Permeation of both cations and anions through a single class of ATP-activated ion channels in developing chick skeletal muscle.

Micromolar concentrations of extracellular adenosine 5'-triphosphate (ATP) elicit a rapid excitatory response in developing chick skeletal muscle. Excitation is the result of a simultaneous increase in membrane permeability to sodium, potassium, and chloride ions. In the present study we quantify the selectivity of the ATP response, and provide evidence that a single class of ATP-activated ion channels conducts both cations and anions. Experiments were performed on myoballs using the whole-cell patch-clamp technique. We estimated permeability ratios by measuring the shift in reversal potential when one ion was substituted for another. We found that monovalent cations, divalent cations, and monovalent anions all permeate the membrane during the ATP response, and that there was only moderate selectivity between many of these ions. Calcium was the most permeant ion tested. To determine if ATP activates a single class of channels that conducts both cations and anions, or if ATP activates separate classes of cation and anion channels, we analyzed the fluctuations about the mean current induced by ATP. Ionic conditions were arranged so that the reversal potential for cations was +50 mV and the reversal potential for anions was -50 mV. Under these conditions, if ATP activates a single class of channels, ATP should not evoke an increase in noise at the reversal potential of the ATP current. However, if ATP activates separate classes of cation and anion channels, ATP should evoke a significant increase in noise at the reversal potential of the ATP current. At both +40 and -50 mV ATP elicited a clear increase in noise, but at the reversal potential of the ATP current (-5 mV), no increase in noise above background was seen. These results indicate that there is only a single class of excitatory ATP-activated channels, which do not select by charge. Based on analysis of the noise spectrum, the conductance of individual channels is estimated to be 0.2-0.4 pS.     

Properties of Two Outward-Rectifying Channels in Root Xylem Parenchyma Cells Suggest a Role in K+ Homeostasis and Long-Distance Signaling

Xylem parenchyma cells (XPCs) control the composition of the transpiration stream in plants and are thought to play a role in long-distance signaling as well. We addressed the regulation, selectivity, and dependence on the apoplastic ion concentrations of two types of outward rectifiers in the plasma membrane of XPCs, to assess the physiological role of these conductances. In whole-cell recordings, the membrane conductance at depolarization was under the control of cytosolic Ca2+: at physiological Ca2+ levels (150 nM) the K+ outward-rectifying conductance (KORC) predominated, whereas at elevated Ca2+ levels (5 [mu]M), only the nonselective outward-rectifying conductance (NORC) was active. No such regulatory effect of Ca2+ was observed in inside-out experiments. The voltage dependence of whole-cell KORC currents strongly depended on apoplastic K+ concentration: an increase in apoplastic K+ resulted in a positive shift of the current-voltage curve, roughly following the shift in Nernst potential of K+. KORC is impermeable to Na+, but does translocate Ca2+ in addition to K+. In contrast to KORC, NORC selected poorly among monovalent cations and anions, the relative permeability PC+/PA- being about 1.9. Gating of NORC was largely unaffected by the level of K+ in the bath. Under all ionic conditions tested, NORC tail currents or single-channel currents reversed close to 0 mV. Using an in vivo xylem-perfusion technique, tetraethylammonium (an inhibitor of KORC) was shown to block K+ transport to the shoot. These data support the hypothesis that release of K+ to the xylem sap is mediated by KORC. The molecular properties of these two conductances are discussed in the light of the distinct physiological role of XPCs.     

Calcium- and voltage-dependent ion channels in Saccharomyces cerevisiae.

Ion channels in both the tonoplast and the plasma membrane of Saccharomyces cerevisiae have been characterized at the single channel level by patch-clamp techniques. The predominant tonoplast channel is cation selective, has an open-channel conductance of 120 pS in 100 mM KCl, and conducts Na+ or K+ equally well, and Ca2+ to a lesser extent. Its open probability (Po) is voltage-dependent, peaking at about -80 mV (cytoplasm negative), and falling to near zero at +80 mV. Elevated cytoplasmic Ca2+, alkaline cytoplasmic pH, and reducing agents activate the channel. The predominant plasma membrane channel is highly selective for K+ over anions and other cations, and shows strong outward rectification of the time-averaged current-voltage curves in cell-attached experiments. In isolated inside-out patches with micromolar cytoplasmic Ca2+, this channel is activated by positive going membrane voltages: mean Po is zero at negative membrane voltages and near unity at 100 mV. At moderate positive membrane voltages (20-40 mV), elevating cytoplasmic Ca2+ activates the channel to open in bursts of several hundred milliseconds duration. At higher positive membrane voltages, however, elevating cytoplasmic Ca2+ blocks the channel in a voltage-dependent fashion for periods of 2-3 ms. The frequency of these blocking events depends on cytoplasmic Ca2+ and membrane voltage according to second-order kinetics. Alternative cations, such as Mg2+ or Na+, block the yeast plasma-membrane K+ channel in a similar but less pronounced manner.     

