scholarly journals Maintenance of K+/Na+ Balance in the Roots of Nitraria sibirica Pall. in Response to NaCl Stress

Forests ◽  
2018 ◽  
Vol 9 (10) ◽  
pp. 601 ◽  
Author(s):  
Xiaoqian Tang ◽  
Xiuyan Yang ◽  
Huanyong Li ◽  
Huaxin Zhang
Keyword(s):  
Plasma Membrane ◽  
Nacl Stress ◽  
K Channel ◽  
Sodium Vanadate ◽  
Atpase Inhibitor ◽  
K Channels ◽  
Non Invasive ◽  
Na Efflux ◽  
Seedling Roots ◽  
Nitraria Sibirica

Using Non-invasive Micro-test Technology (NMT), the Na+, K+ and H+ flux profiles in the root meristem regions were investigated in Nitraria sibirica Pall. seedlings under different NaCl concentrations. NaCl stress increased the K+ and Na+ contents in the roots of N. sibirica seedlings. NaCl stress significantly increased the steady Na+ efflux from the N. sibirica seedling roots. Steady K+ effluxes were measured in the control roots (without NaCl) and in the roots treated with 200 mM NaCl, and no significant differences were observed between the two treatments. The steady K+ efflux from roots treated with 400 mM NaCl decreased gradually. NaCl treatment significantly increased the H+ influx. Pharmacological experiments showed that amiloride and sodium vanadate significantly inhibited the Na+ efflux and H+ influx, suggesting that the Na+ efflux was mediated by a Na+/H+ antiporter using energy provided by plasma membrane H+-ATPase. The NaCl-induced root K+ efflux was inhibited by the K+ channel inhibitor tetraethylammonium chloride (TEA), and was significantly increased by the H+-ATPase inhibitor sodium vanadate. The NaCl-induced K+ efflux was mediated by depolarization-activated outward-rectifying K+ channels and nonselective cation channels (NSCCs). Under salt stress, N. sibirica seedlings showed increased Na+ efflux due to increased plasma membrane H+-ATPase and Na+/H+ antiporter activity. High H+ pump activity not only restricts the Na+ influx through NSCCs, but also limits K+ leakage through outward-rectifying K+ channels and NSCCs, leading to maintenance of the K+/Na+ balance and higher salt tolerance.

scholarly journals Messenger-mediated control of potassium channels in secretory cells

1986 ◽  
Vol 124 (1) ◽  
pp. 33-52
Author(s):  
O. H. Petersen ◽  
I. Findlay ◽  
K. Suzuki ◽  
M. J. Dunne
Keyword(s):  
Plasma Membrane ◽  
Pancreatic Beta Cells ◽  
Acinar Cells ◽  
Direct Access ◽  
K Channel ◽  
Secretory Cells ◽  
Single Channels ◽  
Intact Cells ◽  
Membrane Area ◽  
K Channels

In exocrine acinar cells (pancreas, salivary gland, lacrimal gland) stimulation with hormones or neurotransmitters evokes K+ loss due to opening of K+ channels in the plasma membrane whereas in the insulin-secreting pancreatic beta-cells, stimulation with glucose or glyceraldehyde evokes membrane depolarization due to closure of K+ channels. By measuring directly the small K+ currents flowing through single channels, in electrically isolated patches of plasma membrane of intact cells, it can be shown that stimulants having no direct access to the small membrane area from which recording is made can influence the pattern of channel opening. In the case of hormonal activation of exocrine acinar cells, Ca2+ is the final messenger and the K+-selective channel involved in the response has a high unit conductance, is very voltage sensitive and can be blocked by external tetraethylammonium. In the case of the insulin-secreting cells, the K+ channel which is inhibited by metabolic stimulation is a voltage-insensitive, inward rectifier which can be blocked by quinine. In experiments on permeabilized cells or cell-free excised, inside-out, membrane patches it can be shown that ATP evokes channel closure and ATP produced by glycolysis may therefore function as the internal messenger.

