Determining the target of membrane sterols on voltage-gated potassium channels.


Journal

Biochimica et biophysica acta. Molecular and cell biology of lipids
ISSN: 1879-2618
Titre abrégé: Biochim Biophys Acta Mol Cell Biol Lipids
Pays: Netherlands
ID NLM: 101731727

Informations de publication

Date de publication:
03 2019
Historique:
received: 28 09 2018
revised: 30 11 2018
accepted: 12 12 2018
pubmed: 17 12 2018
medline: 10 9 2019
entrez: 17 12 2018
Statut: ppublish

Résumé

Cholesterol, an essential lipid component of cellular plasma membranes, regulates fluidity, mechanical integrity, raft structure and may specifically interact with membrane proteins. Numerous effects on ion channels by cholesterol, including changes in current amplitude, voltage dependence and gating kinetics, have been reported. We have previously described such changes in the voltage-gated potassium channel K

Identifiants

pubmed: 30553843
pii: S1388-1981(18)30307-X
doi: 10.1016/j.bbalip.2018.12.006
pii:
doi:

Substances chimiques

Potassium Channels, Voltage-Gated 0
Sterols 0
Xenopus Proteins 0
beta-Cyclodextrins 0
methyl-beta-cyclodextrin 0
Cholesterol 97C5T2UQ7J
Cysteine K848JZ4886

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

312-325

Informations de copyright

Copyright © 2018 Elsevier B.V. All rights reserved.

Auteurs

Florina Zakany (F)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary.

Pal Pap (P)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary; MTA-DE-NAP B Ion Channel Structure-Function Research Group, RCMM, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary.

Ferenc Papp (F)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary; MTA-DE-NAP B Ion Channel Structure-Function Research Group, RCMM, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary.

Tamas Kovacs (T)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary.

Peter Nagy (P)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary.

Maria Peter (M)

Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Temesvari Krt. 62, Szeged H-6726, Hungary.

Lajos Szente (L)

CycloLab Cyclodextrin R & D Laboratory Ltd., Illatos u. 7, Budapest H-1097, Hungary.

Gyorgy Panyi (G)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary; MTA-DE-NAP B Ion Channel Structure-Function Research Group, RCMM, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary.

Zoltan Varga (Z)

Division of Biophysics, Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary; MTA-DE-NAP B Ion Channel Structure-Function Research Group, RCMM, University of Debrecen, Egyetem ter 1, Debrecen H-4032, Hungary. Electronic address: veze@med.unideb.hu.

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Classifications MeSH