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Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events [Figure 2 mRNA data]

ABSTRACT: Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events [Figure 2 mRNA data]

PROVIDER: PRJNA611596 | ENA |

REPOSITORIES: ENA

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Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events [Figure 8 mRNA data]

Project description:Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events [Figure 8 mRNA data]

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Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events

Project description:Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events

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Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events [Figure 2 mRNA data]

Project description:Analysis of rhythmonome gene expression in cardiac myocytes derived from human induced pluripotent stem cells Cardiac electrical activity is controlled by the carefully orchestrated activity of more than a dozen different ion conductances. Yet, there is considerable variability in cardiac ion channel expression levels both within and between subjects. In this study we tested the hypothesis that variations in ion channel expression between individuals are not random but rather there are modules of co-expressed genes and that these modules make electrical signaling in the heart more robust. Meta-analysis of 3653 public RNA-Seq datasets identified a strong correlation between expression of CACNA1C (L-type calcium current, ICaL) and KCNH2 (rapid delayed rectifier K+ current, IKr), which was verified in mRNA extracted from human induced pluripotent stem cell-derived cardiomyocytes (hiPSC-CM). In silico modeling, validated with functional measurements in hiPSC-CM, indicates that the co-expression of CACNA1C and KCNH2 limits the variability in action potential duration and reduces susceptibility to early afterdepolarizations, a surrogate marker for pro-arrhythmia.

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Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events [Figure 8 mRNA data]

2020-03-10 | GSE146665 | GEO

Co-expression of calcium channels and delayed rectifier potassium channels protects the heart from proarrhythmic events

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-03-10 | GSE146667 | GEO

KCNQ POTASSIUM CHANNELS MODULATE WNT ACTIVITY IN GASTRO-OESOPHAGEAL ADENOCARCINOMAS

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Confirmation of recombinant Calcium-activated potassium channel from Leishmania donovani

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Identification of proteins associated with Kv1.2 potassium channels.

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Mechanism of pharmacochaperoning in ATP-sensitive potassium channels revealed by cryo-EM

Project description:ATP-sensitive potassium (K-ATP) channels composed of a pore-forming Kir6.2 potassium channel and a regulatory ABC transporter sulfonylurea receptor 1 (SUR1) regulate insulin secretion in pancreatic beta-cells to maintain glucose homeostasis. Mutations that impair channel folding or assembly prevent cell surface expression and cause congenital hyperinsulinism. Structurally diverse K-ATP inhibitors have been shown to act as pharmacochaperones to correct mutant channel expression, but the mechanism is unknown. Here, we compare cryoEM structures of K-ATP channels bound to pharmacochaperones glibenclamide, repaglinide, and carbamazepine. DSP cross-linking mass spectrometry was used to partially confirm cryoEM structures.

2019-11-12 | PXD013873 | Pride

Mechanism of pharmacochaperoning in ATP-sensitive potassium channels revealed by cryo-EM

Project description:ATP-sensitive potassium (K-ATP) channels composed of a pore-forming Kir6.2 potassium channel and a regulatory ABC transporter sulfonylurea receptor 1 (SUR1) regulate insulin secretion in pancreatic beta-cells to maintain glucose homeostasis. Mutations that impair channel folding or assembly prevent cell surface expression and cause congenital hyperinsulinism. Structurally diverse K-ATP inhibitors have been shown to act as pharmacochaperones to correct mutant channel expression, but the mechanism is unknown. Here, we compare cryoEM structures of K-ATP channels bound to pharmacochaperones glibenclamide, repaglinide, and carbamazepine. CyanurBiotinDimercaptoPropionylSuccinimide (CBDPS) cross-linking mass spectrometry was used to partially confirm cryoEM structures.

2019-08-12 | PXD014498 | Pride

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