: 7680431
  13. Primary structure and functional expression of a mouse inward rectifier potassium channel.
    Nature. 1993 Mar 11;362(6416):127-33 PMID: 7680768
  14. Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel.
    Nature. 1993 Aug 26;364(6440):802-6 PMID: 8355805
  15. The protein IsK is a dual activator of K+ and Cl- channels.
    Nature. 1993 Oct 28;365(6449):850-2 PMID: 8413671
  16. Atrial G protein-activated K+ channel: expression cloning and molecular properties.
    Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10235-9 PMID: 8234283
  17. The minK potassium channel exists in functional and nonfunctional forms when expressed in the plasma membrane of Xenopus oocytes.
    J Neurosci. 1994 May;14(5 Pt 2):3097-105 PMID: 7514215
  18. Hyperpolarization-activated chloride currents in Xenopus oocytes.
    J Gen Physiol. 1994 Feb;103(2):217-30 PMID: 7514644
  19. Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex.
    J Neurosci. 1994 Sep;14(9):5559-69 PMID: 7521911
  20. Expression of functional potassium channels from Shaker cDNA in Xenopus oocytes.
    Nature. 1988 Jan 14;331(6152):143-5 PMID: 2448636
Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1995-09-00
Pages
904-8
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1236319
Subset
IM
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