scholarly journals The Arabidopsis R-SNARE VAMP721 Interacts with KAT1 and KC1 K+ Channels to Moderate K+ Current at the Plasma Membrane

2015 ◽  
Vol 27 (6) ◽  
pp. 1697-1717 ◽  
Author(s):  
Ben Zhang ◽  
Rucha Karnik ◽  
Yizhou Wang ◽  
Niklas Wallmeroth ◽  
Michael R. Blatt ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
K Channels ◽  
K Current

Voltage-Dependence of Extracellular Ca2+-Induced Modification in Properties of the Inward Rectifying K+ Channels in the Plasma Membrane of Mesophyll Protoplasts of Avena sativa

1996 ◽  
Vol 23 (3) ◽  
pp. 349 ◽  
Author(s):  
J Kourie
Keyword(s):  
Plasma Membrane ◽  
Time Constant ◽  
Avena Sativa ◽  
Voltage Dependence ◽  
Membrane Current ◽  
Time Dependent ◽  
Mesophyll Cells ◽  
K Channels ◽  
Current Passing ◽  
K Current

Data obtained using the whole-celi configuration of the patch-clamp technique reveal that characteristics of the inward rectifying K+ current across the plasma membrane of protoplasts isolated from mesophyll cells of leaves of oat (Avena sativa) are modified by increasing concentrations or removing the extracellular Ca2+. The whole-cell membrane current reveals two components. The first component an initial current II* which is the sum of two currents: (a) a linear ohmic leak current passing through non-gated channels, liNGC, and (b) a rectifying inward K+ current passing through inward rectifying gated K+ channels, IKi, that are instantaneously open. The second component of the membrane current at the steady state Iss is a time-dependent K+ current IKss defined as Iss-IiNGC and passes through inward rectifying gated K+ channels. The tail K+ current, IKT, is also defined as IT-IiNGC. Raising external calcium concentration, [Ca2+]o, from 0.1 mM to 10 mM blocked the inward rectifying currents IKi, IKss and IKT. The voltage-dependence of the activation time constant (τa) for time-dependent KC current IKss was not altered significantly by increasing [Ca2+]o whereas the deactivation time constant (τd) of the IKT increased from 16 ms to 30 ms at a Vm of -100 mV. Removal of [Ca2+]o increased the amplitude and altered the characteristics of the inward rectifying K+ current. Ten minutes after the removal of [Ca2+]o the increase in IKi was 3.5-fold larger than the increase in IKss. Furthermore, removing [Ca2+]o hastened the activation of IKss and the deactivation of IKT. However, the deactivation time constant (Td) remained dependent on membrane voltage (Vm). Extracellular Ca2+ may modulate the function of mesophyll cells by regulating K+ transport through the inward rectifying K+ channels and this may have significant implications for photosynthesis and cell expansion.

scholarly journals Potassium channel types in arterial chemoreceptor cells and their selective modulation by oxygen.

1992 ◽  
Vol 100 (3) ◽  
pp. 401-426 ◽  
Author(s):  
M D Ganfornina ◽  
J López-Barneo
Keyword(s):  
Time Course ◽  
Single Channel ◽  
K Channel ◽  
Open Probability ◽  
K Channels ◽  
Glomus Cells ◽  
Control Value ◽  
Voltage Dependent ◽  
K Current ◽  
Chemoreceptor Cells

Single K+ channel currents were recorded in excised membrane patches from dispersed chemoreceptor cells of the rabbit carotid body under conditions that abolish current flow through Na+ and Ca2+ channels. We have found three classes of voltage-gated K+ channels that differ in their single-channel conductance (gamma), dependence on internal Ca2+ (Ca2+i), and sensitivity to changes in O2 tension (PO2). Ca(2+)-activated K+ channels (KCa channels) with gamma approximately 210 pS in symmetrical K+ solutions were observed when [Ca2+]i was greater than 0.1 microM. Small conductance channels with gamma = 16 pS were not affected by [Ca2+]i and they exhibited slow activation and inactivation time courses. In these two channel types open probability (P(open)) was unaffected when exposed to normoxic (PO2 = 140 mmHg) or hypoxic (PO2 approximately 5-10 mmHg) external solutions. A third channel type (referred to as KO2 channel), having an intermediate gamma(approximately 40 pS), was the most frequently recorded. KO2 channels are steeply voltage dependent and not affected by [Ca2+]i, they inactivate almost completely in less than 500 ms, and their P(open) reversibly decreases upon exposure to low PO2. The effect of low PO2 is voltage dependent, being more pronounced at moderately depolarized voltages. At 0 mV, for example, P(open) diminishes to approximately 40% of the control value. The time course of ensemble current averages of KO2 channels is remarkably similar to that of the O2-sensitive K+ current. In addition, ensemble average and macroscopic K+ currents are affected similarly by low PO2. These observations strongly suggest that KO2 channels are the main contributors to the macroscopic K+ current of glomus cells. The reversible inhibition of KO2 channel activity by low PO2 does not desensitize and is not related to the presence of F-, ATP, and GTP-gamma-S at the internal face of the membrane. These results indicate that KO2 channels confer upon glomus cells their unique chemoreceptor properties and that the O2-K+ channel interaction occurs either directly or through an O2 sensor intrinsic to the plasma membrane closely associated with the channel molecule.

