Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Ion Channel Gating”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 433 records · Page 24Linked to original sources
PubMed2002

Human neural stem cells: electrophysiological properties of voltage-gated ion channels.

We have characterized the profile of membrane currents in an immortalized human neural stem cell line, HB1.F3 cells, using whole-cell patch clamp technique. Human neural stem cell line generated from primary cell cultures of embryonic human telencephalon using a replication-incompetent retroviral vector containing v-myc expresses nestin, a cell type-specific marker for neural stem cells. The human neural stem cells expressed both outward and inward K(+) currents with no evidence for Na(+) currents. The density of the outward, delayed rectifying type K(+) current was 1.8 +/- 0.015 nA/pF, and that of the inwardly rectifying K(+) current was 0.37 +/- 0.012 nA/pF (at 30 mM of [K(+)](o)). In order to induce neuronal differentiation of the neural stem cells, a full-length coding region of NeuroD, a neurogenic transcription factor, was transfected into HB1.F3 cells. Introduction of NeuroD induced expression of Na(+) currents with the current density of 0.042 +/- 0.011 nA/pF. The presence of two types of K(+) currents and expression of Na(+) currents induced by NeuroD appear to reflect the characteristic physiological features of human neural stem cells.

Basic Helix-Loop-Helix Proteins↗
PubMed1996

Properties of voltage-gated ion channels formed by syringomycin E in planar lipid bilayers.

Using the planar lipid bilayer technique we demonstrate that the lipodepsipeptide antibiotic, syringomycin E, forms voltage-sensitive ion channels of weak anion selectivity. The formation of channels in bilayers made from dioleoylglycerophosphatidylserine doped with syringomycin E at one side (1-40 micrograms/ml) was greatly affected by cis-positive voltage. A change of voltage from a positive to a negative value resulted in (i) an abrupt increase in the single channel conductance (the rate of increase was voltage dependent) simultaneous with (ii) a closing of these channels and an exponential decrease in macroscopic conductance over time. The strong voltage dependence of multichannel steady state conductance, the single channel conductance, the rate of opening of channels at positive voltages and closing them at negative voltages, as well as the observed abrupt increase of single channel conductance after voltage sign reversal suggest that the change of the transmembrane field induces a significant rearrangement of syringomycin E channels, including a change in the spacing of charged groups that function as voltage sensors. The conductance induced by syringomycin E increased with the sixth power of syringomycin E concentration suggesting that at least six monomers are required for channel formation.

Anions↗
PubMed1995

The effects of nitrous oxide on a glutamate-gated ion channel and their reversal by high pressure; a single channel analysis.

Nitrous oxide reversibly affects the kinetics, but not the conductance, of the qGluR channel of locust muscle. 0.5 atm N2O at 20.5 degrees C was without effect but both 1.5 and 2.7 atm significantly reduced the probability of the channel opening, the frequency of opening and the mean open time, and prolonged the mean closed time. 100 atm helium was without effect on these parameters, but when 98.5 atm He was combined with 1.5 atm N2O they, and the associated dwell time distributions, were restored to normal. 100 atm similarly combined with 2.7 atm N2O exerted a comparable trend which fell short of significance. The results are consistent with nitrous oxide binding to the channel with a significant molar volume increase, which pressure opposes. This suggests that nitrous oxide may cause conformational changes in the channel, and that the pressure reversal of nitrous oxide anaesthesia in animals could be caused by molecular antagonism.

Animals↗
PubMed1989

The selectivity filter of a ligand-gated ion channel. The helix-M2 model of the ion channel of the nicotinic acetylcholine receptor.

Evidence from electrophysiology and biochemistry supports the hypothesis that the ion channel of the nicotinic acetylcholine receptor is formed by homologous amino acid sequences of all receptor subunits, called helices M2. A model of the ion channel is proposed and the selectivity filter is described as a ring of negatively-charged amino acid side chains [(1988) Nature 335, 645-648] which may undergo conformational changes upon permeation of the cation.

Amino Acid Sequence↗
PubMed2001

Agonist-stimulated internalisation of the ligand-gated ion channel P2X(1) in rat vas deferens.

Using cell surface biotinylation and Western blotting, we investigated the extent to which native P2X(1) receptors in rat vas deferens are internalised after exposure to agonist. Exposure to 100 microM alpha,beta-meATP 30 min prior and during a 10 min biotinylation period resulted in a approximately 50% reduction in the amount of biotinylated P2X(1) receptor indicating that activation of the receptor by agonist induces receptor internalisation. Furthermore, biotinylation under saturating conditions suggests that once internalised, a rapid recycling of P2X(1) receptor back to the cell surface occurs. The physiological implications of these mechanisms in terms of receptor function are discussed.

Adenosine Triphosphate↗
PubMed2006

Non-conducting functions of voltage-gated ion channels.

Various studies, mostly in the past 5 years, have demonstrated that, in addition to their well-described function in regulating electrical excitability, voltage-dependent ion channels participate in intracellular signalling pathways. Channels can directly activate enzymes linked to cellular signalling pathways, serve as cell adhesion molecules or components of the cytoskeleton, and their activity can alter the expression of specific genes. Here, I review these findings and discuss the extent to which the molecular mechanisms of such signalling are understood.

