Cation-Selective Channel Regulated by Anions According to Their Hofmeister Ranking

2017 ◽  
Vol 129 (13) ◽  
pp. 3560-3563 ◽  
Author(s):  
Philip A. Gurnev ◽  
Torri C. Roark ◽  
Horia I. Petrache ◽  
Alexander J. Sodt ◽  
Sergey M. Bezrukov
Keyword(s):  
Selective Channel ◽  
Cation Selective Channel

scholarly journals Cation-Selective Channel Regulated by Anions According to Their Hofmeister Ranking

2017 ◽  
Vol 56 (13) ◽  
pp. 3506-3509 ◽  
Author(s):  
Philip A. Gurnev ◽  
Torri C. Roark ◽  
Horia I. Petrache ◽  
Alexander J. Sodt ◽  
Sergey M. Bezrukov
Keyword(s):  
Selective Channel ◽  
Cation Selective Channel

scholarly journals ZAC (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Paul Davies ◽  
Tim G. Hales ◽  
Anders A. Jensen ◽  
John A. Peters
Keyword(s):  
Constitutive Activity ◽  
Glycine Receptors ◽  
Selective Channel ◽  
High Concentrations ◽  
Cation Selective Channel

The zinc-activated channel (ZAC, nomenclature as agreed by the NC-IUPHAR Subcommittee for the Zinc Activated Channel) is a member of the Cys-loop family that includes the nicotinic ACh, 5-HT3, GABAA and strychnine-sensitive glycine receptors [1, 2, 3]. The channel is likely to exist as a homopentamer of 4TM subunits that form an intrinsic cation selective channel equipermeable to Na+, K+ and Cs+, but impermeable to Ca2+ and Mg2+ [3]. ZAC displays constitutive activity that can be blocked by tubocurarine and high concentrations of Ca2+ [3]. Although denoted ZAC, the channel is more potently activated by protons and copper, with greater and lesser efficacy than zinc, respectively [3]. ZAC is present in the human, chimpanzee, dog, cow and opossum genomes, but is functionally absent from mouse, or rat, genomes [1, 2].

Role of an apical cation-selective channel in function of tight epithelia

1989 ◽  
Vol 66 (1-2) ◽  
pp. 37-41
Author(s):  
Willy Driessche ◽  
David Erlij ◽  
Jeannine Simaels
Keyword(s):  
Tight Epithelia ◽  
Selective Channel ◽  
Cation Selective Channel

scholarly journals Converting the Depolarization-Activated Shaker KV Channel into a Hyperpolarization-Conducting Cation-Selective Channel by Two Pore Mutations

2018 ◽  
Vol 114 (3) ◽  
pp. 475a
Author(s):  
Evelyn Martinez-Morales ◽  
Laura C. Coonen ◽  
Dieter V. Van de Sande ◽  
Dirk J. Snyders ◽  
Alain J. Labro
Keyword(s):  
Kv Channel ◽  
Selective Channel ◽  
Cation Selective Channel

Regulation of the Retinal Bipolar Cell mGluR6 Pathway by Calcineurin

2002 ◽  
Vol 88 (3) ◽  
pp. 1088-1096 ◽  
Author(s):  
Josefin Snellman ◽  
Scott Nawy
Keyword(s):  
Bipolar Cells ◽  
Cation Channels ◽  
Tetraacetic Acid ◽  
Metabotropic Receptor ◽  
Postsynaptic Potential ◽  
Independent Form ◽  
Selective Channel ◽  
Whole Cell Recordings ◽  
Cation Selective Channel ◽  
Adaptive Role

Glutamate produces a hyperpolarizing postsynaptic potential inon bipolar cells by binding to the metabotropic receptor mGluR6 and subsequently closing a cation-selective channel. It has been proposed that Ca2+ influx through the cation channel triggers a depression of the synaptic potential. Here we report that this Ca2+-mediated depression requires activation of calcineurin, a Ca2+/calmodulin-regulated phosphatase. We measured glutamate-evoked currents ( I glu) with whole cell recordings ofon bipolar cells in light-adapted retinal slices. Depression of I glu by Ca2+ was prevented by inhibitors of calcineurin or by tightly buffering Ca2+ with bis-( o-aminophenoxy)- N,N,N′,N′-tetraacetic acid (BAPTA). However, when cells were dialyzed with BAPTA and a Ca2+-independent form of calcineurin (CaN420), depression of I glu was restored. Similarly, CaN420 induced depression of I glu during continuous glutamate application, a protocol that ordinarily prevents depression. Analysis of changes in the amplitude of the cation-selective current ( I cat) of cells that were dialyzed with high Ca2+ (1 μM), or with BAPTA and CaN420, indicates that Ca2+ depresses I glu by reducing I cat and that calcineurin acts via the same mechanism. Ca2+-mediated depression of I glu was not found to involve CaMKII, as inhibitors of CaMKII did not prevent this depression nor did they affect the sensitivity of the response to small changes in the concentration of mGluR6 agonist. Our data suggest that Ca2+ and calcineurin may play an adaptive role at the synapse between photoreceptor and on bipolar cells, closing postsynaptic cation channels that are opened by a drop in synaptic glutamate levels during prolonged photoreceptor illumination.

A calcium -activated cation-selective channel in rat cultured Schwann cells

1984 ◽  
Vol 222 (1228) ◽  
pp. 349-355 ◽  
Keyword(s):  
Schwann Cells ◽  
Single Channel ◽  
Outward Current ◽  
Channel Activity ◽  
Experimental Conditions ◽  
Cultured Schwann Cells ◽  
Selective Channel ◽  
Inside Out ◽  
Cation Selective Channel ◽  
Sodium And Potassium

Calcium -activated channels, in the plasm a membrane of rat cultured Schwann cells were studied in isolated ‘inside-out’ membrane patches. With identical (150 mM NaCl) solutions on either side of the membrane, a single channel conductance of 32 pS was calculated for inward current; the conductance was somewhat less for outward current. The channel is about equally permeable to sodium and potassium ions, bu t is not detectably permeable to either chloride or calcium. Under our experimental conditions the channel is activated by high (more than 10 -4 m) concentrations of calcium and is sensitive to voltage, channel activity increasing with membrane depolarization.

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