ArticleThe Journal of membrane biology1993
Pharmacology of the SV channel in the vacuolar membrane of Chenopodium rubrum suspension cells.
Article in The Journal of membrane biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 22 citations in OpenAlex.
- Vacuolar ion channels in the liverwort Marchantia polymorpha: influence of ion channel inhibitors.Planta · 2017Article
- Sodium fluxes through nonselective cation channels in the plasma membrane of protoplasts from Arabidopsis roots.Plant physiology · 2002Article
- Cooperative block of the plant endomembrane ion channel by ruthenium red.Biophysical journal · 1999Article
- Calcineurin, a Type 2B Protein Phosphatase, Modulates the Ca2+-Permeable Slow Vacuolar Ion Channel of Stomatal Guard Cells.The Plant cell · 1995Article
- Green circuits--the potential of plant specific ion channels.Plant molecular biology · 1994Review
- Properties of the K+ inward rectifier in the plasma membrane of xylem parenchyma cells from barley roots: effects of TEA+, Ca2+, Ba2+ and La3+.The Journal of membrane biology · 1994Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single channel performance and deactivation currents have been analyzed in the presence of cation channel blockers to reveal pharmacological properties of the slow-activating (SV) cation-selective ion channel in the vacuolar membrane (tonoplast) isolated from suspension cells of Chenopodium rubrum L. At a holding potential of -100 mV, the SV channel showed half-maximal inhibition with 20 mM tetraethylammonium (TEA), 7 microM 9-amino-acridine, 6 microM (+)-tubocurarine, 300 nM quinacrine, and 35 microM quinine, respectively. The SV channel is also blocked by charybdotoxin (20 nM at -80 mV) but not by apamine. 9-Amino-acridine, (+)-tubocurarine and quinacrine act in a voltage-dependent fashion, binding to the open channel and to different sites along the transmembrane voltage profile according to Woodhull (J. Gen. Physiol. 61:687-708, 1973). No binding site could be specified for charybdotoxin, which binds to the closed channel, and for quinine. Except for quinine, all tested blockers were effective only if added to the cytoplasmic side of the tonoplast. A structural relationship between the SV channel and Maxi-K channels in animal systems is inferred.
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