Calcium and Potassium Channels in Experimental Subarachnoid Hemorrhage and Transient Global Ischemia

Healthy cerebrovascular myocytes express members of several different ion channel families which regulate resting membrane potential, vascular diameter, and vascular tone and are involved in cerebral autoregulation. In animal models, in response to subarachnoid blood, a dynamic transition of ion channel expression and function is initiated, with acute and long-term effects differing from each other. Initial hypoperfusion after exposure of cerebral vessels to oxyhemoglobin correlates with a suppression of voltage-gated potassium channel activity, whereas delayed cerebral vasospasm involves changes in other potassium channel and voltage-gated calcium channels expression and function. Furthermore, expression patterns and function of ion channels appear to differ between main and small peripheral vessels, which may be key in understanding mechanisms behind subarachnoid hemorrhage-induced vasospasm. Here, changes in calcium and potassium channel expression and function in animal models of subarachnoid hemorrhage and transient global ischemia are systematically reviewed and their clinical significance discussed.

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Changes in ion channel expression and function associated with cardiac arrhythmogenic remodeling by Sorbs2

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease ◽

10.1016/j.bbadis.2021.166247 ◽

2021 ◽

Vol 1867 (12) ◽

pp. 166247

Author(s):

Ling-Ling Qian ◽

Xiaojing Sun ◽

Jingchun Yang ◽

Xiao-Li Wang ◽

Michael J. Ackerman ◽

...

Keyword(s):

Ion Channel ◽

Channel Expression ◽

And Function

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Ion Channel Expression and Function of iPSC-derived Cardiomyocytes

Cardiac Regeneration using Stem Cells ◽

10.1201/b14990-10 ◽

2013 ◽

pp. 153-172

Author(s):

Tetsushi Furukawa

Keyword(s):

Ion Channel ◽

Channel Expression ◽

And Function

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Endothelial Cell Ion Channel Expression and Function in Arterioles and Resistance Arteries

Vascular Ion Channels in Physiology and Disease ◽

10.1007/978-3-319-29635-7_1 ◽

2016 ◽

pp. 3-36 ◽

Cited By ~ 3

Author(s):

William F. Jackson

Keyword(s):

Endothelial Cell ◽

Ion Channel ◽

Resistance Arteries ◽

Channel Expression ◽

And Function

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Abstract 17384: Cardiac-Specific Overexpression of Human Mutant Desmoplakin in Mice Disrupts Cardiac Voltage-Gated Sodium Channel Expression

Circulation ◽

10.1161/circ.138.suppl_1.17384 ◽

2018 ◽

Vol 138 (Suppl_1) ◽

Author(s):

Subat Turdi ◽

Jeffrey A Towbin

Keyword(s):

Sodium Channel ◽

Fatty Infiltration ◽

Electrical Coupling ◽

Cx43 Expression ◽

Voltage Gated Sodium Channel ◽

Voltage Gated ◽

Intercalated Discs ◽

Channel Expression ◽

Life Threatening ◽

And Function

Introduction: Arrhythmogenic cardiomyopathy (AC) is characterized by bi-ventricular dilation, fibro-fatty infiltration and life-threatening arrhythmias. Disruptions in cardiac voltage-gated sodium channel (Nav1.5) expression and function are known to cause arrhythmias. We have demonstrated that cardiac-specific overexpression of human mutant desmoplakin (DSP, Tg-R2834H) in mice leads to AC. However, whether mutant DSP expression in the heart affects the Nav1.5 distribution and function are unknown Hypothesis: Here, we tested whether Nav1.5 localization and expression are altered in the R2834H-Tg mouse hearts. Methods: Primary cardiomyocytes and frozen myocardial sections from non-transgenic (NTg), wild-type DSP (Tg-DSP) and Tg-R2834H mice were used for immunofluorescence studies to assess subcellular localization of DSP, desmin, Nav1.5, Cx43, plakoglobin and β-catenin. Western blot and qPCR were used for quantitative analysis. Results: Double staining of cardiomyocytes from NTg mice with DSP and Nav1.5 revealed that Nav1.5 was colocalized with DSP at the intercalated discs (IDs). In contrast, Tg-R2834H cardiomyocytes exhibited marked increase of mutant DSP expression at the IDs concomitant with a reduction in Nav1.5 immunoreactive signals. Tg-R2834H cardiomyocytes also revealed an aberration of DSP and desmin colocalizations at the IDs. There were not obvious differences in Cx43 expression between the genotypes, although the redistribution of Cx43 from the IDs to the sarcolemma was evident in Tg-R2834H cardiomyocytes. qPCR results correlated with reduced Nav1.5 mRNA expression in the Tg-R2834H mouse hearts. Conclusions: Defective DSP protein expression in the heart disrupts Nav1.5 localization and expression, implying an interaction between DSP and Nav1.5 to orchestrate normal mechanical and electrical coupling. Further electrophysiology studies to assess whole-cell Na + currents in these cardiomyocytes will provide insight into DSP and Nav1.5 interaction.

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Butamben derivatives enhance BMP-2-stimulated commitment of C2C12 cells into osteoblasts with induction of voltage-gated potassium channel expression

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2011.10.020 ◽

2011 ◽

Vol 21 (24) ◽

pp. 7363-7366 ◽

Cited By ~ 2

Author(s):

Hye Joo Kim ◽

Mikyung Park ◽

Young-Min Han ◽

Byoung-Mog Kwon ◽

Seong Hwan Kim

Keyword(s):

Potassium Channel ◽

C2c12 Cells ◽

Voltage Gated ◽

Channel Expression

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Insights into the structure and function of HV1 from a meta-analysis of mutation studies

The Journal of General Physiology ◽

10.1085/jgp.201611619 ◽

2016 ◽

Vol 148 (2) ◽

pp. 97-118 ◽

Cited By ~ 16

Author(s):

Thomas E. DeCoursey ◽

Deri Morgan ◽

Boris Musset ◽

Vladimir V. Cherny

Keyword(s):

Amino Acid ◽

Ion Channel ◽

Meta Analysis ◽

Structure And Function ◽

Proton Channel ◽

Vast Array ◽

Voltage Gated ◽

Interspecies Differences ◽

And Function ◽

Sheer Number

The voltage-gated proton channel (HV1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for HV1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by the sheer number of mutations and interspecies differences in amino acid numbering. This review organizes all existing information in a logical manner to allow swift identification of studies that have characterized any particular mutation. Although much can be gained from this meta-analysis, important questions about the inner workings of HV1 await future revelation.

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