scholarly journals Exogenous Potassium (K+) Positively Regulates Na+/H+ Antiport System, Carbohydrate Metabolism, and Ascorbate–Glutathione Cycle in H2S-Dependent Manner in NaCl-Stressed Tomato Seedling Roots

Plants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 948
Author(s):  
M. Nasir Khan ◽  
Soumya Mukherjee ◽  
Asma A. Al-Huqail ◽  
Riyadh A. Basahi ◽  
Hayssam M. Ali ◽  
...  
Keyword(s):  
Carbohydrate Metabolism ◽  
Reactive Oxygen Species Generation ◽  
Nacl Stress ◽  
K Channel ◽  
Dependent Manner ◽  
Defense System ◽  
Tomato Seedling ◽  
Seedling Roots ◽  
Glutathione Cycle

Potassium (K+) is one of the vital macronutrients required by plants for proper growth and blossoming harvest. In addition, K+ also plays a decisive role in promoting tolerance to various stresses. Under stressful conditions, plants deploy their defense system through various signaling molecules, including hydrogen sulfide (H2S). The present investigation was carried out to unravel the role of K+ and H2S in plants under NaCl stress. The results of the study show that NaCl stress caused a reduction in K+ and an increase in Na+ content in the tomato seedling roots which coincided with a lower H+-ATPase activity and K+/Na+ ratio. However, application of 5 mM K+, in association with endogenous H2S, positively regulated the Na+/H+ antiport system that accelerated K+ influx and Na+ efflux, resulting in the maintenance of a higher K+/Na+ ratio. The role of K+ and H2S in the regulation of the Na+/H+ antiport system was validated by applying sodium orthovanadate (plasma membrane H+-ATPase inhibitor), tetraethylammonium chloride (K+ channel blocker), amiloride (Na+/H+ antiporter inhibitor), and hypotaurine (HT, H2S scavenger). Application of 5 mM K+ positively regulated the ascorbate–glutathione cycle and activity of antioxidant enzymes that resulted in a reduction in reactive oxygen species generation and associated damage. Under NaCl stress, K+ also activated carbohydrate metabolism and proline accumulation that caused improvement in osmotic tolerance and enhanced the hydration level of the stressed seedlings. However, inclusion of the H2S scavenger HT reversed the effect of K+, suggesting H2S-dependent functioning of K+ under NaCl stress. Therefore, the present findings report that K+, in association with H2S, alleviates NaCl-induced impairments by regulating the Na+/H+ antiport system, carbohydrate metabolism, and antioxidative defense system.

Salinity effects on chloroplast PSII performance in glycophytes and halophytes

2016 ◽  
Vol 43 (11) ◽  
pp. 1003 ◽  
Author(s):  
William J. Percey ◽  
Andrew McMinn ◽  
Jayakumar Bose ◽  
Michael C. Breadmore ◽  
Rosanne M. Guijt ◽  
...  
Keyword(s):  
Critical Role ◽  
Photochemical Efficiency ◽  
Chenopodium Quinoa ◽  
Nacl Stress ◽  
Photosynthetic Performance ◽  
K Channel ◽  
Photosynthetic Parameters ◽  
Atpase Inhibitor ◽  
Mesophyll Cells ◽  
Isolated Chloroplasts

