scholarly journals Development of the L-type CaV / BK Complex Simulator (II): estimation of the distance between the channels

2021 ◽  
Vol 2 (2) ◽  
pp. 1258-1265
Author(s):  
Marleni Reyes Monreal ◽  
Jessica Quintero Pérez ◽  
Miguel Pérez Escalera ◽  
Arturo Reyes Lazalde ◽  
María Eugenia Pérez Bonilla
Keyword(s):  
Cell Membrane ◽  
Mathematical Models ◽  
Visual Basic ◽  
Bk Channel ◽  
Excitable Cells ◽  
K Channels ◽  
Voltage Gated ◽  
Ca2 Channels ◽  
High Conductance

The presence, in the cell membrane, of high-conductance K+ channels and voltage-gated Ca2+ channels (CaV) forming complexes has been reported. These complexes have important functions in excitable cells. The [Ca2+]i at the mouth of the CaV channel decreases with distance and with the concentration of chelators. For the BK channel to be activated with internal Ca2, a concentration of the order of M is necessary and this implies a closeness between the BK-CaV channels. A simulator of the decay of Ca2+ in the presence of BAPTA to estimate the distance between the channels was developed. The mathematical models were implemented in Visual Basic® 6.0 and were solved numerically. The results indicate the coexistence of L-type CaV channel and BK grouped in nanodomains with a distance between channels of ~30 nm.

Enhancement of Voltage-Gated K+ Channels and Depression of Voltage-Gated Ca2+ Channels Are Involved in Quercetin-Induced Vasorelaxation in Rat Coronary Artery

Planta Medica ◽  
2014 ◽  
Vol 80 (06) ◽  
pp. 465-472 ◽  
Author(s):  
Xiaomin Hou ◽  
Yu Liu ◽  
Longgang Niu ◽  
Lijuan Cui ◽  
Mingsheng Zhang
Keyword(s):  
Coronary Artery ◽  
K Channels ◽  
Voltage Gated ◽  
Ca2 Channels

scholarly journals Activation of pre-synaptic M-type K+channels inhibits [3H]d-aspartate release by reducing Ca2+entry through P/Q-type voltage-gated Ca2+channels

2009 ◽  
Vol 109 (1) ◽  
pp. 168-181 ◽  
Author(s):  
Rosa Luisi ◽  
Elisabetta Panza ◽  
Vincenzo Barrese ◽  
Fabio Arturo Iannotti ◽  
Davide Viggiano ◽  
...  
Keyword(s):  
K Channels ◽  
Voltage Gated ◽  
Type K ◽  
Ca2 Channels

scholarly journals Role of pertussis toxin-sensitive G-protein, K+ channels, and voltage-gated Ca2+ channels in the antinociceptive effect of inosine

2012 ◽  
Vol 9 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Sérgio José Macedo-Junior ◽  
Francisney Pinto Nascimento ◽  
Murilo Luiz-Cerutti ◽  
Adair Roberto Soares Santos
Keyword(s):  
G Protein ◽  
Pertussis Toxin ◽  
Antinociceptive Effect ◽  
K Channels ◽  
Voltage Gated ◽  
Ca2 Channels

scholarly journals Coupling between Voltage Sensors and Activation Gate in Voltage-gated K+ Channels

2002 ◽  
Vol 120 (5) ◽  
pp. 663-676 ◽  
Author(s):  
Zhe Lu ◽  
Angela M. Klem ◽  
Yajamana Ramu
Keyword(s):  
Electrical Signal ◽  
K Channel ◽  
Coupling Mechanism ◽  
Excitable Cells ◽  
Voltage Sensing ◽  
K Channels ◽  
Voltage Sensors ◽  
Voltage Gated ◽  
Transmembrane Segments ◽  
Activation Gate

