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Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity

BK channels are potassium selective and exhibit large single-channel conductance. They play an important physiological role in glioma cells: they are involved in cell growth and extensive migrating behavior. Due to the fact that these processes are accompanied by changes in membrane stress, here, we...

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Autores principales: Wawrzkiewicz-Jałowiecka, Agata, Trybek, Paulina, Machura, Łukasz, Dworakowska, Beata, Grzywna, Zbigniew J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6244768/
https://www.ncbi.nlm.nih.gov/pubmed/30094475
http://dx.doi.org/10.1007/s00232-018-0044-9
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author Wawrzkiewicz-Jałowiecka, Agata
Trybek, Paulina
Machura, Łukasz
Dworakowska, Beata
Grzywna, Zbigniew J.
author_facet Wawrzkiewicz-Jałowiecka, Agata
Trybek, Paulina
Machura, Łukasz
Dworakowska, Beata
Grzywna, Zbigniew J.
author_sort Wawrzkiewicz-Jałowiecka, Agata
collection PubMed
description BK channels are potassium selective and exhibit large single-channel conductance. They play an important physiological role in glioma cells: they are involved in cell growth and extensive migrating behavior. Due to the fact that these processes are accompanied by changes in membrane stress, here, we examine mechanosensitive properties of BK channels from human glioblastoma cells (gBK channels). Experiments were performed by the use of patch-clamp method on excised patches under membrane suction (0–40 mmHg) at membrane hyper- and depolarization. We have also checked whether channel’s activity is affected by possible changes of membrane morphology after a series of long impulses of suction. Unconventionally, we also analyzed internal structure of the experimental signal to make inferences about conformational dynamics of the channel in stressed membranes. We examined the fractal long-range memory effect (by R/S Hurst analysis), the rate of changes in information by sample entropy, or correlation dimension, and characterize its complexity over a range of scales by the use of Multiscale Entropy method. The obtained results indicate that gBK channels are mechanosensitive at membrane depolarization and hyperpolarization. Prolonged suction of membrane also influences open–closed fluctuations—it decreases channel’s activity at membrane hyperpolarization and, in contrary, increases channel’s activity at high voltages. Both membrane strain and its “fatigue” reduce dynamical complexity of channel gating, which suggest decrease in the number of available open conformations of channel protein in stressed membranes.
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spelling pubmed-62447682018-12-04 Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity Wawrzkiewicz-Jałowiecka, Agata Trybek, Paulina Machura, Łukasz Dworakowska, Beata Grzywna, Zbigniew J. J Membr Biol Article BK channels are potassium selective and exhibit large single-channel conductance. They play an important physiological role in glioma cells: they are involved in cell growth and extensive migrating behavior. Due to the fact that these processes are accompanied by changes in membrane stress, here, we examine mechanosensitive properties of BK channels from human glioblastoma cells (gBK channels). Experiments were performed by the use of patch-clamp method on excised patches under membrane suction (0–40 mmHg) at membrane hyper- and depolarization. We have also checked whether channel’s activity is affected by possible changes of membrane morphology after a series of long impulses of suction. Unconventionally, we also analyzed internal structure of the experimental signal to make inferences about conformational dynamics of the channel in stressed membranes. We examined the fractal long-range memory effect (by R/S Hurst analysis), the rate of changes in information by sample entropy, or correlation dimension, and characterize its complexity over a range of scales by the use of Multiscale Entropy method. The obtained results indicate that gBK channels are mechanosensitive at membrane depolarization and hyperpolarization. Prolonged suction of membrane also influences open–closed fluctuations—it decreases channel’s activity at membrane hyperpolarization and, in contrary, increases channel’s activity at high voltages. Both membrane strain and its “fatigue” reduce dynamical complexity of channel gating, which suggest decrease in the number of available open conformations of channel protein in stressed membranes. Springer US 2018-08-09 2018 /pmc/articles/PMC6244768/ /pubmed/30094475 http://dx.doi.org/10.1007/s00232-018-0044-9 Text en © The Author(s) 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Article
Wawrzkiewicz-Jałowiecka, Agata
Trybek, Paulina
Machura, Łukasz
Dworakowska, Beata
Grzywna, Zbigniew J.
Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity
title Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity
title_full Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity
title_fullStr Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity
title_full_unstemmed Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity
title_short Mechanosensitivity of the BK Channels in Human Glioblastoma Cells: Kinetics and Dynamical Complexity
title_sort mechanosensitivity of the bk channels in human glioblastoma cells: kinetics and dynamical complexity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6244768/
https://www.ncbi.nlm.nih.gov/pubmed/30094475
http://dx.doi.org/10.1007/s00232-018-0044-9
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