scholarly journals Characterization of Convergent Suppression by UCL-2077 (3-(Triphenylmethylaminomethyl)pyridine), Known to Inhibit Slow Afterhyperpolarization, of erg-Mediated Potassium Currents and Intermediate-Conductance Calcium-Activated Potassium Channels

2020 ◽  
Vol 21 (4) ◽  
pp. 1441 ◽  
Author(s):  
Hung-Te Hsu ◽  
Yi-Ching Lo ◽  
Sheng-Nan Wu
Keyword(s):  
Ionic Currents ◽  
Gh3 Cells ◽  
Excitable Cells ◽  
Activation Curve ◽  
K Channels ◽  
Kd Values ◽  
K Current ◽  
Calcium Activated Potassium Channels ◽  
Voltage Hysteresis

UCL-2077 (triphenylmethylaminomethyl)pyridine) was previously reported to suppress slow afterhyperpolarization in neurons. However, the information with respect to the effects of UCL-2077 on ionic currents is quite scarce. The addition of UCL-2077 decreased the amplitude of erg-mediated K+ current (IK(erg)) together with an increased deactivation rate of the current in pituitary GH3 cells. The IC50 and KD values of UCL-2077-induced inhibition of IK(erg) were 4.7 and 5.1 μM, respectively. UCL-2077 (10 μM) distinctly shifted the midpoint in the activation curve of IK(erg) to less hyperpolarizing potentials by 17 mV. Its presence decreased the degree of voltage hysteresis for IK(erg) elicitation by long-lasting triangular ramp pulse. It also diminished the probability of the opening of intermediate-conductance Ca2+-activated K+ channels. In cell-attached current recordings, UCL-2077 raised the frequency of action currents. When KCNH2 mRNA was knocked down, a UCL-2077-mediated increase in AC firing was attenuated. Collectively, the actions elaborated herein conceivably contribute to the perturbating effects of this compound on electrical behaviors of excitable cells.

Different properties of the atrial G protein-gated K+ channels activated by extracellular ATP and adenosine

1995 ◽  
Vol 269 (4) ◽  
pp. H1349-H1358 ◽  
Author(s):  
C. Fu ◽  
A. Pleumsamran ◽  
U. Oh ◽  
D. Kim
Keyword(s):  
G Protein ◽  
Single Channel ◽  
Extracellular Atp ◽  
K Channel ◽  
Affinity Constant ◽  
Channel Activity ◽  
K Channels ◽  
Atrial Cells ◽  
K Current ◽  
Inside Out

Extracellular ATP (ATPo) and adenosine activate G protein-gated inwardly rectifying K+ currents in atrial cells. Earlier studies have suggested that the two agonists may use separate pathways to activate the K+ current. Therefore, we examined whether the K+ channels activated by the two agonists have different properties under identical ionic conditions. In cell-attached patches, K+ channels activated by 100 microM ATP in the pipette had a single-channel conductance and mean open time of 32.0 +/- 0.2 pS and 0.5 +/- 0.1 ms, respectively, compared with 31.3 +/- 0.3 pS and 0.9 +/- 0.1 ms for the K+ channels activated by adenosine (140 mM KCl). With ATPo as the agonist, the K+ channel activity in cell-attached patches was approximately threefold lower than that in inside-out patches with 100 microM GTP in the bath. Applying ATP to the cytoplasmic side of the membrane (ATPi) produced a biphasic concentration-dependent effect on channel activity: an increase at low [mean affinity constant (K0.5) = 190 microM] and a decrease at high (K0.5 = 1.3 mM) concentrations. In contrast, with adenosine as the agonist, K+ channel activity in cell-attached patches was approximately fourfold greater than that in inside-out patches with 100 microM GTP in the bath. In inside-out patches, ATPi only augmented the K+ channel activity (K0.5 = 32 microM). These results show that although both ATPo and adenosine activate kinetically similar K+ channels in atrial cells, the channels are regulated differently by intracellular nucleotides.

scholarly journals K+ channels of stomatal guard cells. Characteristics of the inward rectifier and its control by pH.