Current through voltage-gated K+ channels underlies the action potential encoding the electrical signal in excitable cells. The four subunits of a voltage-gated K+ channel each have six transmembrane segments (S1–S6), whereas some other K+ channels, such as eukaryotic inward rectifier K+ channels and the prokaryotic KcsA channel, have only two transmembrane segments (M1 and M2). A voltage-gated K+ channel is formed by an ion-pore module (S5–S6, equivalent to M1–M2) and the surrounding voltage-sensing modules. The S4 segments are the primary voltage sensors while the intracellular activation gate is located near the COOH-terminal end of S6, although the coupling mechanism between them remains unknown. In the present study, we found that two short, complementary sequences in voltage-gated K+ channels are essential for coupling the voltage sensors to the intracellular activation gate. One sequence is the so called S4–S5 linker distal to the voltage-sensing S4, while the other is around the COOH-terminal end of S6, a region containing the actual gate-forming residues.

scholarly journals Up-Regulation of Voltage Gated K+ Channels Kv1.3 and Kv1.5 by Protein Kinase PKB/Akt

2015 ◽  
Vol 37 (6) ◽  
pp. 2454-2463 ◽  
Author(s):  
Jamshed Warsi ◽  
Myriam Fezai ◽  
Mireia Fores ◽  
Bernat Elvira ◽  
Florian Lang
Keyword(s):  
Cell Proliferation ◽  
Protein Kinase ◽  
Cell Membrane ◽  
Brefeldin A ◽  
Xenopus Laevis Oocytes ◽  
K Channels ◽  
Voltage Gated ◽  
Electrode Voltage ◽  
And Function ◽  
K Currents

Background: The voltage gated K+ channels Kv1.3 and Kv1.5 contribute to the orchestration of cell proliferation. Kinases participating in the regulation of cell proliferation include protein kinase B (PKB/Akt). The present study thus explored whether PKB/Akt modifies the abundance and function of Kv1.3 and Kv1.5. Methods: Kv1.3 or Kv1.5 was expressed in Xenopus laevis oocytes with or without wild-type PKB/Akt, constitutively active T308D/S473DPKB/Akt or inactive T308A/S473APKB/Akt. The channel activity was quantified utilizing dual electrode voltage clamp. Moreover, HA-tagged Kv1.5 protein was determined utilizing chemiluminescence. Results: Voltage gated K+ currents were observed in Kv1.3 or Kv1.5 expressing oocytes but not in water-injected oocytes or in oocytes expressing PKB/Akt alone. Co-expression of PKB/Akt or T308D/S473DPKB/Akt, but not co-expression of T308A/S473APKB/Akt significantly increased the voltage gated current in both Kv1.3 and Kv1.5 expressing oocytes. As shown for Kv1.5, co-expression of PKB/Akt enhanced the channel protein abundance in the cell membrane. In Kv1.5 expressing oocytes voltage gated current decreased following inhibition of carrier insertion by brefeldin A (5 µM) to similarly low values in the absence and presence of PKB/Akt, suggesting that PKB/Akt stimulated carrier insertion into rather than inhibiting carrier retrieval from the cell membrane. Conclusion: PKB/Akt up-regulates both, Kv1.3 and Kv1.5 K+ channels.

scholarly journals Evidence for a role for BK channels in the regulation of ADAM17 activity

2019 ◽  
Author(s):  
Minae Yoshida ◽  
Dean Willis
Keyword(s):  
Cell Membrane ◽  
Cell Biology ◽  
Cancer Biology ◽  
Bk Channels ◽  
Bk Channel ◽  
Potassium Ions ◽  
Excitable Cells ◽  
Tnf Α ◽  
A Disintegrin And Metalloproteinase ◽  
Physical And Chemical

AbstractLarge-conductance voltage and calcium activated channels, KCa1.1, have a large single conductance (~p250) and are highly selective for potassium ions. As a result they have been termed big potassium channels (BK channels). Because of the channel’s ability to integrate multiple physical and chemical signals they have received much attention in excitable cells. In comparison they have received relatively little attention in non-excitable cells in those of the immune system. Here we report evidence that the BK channel regulates ADAM17 activity. Upon macrophage activation, BK channels translocate to the cell membrane. Genetic or pharmacological inhibition of the cell membrane BK channels resulted in elevated TNF-α release and increased metalloproteinase a disintegrin and metalloproteinase domain 17 (ADAM17) activity. Inhibitors of BK channels also increased IL-6Rα release, a second ADAM17 substrate. In comparison, a BK channel opener decreases TNF-α release. Taken together, our results demonstrate a novel mechanism by which ion channel regulates ADAM17 activity. Given the broad range of ADAM17 substrates, this finding has implications in many fields of cell biology including immunology, neurology and cancer biology.