The effects of NaCl stress and K+ nutrition on photosynthetic parameters of isolated chloroplasts were investigated using PAM fluorescence. Intact mesophyll cells were able to maintain optimal photosynthetic performance when exposed to salinity for more than 24 h whereas isolated chloroplasts showed declines in both the relative electron transport rate (rETR) and the maximal photochemical efficiency of PSII (Fv/Fm) within the first hour of treatment. The rETR was much more sensitive to salt stress compared with Fv/Fm, with 40% inhibition of rETR observed at apoplastic NaCl concentration as low as 20 mM. In isolated chloroplasts, absolute K+ concentrations were more essential for the maintenance of the optimal photochemical performance (Fv/Fm values) rather than sodium concentrations per se. Chloroplasts from halophyte species of quinoa (Chenopodium quinoa Willd.) and pigface (Carpobrotus rosii (Haw.) Schwantes) showed less than 18% decline in Fv/Fm under salinity, whereas the Fv/Fm decline in chloroplasts from glycophyte pea (Pisum sativum L.) and bean (Vicia faba L.) species was much stronger (31 and 47% respectively). Vanadate (a P-type ATPase inhibitor) significantly reduced Fv/Fm in both control and salinity treated chloroplasts (by 7 and 25% respectively), whereas no significant effects of gadolinium (blocker of non-selective cation channels) were observed in salt-treated chloroplasts. Tetraethyl ammonium (TEA) (K+ channel inhibitor) and amiloride (inhibitor of the Na+/H+ antiporter) increased the Fv/Fm of salinity treated chloroplasts by 16 and 17% respectively. These results suggest that chloroplasts’ ability to regulate ion transport across the envelope and thylakoid membranes play a critical role in leaf photosynthetic performance under salinity.

Enhanced role of K+ channels in relaxations of hypercholesterolemic rabbit carotid artery to NO

1995 ◽  
Vol 269 (3) ◽  
pp. H805-H811 ◽  
Author(s):  
S. Najibi ◽  
R. A. Cohen
Keyword(s):  
Carotid Artery ◽  
Sodium Nitroprusside ◽  
Channel Blocker ◽  
Isometric Tension ◽  
K Channel ◽  
K Channels ◽  
Rabbit Carotid Artery ◽  
Cyclic Monophosphate ◽  
Endothelium Dependent Relaxation

Endothelium-dependent relaxations to acetylcholine remain normal in the carotid artery of hypercholesterolemic rabbits, but unlike endothelium-dependent relaxations of normal rabbits, they are inhibited by charybdotoxin, a specific blocker of Ca(2+)-dependent K+ channels. Because nitric oxide (NO) is the mediator of endothelium-dependent relaxation and can activate Ca(2+)-dependent K+ channels directly or via guanosine 3',5'-cyclic monophosphate, the present study investigated the role of Ca(2+)-dependent K+ channels in relaxations caused by NO, sodium nitroprusside, and 8-bromoguanosine 3',5'-cyclic monophosphate (8-Brc-GMP) in hypercholesterolemic rabbit carotid artery. Isometric tension was measured in rabbit carotid artery denuded of endothelium from normal and hypercholesterolemic rabbits which were fed 0.5% cholesterol for 12 wk. Under control conditions, relaxations to all agents were similar in normal and hypercholesterolemic rabbit arteries. Charybdotoxin had no significant effect on relaxations of normal arteries to NO, sodium nitroprusside, or 8-BrcGMP, but the Ca(2+)-dependent K+ channel blocker significantly inhibited the relaxations caused by each of these agents in the arteries from hypercholesterolemic rabbits. By contrast, relaxations to the calcium channel blocker nifedipine were potentiated to a similar extent by charybdotoxin in both groups. In addition, arteries from hypercholesterolemic rabbits relaxed less than normal to sodium nitroprusside when contracted with depolarizing potassium solution. These results indicate that although nitrovasodilator relaxations are normal in the hypercholesterolemic rabbit carotid artery, they are mediated differently, and to a greater extent, by Ca(2+)-dependent K+ channels. These data also suggest that K+ channel-independent mechanism(s) are impaired in hypercholesterolemia.

scholarly journals Membrane-delimited Inhibition of Maxi-K Channel Activity by the Intermediate Conductance Ca2+-activated K Channel

2006 ◽  
Vol 127 (2) ◽  
pp. 159-169 ◽  
Author(s):  
Jill Thompson ◽  
Ted Begenisich
Keyword(s):  
Single Channel ◽  
Expression System ◽  
Chemical Activation ◽  
K Channel ◽  
Channel Activity ◽  
Single Family ◽  
Open Probability ◽  
K Channels ◽  
Channel Proteins ◽  
K Activity

