---
_id: '12925'
abstract:
- lang: eng
  text: Normal function of organs and cells is tightly linked to the cytoarchitecture.
    Control of the cell volume is therefore vital for the organism. A widely established
    strategy of cells to counteract swelling is the activation of chloride and potassium
    channels, which leads to a net efflux of salt followed by water - a process termed
    regulatory volume decrease. Since there is evidence for swelling-dependent chloride
    channels (IClswell) being activated also during pathological processes, the identification
    of the molecular entity underlying IClswell is of utmost importance. Several proteins
    are discussed as the channel forming IClswell, i.e. phospholemman, p-glycoprotein,
    CLC-3 and ICln. In this review we would like to focus on the properties of ICln,
    a protein cloned from a Madin Darby canine kidney (MDCK) cell library whose expression
    in Xenopus laevis oocytes resulted in a nucleotide sensitive outwardly rectifying
    chloride current closely resembling the biophysical properties of IClswell.
article_processing_charge: No
article_type: original
author:
- first_name: Johannes
  full_name: Fürst, Johannes
  last_name: Fürst
- first_name: Martin
  full_name: Jakab, Martin
  last_name: Jakab
- first_name: Matthias
  full_name: König, Matthias
  last_name: König
- first_name: Markus
  full_name: Ritter, Markus
  last_name: Ritter
- first_name: Martin
  full_name: Gschwentner, Martin
  last_name: Gschwentner
- first_name: Jakob
  full_name: Rudzki, Jakob
  last_name: Rudzki
- first_name: Johann G
  full_name: Danzl, Johann G
  id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
  last_name: Danzl
  orcid: 0000-0001-8559-3973
- first_name: Michael
  full_name: Mayer, Michael
  last_name: Mayer
- first_name: Carmen M.
  full_name: Burtscher, Carmen M.
  last_name: Burtscher
- first_name: Julia
  full_name: Schirmer, Julia
  last_name: Schirmer
- first_name: Brigitte
  full_name: Maier, Brigitte
  last_name: Maier
- first_name: Manfred
  full_name: Nairz, Manfred
  last_name: Nairz
- first_name: Sabine
  full_name: Chwatal, Sabine
  last_name: Chwatal
- first_name: Markus
  full_name: Paulmichl, Markus
  last_name: Paulmichl
citation:
  ama: Fürst J, Jakab M, König M, et al. Structure and Function of the Ion Channel
    ICln. <i>Cellular Physiology and Biochemistry</i>. 2000;10(5-6):329-334. doi:<a
    href="https://doi.org/10.1159/000016374">10.1159/000016374</a>
  apa: Fürst, J., Jakab, M., König, M., Ritter, M., Gschwentner, M., Rudzki, J., …
    Paulmichl, M. (2000). Structure and Function of the Ion Channel ICln. <i>Cellular
    Physiology and Biochemistry</i>. S. Karger AG. <a href="https://doi.org/10.1159/000016374">https://doi.org/10.1159/000016374</a>
  chicago: Fürst, Johannes, Martin Jakab, Matthias König, Markus Ritter, Martin Gschwentner,
    Jakob Rudzki, Johann G Danzl, et al. “Structure and Function of the Ion Channel
    ICln.” <i>Cellular Physiology and Biochemistry</i>. S. Karger AG, 2000. <a href="https://doi.org/10.1159/000016374">https://doi.org/10.1159/000016374</a>.
  ieee: J. Fürst <i>et al.</i>, “Structure and Function of the Ion Channel ICln,”
    <i>Cellular Physiology and Biochemistry</i>, vol. 10, no. 5–6. S. Karger AG, pp.
    329–334, 2000.
  ista: Fürst J, Jakab M, König M, Ritter M, Gschwentner M, Rudzki J, Danzl JG, Mayer
    M, Burtscher CM, Schirmer J, Maier B, Nairz M, Chwatal S, Paulmichl M. 2000. Structure
    and Function of the Ion Channel ICln. Cellular Physiology and Biochemistry. 10(5–6),
    329–334.
  mla: Fürst, Johannes, et al. “Structure and Function of the Ion Channel ICln.” <i>Cellular
    Physiology and Biochemistry</i>, vol. 10, no. 5–6, S. Karger AG, 2000, pp. 329–34,
    doi:<a href="https://doi.org/10.1159/000016374">10.1159/000016374</a>.
  short: J. Fürst, M. Jakab, M. König, M. Ritter, M. Gschwentner, J. Rudzki, J.G.
    Danzl, M. Mayer, C.M. Burtscher, J. Schirmer, B. Maier, M. Nairz, S. Chwatal,
    M. Paulmichl, Cellular Physiology and Biochemistry 10 (2000) 329–334.
date_created: 2023-05-08T09:04:58Z
date_published: 2000-01-01T00:00:00Z
date_updated: 2023-05-08T10:07:10Z
doi: 10.1159/000016374
extern: '1'
external_id:
  pmid:
  - '11125213'
intvolume: '        10'
issue: 5-6
keyword:
- Physiology
language:
- iso: eng
oa_version: None
page: 329-334
pmid: 1
publication: Cellular Physiology and Biochemistry
publication_identifier:
  issn:
  - 1015-8987
  - 1421-9778
publication_status: published
publisher: S. Karger AG
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure and Function of the Ion Channel ICln
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10
year: '2000'
...