1992 ◽  
Vol 99 (4) ◽  
pp. 615-644 ◽  
Author(s):  
M R Blatt
Keyword(s):  
Intracellular Ph ◽  
Guard Cells ◽  
Inward Rectifier ◽  
Equilibrium Potential ◽  
Egg Cell ◽  
K Channels ◽  
Inward Rectifiers ◽  
Stomatal Guard Cells ◽  
K Current ◽  
Current Reversal

Intracellular microelectrode recordings and a two-electrode voltage clamp have been used to characterize the current carried by inward rectifying K+ channels of stomatal guard cells from the broadbean, Vicia faba L. Superficially, the current displayed many features common to inward rectifiers of neuromuscular and egg cell membranes. In millimolar external K+ concentrations (Ko+), it activated on hyperpolarization with half-times of 100-200 ms, showed no evidence of time- or voltage-dependent inactivation, and deactivated rapidly (tau approximately 10 ms) on clamping to 0 mV. Steady-state conductance-voltage characteristics indicated an apparent gating charge of 1.3-1.6. Current reversal showed a Nernstian dependence on Ko+ over the range 3-30 mM, and the inward rectifier was found to be highly selective for K+ over other monovalent cations (K+ greater than Rb+ greater than Cs+ much greater than Na+). Unlike the inward rectifiers of animal membranes, the current was blocked by charybdotoxin and alpha-dendrotoxin (Kd much less than 50 nM), as well as by tetraethylammonium chloride (K1/2 = 9.1 mM); gating of the guard cell K+ current was fixed to voltages near -120 mV, independent of Ko+, and the current activated only with supramillimolar K+ outside (EK+ greater than -120 mV). Most striking, however, was inward rectifier sensitivity to [H+] with the K+ current activated reversibly by mild acid external pH. Current through the K+ inward rectifier was found to be largely independent of intracellular pH and the current reversal (equilibrium) potential was unaffected by pHo from 7.4 to 5.5. By contrast, current through the K+ outward rectifier previously characterized in these cells (1988. J. Membr. Biol. 102:235) was largely insensitive to pHo, but was blocked reversibly by acid-going intracellular pH. The action of pHo on the K+ inward rectifier could not be mimicked by extracellular Ca2+ for which changes in activation, deactivation, and conductance were consonant with an effect on surface charge ([Ca2+] less than or equal to 1 mM). Rather, extracellular pH affected activation and deactivation kinetics disproportionately, with acid-going pHo raising the K+ conductance and shifting the conductance-voltage profile positive-going along the voltage axis and into the physiological voltage range. Voltage and pH dependencies for gating were consistent with a single, titratable group (pKa approximately 7 at -200 mV) residing deep within the membrane electric field and accessible from the outside.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Nateglinide, but not repaglinide, stimulates growth hormone release in rat pituitary cells by inhibition of K channels and stimulation of cyclic AMP-dependent exocytosis

2002 ◽  
pp. 133-142 ◽  
Author(s):  
J Gromada ◽  
K Bokvist ◽  
M Hoy ◽  
HL Olsen ◽  
P Lindstrom ◽  
...  
Keyword(s):  
Action Potential ◽  
Oral Glucose ◽  
Pituitary Cells ◽  
Action Potential Firing ◽  
K Channels ◽  
Gh Secretion ◽  
Potential Firing ◽  
K Current ◽  
Rat Pituitary Cells ◽  
Stimulation Of

OBJECTIVE: GH causes insulin resistance, impairs glycemic control and increases the risk of vascular diabetic complications. Sulphonylureas stimulate GH secretion and this study was undertaken to investigate the possible stimulatory effect of repaglinide and nateglinide, two novel oral glucose regulators, on critical steps of the stimulus-secretion coupling in single rat somatotrophs. METHODS: Patch-clamp techniques were used to record whole-cell ATP-sensitive K(+) (K(ATP)) and delayed outward K(+) currents, membrane potential and Ca(2+)-dependent exocytosis. GH release was measured from perifused rat somatotrophs. RESULTS: Both nateglinide and repaglinide dose-dependently suppressed K(ATP) channel activity with half-maximal inhibition being observed at 413 nM and 13 nM respectively. Both compounds induced action potential firing in the somatotrophs irrespective of whether GH-releasing hormone was present or not. The stimulation of electrical activity by nateglinide, but not repaglinide, was associated with an increased mean duration of the action potentials. The latter effect correlated with a reduction of the delayed outward K(+) current, which accounts for action potential repolarization. The latter effect had a K(d) of 19 microM but was limited to 38% inhibition. When applied at concentrations similar to those required to block K(ATP) channels, nateglinide in addition potentiated Ca(2+)-evoked exocytosis 3.3-fold (K(d)=3 microM) and stimulated GH release 4.5-fold. The latter effect was not shared by repaglinide. The stimulation of exocytosis by nateglinide was mimicked by cAMP and antagonized by the protein kinase A inhibitor Rp-cAMPS. CONCLUSION: Nateglinide stimulates GH release by inhibition of plasma membrane K(+) channels, elevation of cytoplasmic cAMP levels and stimulation of Ca(2+)-dependent exocytosis. By contrast, the effect of repaglinide was confined to inhibition of the K(ATP) channels.

scholarly journals ATP-sensitive K+ channels in a plasma membrane H+-ATPase mutant of the yeast Saccharomyces cerevisiae.

1989 ◽  
Vol 86 (20) ◽  
pp. 7866-7870 ◽  
Author(s):  
J. A. Ramirez ◽  
V. Vacata ◽  
J. H. McCusker ◽  
J. E. Haber ◽  
R. K. Mortimer ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Yeast Saccharomyces Cerevisiae ◽  
K Channels
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