The complexity of mammalian physiology requires a diverse array of ion channel proteins. This diversity extends even to a single family of channels. For example, the family of Ca2+-activated K channels contains three structural subfamilies characterized by small, intermediate, and large single channel conductances. Many cells and tissues, including neurons, vascular smooth muscle, endothelial cells, macrophages, and salivary glands express more than a single class of these channels, raising questions about their specific physiological roles. We demonstrate here a novel interaction between two types of Ca2+-activated K channels: maxi-K channels, encoded by the KCa1.1 gene, and IK1 channels (KCa3.1). In both native parotid acinar cells and in a heterologous expression system, activation of IK1 channels inhibits maxi-K activity. This interaction was independent of the mode of activation of the IK1 channels: direct application of Ca2+, muscarinic receptor stimulation, or by direct chemical activation of the IK1 channels. The IK1-induced inhibition of maxi-K activity occurred in small, cell-free membrane patches and was due to a reduction in the maxi-K channel open probability and not to a change in the single channel current level. These data suggest that IK1 channels inhibit maxi-K channel activity via a direct, membrane-delimited interaction between the channel proteins. A quantitative analysis indicates that each maxi-K channel may be surrounded by four IK1 channels and will be inhibited if any one of these IK1 channels opens. This novel, regulated inhibition of maxi-K channels by activation of IK1 adds to the complexity of the properties of these Ca2+-activated K channels and likely contributes to the diversity of their functional roles.

scholarly journals Correlation between Charge Movement and Ionic Current during Slow Inactivation in Shaker K+ Channels

1997 ◽  
Vol 110 (5) ◽  
pp. 579-589 ◽  
Author(s):  
Riccardo Olcese ◽  
Ramón Latorre ◽  
Ligia Toro ◽  
Francisco Bezanilla ◽  
Enrico Stefani
Keyword(s):  
Time Course ◽  
Voltage Dependence ◽  
Ionic Current ◽  
K Channel ◽  
Charge Movement ◽  
Slow Inactivation ◽  
Gating Currents ◽  
Similar Time ◽  
K Channels ◽  
Recovery From Inactivation

Prolonged depolarization induces a slow inactivation process in some K+ channels. We have studied ionic and gating currents during long depolarizations in the mutant Shaker H4-Δ(6–46) K+ channel and in the nonconducting mutant (Shaker H4-Δ(6–46)-W434F). These channels lack the amino terminus that confers the fast (N-type) inactivation (Hoshi, T., W.N. Zagotta, and R.W. Aldrich. 1991. Neuron. 7:547–556). Channels were expressed in oocytes and currents were measured with the cut-open-oocyte and patch-clamp techniques. In both clones, the curves describing the voltage dependence of the charge movement were shifted toward more negative potentials when the holding potential was maintained at depolarized potentials. The evidences that this new voltage dependence of the charge movement in the depolarized condition is associated with the process of slow inactivation are the following: (a) the installation of both the slow inactivation of the ionic current and the inactivation of the charge in response to a sustained 1-min depolarization to 0 mV followed the same time course; and (b) the recovery from inactivation of both ionic and gating currents (induced by repolarizations to −90 mV after a 1-min inactivating pulse at 0 mV) also followed a similar time course. Although prolonged depolarizations induce inactivation of the majority of the channels, a small fraction remains non–slow inactivated. The voltage dependence of this fraction of channels remained unaltered, suggesting that their activation pathway was unmodified by prolonged depolarization. The data could be fitted to a sequential model for Shaker K+ channels (Bezanilla, F., E. Perozo, and E. Stefani. 1994. Biophys. J. 66:1011–1021), with the addition of a series of parallel nonconducting (inactivated) states that become populated during prolonged depolarization. The data suggest that prolonged depolarization modifies the conformation of the voltage sensor and that this change can be associated with the process of slow inactivation.