---
_id: '3473'
abstract:
- lang: eng
  text: Sixteen different K+ channel subtypes have been cloned from mammalian tissue.
    Considering their sequence homology to Drosophila Shaker, Shab, Shaw and Shal
    channels, they were classified into four corresponding classes Kv1-4. All K+ channels
    belonging to these classes consist of four subunits with each six hydrophobic
    segments (S1-S6) and a characteristic structure-function relationship of certain
    domains in their amino acid sequence. These domains are, the inactivation gate
    in the N-terminal region of the sequence, the voltage sensor in the fourth hydrophobic
    segment (S4), and the pore-region in the H5 segment between S5 and S6. In some
    functional properties K+ channels cloned from the mammalian brain, however, differ
    from Drosophila K+ channels. These are pharmacological differences, differences
    in the threshold of activation and in regulation of inactivation. Part of these
    differences are important to understand their physiological role in the brain.
    Based on their functional characteristics the expression pattern of cloned K+
    channels in the rat brain can be correlated with the properties of K+ currents
    measured in central neurones.
article_processing_charge: No
article_type: original
author:
- first_name: Peter
  full_name: Ruppersberg, Peter
  last_name: Ruppersberg
- first_name: Mamfred
  full_name: Ermler, Mamfred
  last_name: Ermler
- first_name: Martin
  full_name: Knopf, Martin
  last_name: Knopf
- first_name: Wilfried
  full_name: Kues, Wilfried
  last_name: Kues
- first_name: Peter M
  full_name: Jonas, Peter M
  id: 353C1B58-F248-11E8-B48F-1D18A9856A87
  last_name: Jonas
  orcid: 0000-0001-5001-4804
- first_name: Michael
  full_name: Koenen, Michael
  last_name: Koenen
citation:
  ama: Ruppersberg P, Ermler M, Knopf M, Kues W, Jonas PM, Koenen M. Properties of
    Shaker-homologous potassium channels expressed in the mammalian brain. <i>Cellular
    Physiology and Biochemistry</i>. 1993;3:250-269. doi:<a href="https://doi.org/10.1159/000154691">10.1159/000154691</a>
  apa: Ruppersberg, P., Ermler, M., Knopf, M., Kues, W., Jonas, P. M., &#38; Koenen,
    M. (1993). Properties of Shaker-homologous potassium channels expressed in the
    mammalian brain. <i>Cellular Physiology and Biochemistry</i>. S. Karger AG. <a
    href="https://doi.org/10.1159/000154691">https://doi.org/10.1159/000154691</a>
  chicago: Ruppersberg, Peter, Mamfred Ermler, Martin Knopf, Wilfried Kues, Peter
    M Jonas, and Michael Koenen. “Properties of Shaker-Homologous Potassium Channels
    Expressed in the Mammalian Brain.” <i>Cellular Physiology and Biochemistry</i>.
    S. Karger AG, 1993. <a href="https://doi.org/10.1159/000154691">https://doi.org/10.1159/000154691</a>.
  ieee: P. Ruppersberg, M. Ermler, M. Knopf, W. Kues, P. M. Jonas, and M. Koenen,
    “Properties of Shaker-homologous potassium channels expressed in the mammalian
    brain.,” <i>Cellular Physiology and Biochemistry</i>, vol. 3. S. Karger AG, pp.
    250–269, 1993.
  ista: Ruppersberg P, Ermler M, Knopf M, Kues W, Jonas PM, Koenen M. 1993. Properties
    of Shaker-homologous potassium channels expressed in the mammalian brain. Cellular
    Physiology and Biochemistry. 3, 250–269.
  mla: Ruppersberg, Peter, et al. “Properties of Shaker-Homologous Potassium Channels
    Expressed in the Mammalian Brain.” <i>Cellular Physiology and Biochemistry</i>,
    vol. 3, S. Karger AG, 1993, pp. 250–69, doi:<a href="https://doi.org/10.1159/000154691">10.1159/000154691</a>.
  short: P. Ruppersberg, M. Ermler, M. Knopf, W. Kues, P.M. Jonas, M. Koenen, Cellular
    Physiology and Biochemistry 3 (1993) 250–269.
date_created: 2018-12-11T12:03:31Z
date_published: 1993-01-01T00:00:00Z
date_updated: 2022-03-30T10:21:04Z
day: '01'
doi: 10.1159/000154691
extern: '1'
intvolume: '         3'
language:
- iso: eng
main_file_link:
- url: https://www.karger.com/Article/Abstract/154691
month: '01'
oa_version: None
page: 250 - 269
publication: Cellular Physiology and Biochemistry
publication_identifier:
  issn:
  - 1015-8987
publication_status: published
publisher: S. Karger AG
publist_id: '2914'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Properties of Shaker-homologous potassium channels expressed in the mammalian
  brain.
type: journal_article
user_id: ea97e931-d5af-11eb-85d4-e6957dddbf17
volume: 3
year: '1993'
...