Animals↗
PubMed2006

P2RX7, a gene coding for a purinergic ligand-gated ion channel, is associated with major depressive disorder.

The P2RX7 gene is located within a region on chromosome 12q24.31 that has been identified as a susceptibility locus for affective disorders by linkage and association studies. P2RX7 is a purinergic ATP-binding calcium channel expressed in neurons as well as in microglial cells in various brain regions. We investigated 29 single nucleotide polymorphisms (SNPs) within the P2RX7 gene and adjacent genes in a sample of 1000 German Caucasian patients suffering from recurrent major depressive disorder (MDD). These were contrasted with diagnosed healthy Caucasian controls from the same population (n=1029). A non-synonymous coding SNP in the P2RX7 gene (rs2230912), previously found to be associated with bipolar disorder, was significantly associated (P=0.0019) with MDD. This polymorphism results in an amino acid exchange in the C-terminal cytosolic domain of the P2RX7 channel protein, suggesting that the observed P2RX7 polymorphism might play a causal role in the development of depression.

Adult↗
PubMed1996

Model of a thalamocortical neurone with dendritic voltage-gated ion channels.

To investigate the functional role of dendrites of thalamocortical neurones, we have used our one-compartmental model to construct a multi-compartmental model with dendritic regions chosen according to a representative soma-to-dendritic terminal path of an X cell of the cat dorsal lateral geniculate nucleus. The multi-compartmental model with dendritic low-threshold Ca2+ and delayed rectifier K+ channels yields more accurate results than the one-compartmental model when simulating tonic firing and oscillatory activities, and provides a useful means for the study of propagation of excitation on the dendrites.

Animals↗
PubMed1994

Emerging neurochemical concepts in the actions of ethanol at ligand-gated ion channels.

Both data and opinion are beginning to unify a consensus concerning the neurochemical mediation of the effects of ethanol in the CNS. This review of the literature is offered as an introduction to the molecular and cellular aspects of the neurochemical effects of ethanol for behavioral pharmacologists. As such, this review emphasizes the receptor pharmacology of ethanol over its behavioral effects. The unifying principle throughout the review is that ethanol has selective effects at particular ionotropic receptors, including GABA(A), NMDA and 5-HT(3) receptors. Current concepts of how ethanol may selectively interact with these receptor systems are discussed. In particular, the molecular characterizations of these receptors are reviewed to provide a foundation for understanding the differential interaction of ethanol with particular receptor subtypes and integrating data addressing the behavioral actions of ethanol. Extension of the neurochemical effects to behavioral outcomes is explored primarily via drug discrimination procedures. The recent advances that are highlighted include the receptor basis for regional sensitivity to ethanol and potential interactions of ethanol-induced neurochemical activity associated with alcohol intoxication. The integration and understanding of how multiple receptor systems interact to influence a behavioral outcome will remain an important challenge for behavioral pharmacologists interested in the effects of ethanol.

Journal Article↗
PubMed2004

The alpha7 nicotinic acetylcholine receptor subunit exists in two isoforms that contribute to functional ligand-gated ion channels.

Fast synaptic transmission in mammalian autonomic ganglia is mediated primarily by nicotinic receptors, and one of the most abundant nicotinic acetylcholine receptor subtypes in these neurons contains the alpha7 subunit (alpha7-nAChRs). Unlike alpha7-nAChRs expressed in other cells, the predominant alpha7-nAChR subtype found in rat intracardiac and superior cervical ganglion neurons exhibits a slow rate of desensitization and is reversibly blocked by alpha-bungarotoxin (alphaBgt). We report here the identification of an alpha7 subunit sequence variant in rat autonomic neurons that incorporates a novel 87-base pair cassette exon in the N terminus of the receptor and preserves the reading frame of the transcript. This alpha7 isoform was detected using reverse transcriptase-polymerase chain reaction techniques in neonatal rat brain and intracardiac and superior cervical ganglion neurons. Immunoblot experiments using a polyclonal antibody directed against the deduced amino acid sequence of the alpha7-2 insert showed a pattern of expression consistent with alpha7-2 subunit mRNA distribution. Moreover, the alpha7-2 subunit could be immunodepleted from protein extracts by solid-phase immunoprecipitation techniques using the anti-alpha7 monoclonal antibody 319. The alpha7-2 subunit was shown to form functional homomeric ion channels that were activated by acetylcholine and blocked by alpha-bungarotoxin when expressed in Xenopus laevis oocytes. This alpha7 isoform exhibited a slow rate of desensitization, and inhibition of these channels by alphaBgt reversed rapidly after washout. Taken together, these data indicate that the alpha7-2 subunit is capable of forming functional alphaBgt-sensitive acetylcholine receptors that resemble the alpha7-nAChRs previously identified in rat autonomic neurons. Furthermore, the distribution of the alpha7-2 isoform is not limited to peripheral neurons.

Acetylcholine↗