Subtype-specific, bi-component inhibition of SK channels by low internal pH.

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Standard

Subtype-specific, bi-component inhibition of SK channels by low internal pH. / Peitersen, Torben; Jespersen, Thomas; Jorgensen, Nanna K; Olesen, Søren-Peter; Grunnet, Morten.

I: Biochemical and Biophysical Research Communications, Bind 343, Nr. 3, 2006, s. 943-9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Peitersen, T, Jespersen, T, Jorgensen, NK, Olesen, S-P & Grunnet, M 2006, 'Subtype-specific, bi-component inhibition of SK channels by low internal pH.', Biochemical and Biophysical Research Communications, bind 343, nr. 3, s. 943-9. https://doi.org/10.1016/j.bbrc.2006.03.026

APA

Peitersen, T., Jespersen, T., Jorgensen, N. K., Olesen, S-P., & Grunnet, M. (2006). Subtype-specific, bi-component inhibition of SK channels by low internal pH. Biochemical and Biophysical Research Communications, 343(3), 943-9. https://doi.org/10.1016/j.bbrc.2006.03.026

Vancouver

Peitersen T, Jespersen T, Jorgensen NK, Olesen S-P, Grunnet M. Subtype-specific, bi-component inhibition of SK channels by low internal pH. Biochemical and Biophysical Research Communications. 2006;343(3):943-9. https://doi.org/10.1016/j.bbrc.2006.03.026

Author

Peitersen, Torben ; Jespersen, Thomas ; Jorgensen, Nanna K ; Olesen, Søren-Peter ; Grunnet, Morten. / Subtype-specific, bi-component inhibition of SK channels by low internal pH. I: Biochemical and Biophysical Research Communications. 2006 ; Bind 343, Nr. 3. s. 943-9.

Bibtex

@article{bcc91440ab5411ddb5e9000ea68e967b,
title = "Subtype-specific, bi-component inhibition of SK channels by low internal pH.",
abstract = "The effects of low intracellular pH (pH(i) 6.4) on cloned small-conductance Ca2+-activated K+ channel currents of all three subtypes (SK1, SK2, and SK3) were investigated in HEK293 cells using the patch-clamp technique. In 400 nM internal Ca2+ [Ca2+]i, all subtypes were inhibited by pH(i) 6.4 in the order of sensitivity: SK1>SK3>SK2. The inhibition increased with the transmembrane voltage. In saturating internal Ca2+, the inhibition was abolished for SK1-3 channels at negative potentials, indicating a [Ca2+]i-dependent mode of inhibition. Application of 50 microM 1-ethyl-2-benzimidazolone was able to potentiate SK3 current to the same extent as at neutral pH(i). We conclude that SK1-3 all are inhibited by low pH(i). We suggest two components of inhibition: a [Ca2+]i-dependent component, likely involving the SK beta-subunits calmodulin, and a voltage-dependent component, consistent with a pore-blocking effect. This pH(i)-dependent inhibition can be reversed pharmacologically.",
author = "Torben Peitersen and Thomas Jespersen and Jorgensen, {Nanna K} and S{\o}ren-Peter Olesen and Morten Grunnet",
note = "Keywords: Animals; Benzimidazoles; Calcium; Cell Line; Electric Conductivity; Humans; Hydrogen-Ion Concentration; Patch-Clamp Techniques; Rats; Small-Conductance Calcium-Activated Potassium Channels",
year = "2006",
doi = "10.1016/j.bbrc.2006.03.026",
language = "English",
volume = "343",
pages = "943--9",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Subtype-specific, bi-component inhibition of SK channels by low internal pH.

AU - Peitersen, Torben

AU - Jespersen, Thomas

AU - Jorgensen, Nanna K

AU - Olesen, Søren-Peter

AU - Grunnet, Morten

N1 - Keywords: Animals; Benzimidazoles; Calcium; Cell Line; Electric Conductivity; Humans; Hydrogen-Ion Concentration; Patch-Clamp Techniques; Rats; Small-Conductance Calcium-Activated Potassium Channels

PY - 2006

Y1 - 2006

N2 - The effects of low intracellular pH (pH(i) 6.4) on cloned small-conductance Ca2+-activated K+ channel currents of all three subtypes (SK1, SK2, and SK3) were investigated in HEK293 cells using the patch-clamp technique. In 400 nM internal Ca2+ [Ca2+]i, all subtypes were inhibited by pH(i) 6.4 in the order of sensitivity: SK1>SK3>SK2. The inhibition increased with the transmembrane voltage. In saturating internal Ca2+, the inhibition was abolished for SK1-3 channels at negative potentials, indicating a [Ca2+]i-dependent mode of inhibition. Application of 50 microM 1-ethyl-2-benzimidazolone was able to potentiate SK3 current to the same extent as at neutral pH(i). We conclude that SK1-3 all are inhibited by low pH(i). We suggest two components of inhibition: a [Ca2+]i-dependent component, likely involving the SK beta-subunits calmodulin, and a voltage-dependent component, consistent with a pore-blocking effect. This pH(i)-dependent inhibition can be reversed pharmacologically.

AB - The effects of low intracellular pH (pH(i) 6.4) on cloned small-conductance Ca2+-activated K+ channel currents of all three subtypes (SK1, SK2, and SK3) were investigated in HEK293 cells using the patch-clamp technique. In 400 nM internal Ca2+ [Ca2+]i, all subtypes were inhibited by pH(i) 6.4 in the order of sensitivity: SK1>SK3>SK2. The inhibition increased with the transmembrane voltage. In saturating internal Ca2+, the inhibition was abolished for SK1-3 channels at negative potentials, indicating a [Ca2+]i-dependent mode of inhibition. Application of 50 microM 1-ethyl-2-benzimidazolone was able to potentiate SK3 current to the same extent as at neutral pH(i). We conclude that SK1-3 all are inhibited by low pH(i). We suggest two components of inhibition: a [Ca2+]i-dependent component, likely involving the SK beta-subunits calmodulin, and a voltage-dependent component, consistent with a pore-blocking effect. This pH(i)-dependent inhibition can be reversed pharmacologically.

U2 - 10.1016/j.bbrc.2006.03.026

DO - 10.1016/j.bbrc.2006.03.026

M3 - Journal article

C2 - 16566895

VL - 343

SP - 943

EP - 949

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

ID: 8418707