scholarly journals Acute Oxygen Sensing in Heme Oxygenase-2 Null Mice

2006 ◽  
Vol 128 (4) ◽  
pp. 405-411 ◽  
Author(s):  
Patricia Ortega-Sáenz ◽  
Alberto Pascual ◽  
Raquel Gómez-Díaz ◽  
José López-Barneo
Keyword(s):  
Gene Expression ◽  
K Channel ◽  
Α Subunit ◽  
Organ Growth ◽  
K Channels ◽  
Channel Gene ◽  
Sensitive Organ ◽  
Stress Dependent ◽  
Acute Oxygen Sensing ◽  
O2 Sensing

Hemeoxygenase-2 (HO-2) is an antioxidant enzyme that can modulate recombinant maxi-K+ channels and has been proposed to be the acute O2 sensor in the carotid body (CB). We have tested the physiological contribution of this enzyme to O2 sensing using HO-2 null mice. HO-2 deficiency leads to a CB phenotype characterized by organ growth and alteration in the expression of stress-dependent genes, including the maxi-K+ channel α-subunit. However, sensitivity to hypoxia of CB is remarkably similar in HO-2 null animals and their control littermates. Moreover, the response to hypoxia in mouse and rat CB cells was maintained after blockade of maxi-K+ channels with iberiotoxin. Hypoxia responsiveness of the adrenal medulla (AM) (another acutely responding O2-sensitive organ) was also unaltered by HO-2 deficiency. Our data suggest that redox disregulation resulting from HO-2 deficiency affects maxi-K+ channel gene expression but it does not alter the intrinsic O2 sensitivity of CB or AM cells. Therefore, HO-2 is not a universally used acute O2 sensor.

scholarly journals Selective Mobility and Sensitivity to SNAREs Is Exhibited by the Arabidopsis KAT1 K+ Channel at the Plasma Membrane

2006 ◽  
Vol 18 (4) ◽  
pp. 935-954 ◽  
Author(s):  
Jens-Uwe Sutter ◽  
Prisca Campanoni ◽  
Matthew Tyrrell ◽  
Michael R. Blatt
Keyword(s):  
Plasma Membrane ◽  
K Channel

scholarly journals Amplification of the thapsigargin-evoked increase in the cytosolic free Ca2+ concentration by acetylcholine in acutely isolated mouse submandibular acinar cells

1996 ◽  
Vol 317 (3) ◽  
pp. 779-783 ◽  
Author(s):  
Peter. M. SMITH ◽  
Helen. E. REED
Keyword(s):  
Plasma Membrane ◽  
Time Course ◽  
Acinar Cells ◽  
Fold Increase ◽  
Extrusion Process ◽  
Significant Alteration ◽  
Atpase Inhibitor ◽  
Fura 2

The intracellular Ca2+ concentration was measured in single, acutely isolated, mouse submandibular acinar cells loaded with fura-2 AM. All experiments were performed in the absence of extracellular Ca2+ in order to eliminate Ca2+ influx. The microsomal ATPase inhibitor, thapsigargin, was used to release Ca2+ from intracellular stores and simultaneously prevent re-uptake into the stores. Sequential application of thapsigargin (2 μM) and the Ca2+ ionophore ionomycin (500 nM) indicated that thapsigargin was able to mobilize practically all intracellular Ca2+. Furthermore, in comparison with results obtained following inhibition of the plasma membrane Ca2+-ATPase by La3+ (2 mM), it may be shown that slowly unloading the intracellular Ca2+ stores using thapsigargin does not normally cause a massive, cytotoxic, increase in the cytosolic Ca2+ concentration, because Ca2+ is rapidly extruded from the cell across the plasma membrane. Application of a submaximal dose of acetylcholine (500 nM) during the rising phase of the response to thapsigargin caused a 3–4-fold increase in the amplitude of the rise in the cytosolic Ca2+ concentration without any significant alteration of the time course of the response. As thapsigargin alone is capable of mobilizing all releasable Ca2+, this increase in amplitude is most likely the result of inhibition of the Ca2+ extrusion process by acetylcholine.

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