scholarly journals Voltage-gated calcium channels (CaV) in GtoPdb v.2021.3

2021 ◽  
Vol 2021 (3) ◽  
Author(s):  
William A. Catterall ◽  
Edward Perez-Reyes ◽  
Terrance P. Snutch ◽  
Jörg Striessnig
Keyword(s):  
High Voltage ◽  
Low Voltage ◽  
Excitable Cells ◽  
Voltage Gated ◽  
Voltage Dependent ◽  
Alternatively Spliced ◽  
Membrane Spanning ◽  
Voltage Gated Ion Channels ◽  
Ca2 Channels ◽  
Α1 Subunit

Ca2+ channels are voltage-gated ion channels present in the membrane of most excitable cells. The nomenclature for Ca2+channels was proposed by [127] and approved by the NC-IUPHAR Subcommittee on Ca2+ channels [70]. Most Ca2+ channels form hetero-oligomeric complexes. The α1 subunit is pore-forming and provides the binding site(s) for practically all agonists and antagonists. The 10 cloned α1-subunits can be grouped into three families: (1) the high-voltage activated dihydropyridine-sensitive (L-type, CaV1.x) channels; (2) the high- to moderate-voltage activated dihydropyridine-insensitive (CaV2.x) channels and (3) the low-voltage-activated (T-type, CaV3.x) channels. Each α1 subunit has four homologous repeats (I-IV), each repeat having six transmembrane domains (S1-S6) and a pore-forming region between S5 and S6. Voltage-dependent gating is driven by the membrane spanning S4 segment, which contains highly conserved positive charges that respond to changes in membrane potential. All of the α1-subunit genes give rise to alternatively spliced products. At least for high-voltage activated channels, it is likely that native channels comprise co-assemblies of α1, β and α2-δ subunits. The γ subunits have not been proven to associate with channels other than the α1s skeletal muscle Cav1.1 channel. The α2-δ1 and α2-δ2 subunits bind gabapentin and pregabalin.

scholarly journals Voltage-gated calcium channels (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
William A. Catterall ◽  
Edward Perez-Reyes ◽  
Terrance P. Snutch ◽  
Jörg Striessnig
Keyword(s):  
High Voltage ◽  
Low Voltage ◽  
Transmembrane Domains ◽  
Excitable Cells ◽  
Voltage Gated ◽  
Alternatively Spliced ◽  
Membrane Spanning ◽  
Voltage Gated Ion Channels ◽  
Ca2 Channels ◽  
Α1 Subunit

Calcium (Ca2+) channels are voltage-gated ion channels present in the membrane of most excitable cells. The nomenclature for Ca2+channels was proposed by [110] and approved by the NC-IUPHAR Subcommittee on Ca2+ channels [60]. Ca2+ channels form hetero-oligomeric complexes. The α1 subunit is pore-forming and provides the binding site(s) for practically all agonists and antagonists. The 10 cloned α1-subunits can be grouped into three families: (1) the high-voltage activated dihydropyridine-sensitive (L-type, CaV1.x) channels; (2) the high-voltage activated dihydropyridine-insensitive (CaV2.x) channels and (3) the low-voltage-activated (T-type, CaV3.x) channels. Each α1 subunit has four homologous repeats (I–IV), each repeat having six transmembrane domains and a pore-forming region between transmembrane domains S5 and S6. Gating is thought to be associated with the membrane-spanning S4 segment, which contains highly conserved positive charges. Many of the α1-subunit genes give rise to alternatively spliced products. At least for high-voltage activated channels, it is likely that native channels comprise co-assemblies of α1, β and α2–δ subunits. The γ subunits have not been proven to associate with channels other than the α1s skeletal muscle Cav1.1 channel. The α2–δ1 and α2–δ2 subunits bind gabapentin and pregabalin.

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