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Query: UMLS:C0019829 (Hodgkin's disease)
 30,247 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In silico simulation based on Markov chains is a powerful way to describe and predict the activity of many transport proteins including ion channels. However, modeling and simulation using realistic models of voltage- or ligand-gated ion channels exposed to a wide range of experimental conditions require building complex kinetic schemes and solving complicated differential equations. To circumvent these problems, we developed IonChannelLab a software tool that includes a user-friendly Graphical User Interface and a simulation library. This program supports channels with Ohmic or Goldman-Hodgkin-Katz behavior and can simulate the time-course of ionic and gating currents, single channel behavior and steady-state conditions. The program allows the simulation of experiments where voltage, ligand and ionic concentration are varied independently or simultaneously.
Channels (Austin)
PMID:Simulating complex ion channel kinetics with IonChannelLab. 2093 53

Many of us were taught in high school biology that the action potential waveform in nerves and other excitable tissues was generated by an initial rapid influx of external Na(+) ions across the plasma membrane, followed by an outward movement of intracellular K(+) ions. The former event, mediated by voltage-gated Na(+) channels, is responsible for the fast depolarizing upstroke of the action potential, while voltage-gated K+ channels are responsible for the subsequent repolarizing phase, which largely controls action potential duration. Although Hodgkin and Huxley described the fundamental importance of this sequential activation process more than 60 y ago, the molecular and structural details underlying the faster activation of voltage-gated Na(+) (Nav) vs. K(+) (Kv) channels have yet to be fully resolved.
Channels (Austin)
PMID:Built for speed: molecular properties of the voltage sensor domain underlie the rapid activation of voltage-gated Na(+) channels compared with Shaker-type K(+) channels. 2397 94

It is generally expected that 2-pore domain K(+) (K2P) channels are open or outward rectifiers in asymmetric physiological K(+) gradients, following the Goldman-Hodgkin-Katz (GHK) current equation. Although cloned K2P channels have been extensively studied, their current-voltage (I-V) relationships are not precisely characterized and previous definitions are contradictory. Here we study all the functional channels from 6 mammalian K2P subfamilies in transfected Chinese hamster ovary cells with patch-clamp technique, and examine whether their I-V relationships are described by the GHK current equation. K2P channels display 2 distinct types of I-V curves in asymmetric physiological K(+) gradients. Two K2P isoforms in the TWIK subfamily conduct large inward K(+) currents and have a nearly linear I-V curve. Ten isoforms from 5 other K2P subfamilies conduct small inward K(+) currents and exhibit open rectification, but fits with the GHK current equation cannot precisely reveal the differences in rectification among K2P channels. The Rectification Index, a ratio of limiting I-V slopes for outward and inward currents, is used to quantitatively describe open rectification of each K2P isoform, which is previously qualitatively defined as strong or weak open rectification. These results systematically and precisely classify K2P channels and suggest that TWIK K(+) channels have a unique feature in regulating cellular function.
Channels (Austin) 2014
PMID:Classification of 2-pore domain potassium channels based on rectification under quasi-physiological ionic conditions. 2561 86

Voltage-gated ion channels (VGIC) are transmembrane proteins responsible for the generation of electrical signals in excitable cells. VGIC were first described in 1952 by Hodgkin and Huxley, (1) and have since been associated with various physiological functions such as propagating nerve impulses, locomotion, and cardiac excitability. VGIC include channels specialized in the selective passage of K(+), Ca(2+) Na(+), or H(+). They are composed of 2 main structures: the pore domain (PD) and the voltage sensor domain (VSD). The PD ensures the physiological flow of ions and is typically composed of 8 transmembrane segments (TM). The VSD detects voltage variations and is composed of 4 TM (S1-S4). Given their crucial physiological role, VGIC dysfunctions are associated with diverse pathologies known as ion channelopathies. These dysfunctions usually affect the membrane expression of ion channels or voltage-dependent conformational changes of the pore. However, an increasing number of ion channelopathies, including periodic paralysis, dilated cardiomyopathy (DCM) associated with cardiac arrhythmias, and peripheral nerve hyperexcitability (PNH), have been linked to the appearance of a new pathological mechanism involving the creation of an alternative permeation pathway through the normally non-conductive VSD of VGIC. This permeation pathway is called the gating pore or omega pore.
Channels (Austin) 2015
PMID:Gating pore currents, a new pathological mechanism underlying cardiac arrhythmias associated with dilated cardiomyopathy. 2604 92