Inward and outward K+-selective currents in the plasma membrane of protoplasts from maize root cortex and stele

In an attempt to understand the processes mediating ion transport within the root, the patch clamp technique was applied to protoplasts isolated from the cortex and stele of maize roots and their plasma membrane conductances investigated. In the whole-cell configuration, membrane hyperpolarization induced a slowly activating inwardly rectifying conductance in most protoplasts isolated from the root cortex. In contrast, most protoplasts isolated from the stele contained a slowly activating outwardly rectifying conductance upon plasma membrane depolarization. The reversal potential of the inward current indicated that it was primarily due to the movement of K⁺; the outwardly rectifying conductance was comparatively less selective for K⁺. Membrane hyperpolarization beyond a threshold of about ?70 mV induced inward currents. When E_K was set negative of this threshold, inward currents activated negative of E_K and no outward currents were observed positive of E_K. Outward currents in the stelar protoplasts activated at potentials positive of ?85 mV. However, when E_K was set positive of ?85 mV a small inward current was also observed at potentials negative (and slightly positive) of the equilibrium potential for K⁺. Inwardly and outwardly rectifying K⁺ channels were observed in outside-out patches from the plasma membrane of cortical and stelar cells, respectively. Characterization of these channels showed that they were likely to be responsible for the macroscopic ‘whole-cell’ currents. Inward and outward currents were affected differently by various K⁺ channel blockers (TEA⁺, Ba²⁺ and Cs⁺). In addition, Ca²⁺ above 1 mM partially blocked the inward current in a voltage-dependent manner but had little effect on the outward current. It is suggested that the inwardly rectifying conductance identified in protoplasts isolated from the cortex probably represents an important component of the low-affinity K⁺ uptake mechanism (mechanism II) identified in intact roots. The outwardly rectifying conductance identified in protoplasts isolated from the stele could play a role in the release of cations into the xylem vessels for transport to the shoot.     

Cytochemical Localization of K-stimulated Adenosine Triphosphatase Activity in Xylem Parenchyma Cells of Barley Roots

ATPase activity in xylem parenchyma cells of barley (Hordeum vulgare L.) roots was demonstrated cytochemically with a lead precipitation reaction. The methodical parameters of this cytochemical test were optimized for distinction between ATPase-specific and nonspecific precipitates. Optimum conditions were prefixation in 1% glutaraldehyde for 1 hour and incubation for 2 hours in a medium containing 2 mm each of ATP, Ca(2+), and Pb(2+) at pH 7 and 25 C. Problems of cytochemical localizations are discussed.ATPase activity occurred mainly at the plasmalemma, the endoplasmic reticulum nuclear envelope, and outer mitochondrial membranes of xylem parenchyma cells. The tonoplast of these cells showed only little ATPase activity. High K(+) concentrations stimulated ATPase activity, particularly at the plasmalemma. Diethylstilbestrol prevented the formation of ATPase-specific precipitates. The cytochemical demonstration of a K(+)-stimulated ATPase at the plasmalemma of xylem parenchyma cells is discussed in relation to the possible role of this membrane in ion transport to the vessels.     

Single-channel properties of a rat brain endoplasmic reticulum anion channel.

Many intracellular membranes contain ion channels, although their physiological roles are often poorly understood. In this study we incorporated single anion channels colocalized with rat brain endoplasmic reticulum (ER) ryanodine-sensitive Ca(2+)-release channels into planar lipid bilayers. The channels opened in bursts, with more activity at negative (cytoplasm-ER lumen) membrane potentials, and they occupied four open conductance levels with frequencies well described by the binomial equation. The probability of a protomer being open decreased from approximately 0.7 at -40 mV to approximately 0.2 at +40 mV, and the channels selected between different anions in the order PSCN > PNO3 > PBr > PCl > PF. They were also permeant to cations, including the large cation Tris+ (PTris/PCl = 0.16). Their conductance saturated at 170 pS in choline Cl. The channels were inactivated by 15 microM 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS) and blocked with low affinity (KD of 1-100 microM) by anthracene-9-carboxylic acid, ethacrynic acid, frusemide (furosemide), HEPES, the indanyloxyacetic acid derivative IAA-94, 5-nitro-2-(3-phenylpropylamino)-benzoate (NPPB), and Zn2+. Unlike protein translocation pores, the channels were unaffected by high salt concentrations or puromycin. They may regulate ER Ca2+ release, or be channel components en route to their final cellular destinations. Alternatively, they may contribute to the fusion machinery involved in intracellular membrane trafficking.     

Background osmolyte current involved in cell volume regulation of neuroblastoma x glioma hybrid NG108-15 cells.

Recently, we showed that at constant extracellular osmolarity, the volume of NG108-15 cells was dependent on the external NaCl concentration and we assumed that the responsible mechanism was mediated by background channels (Rouzaire-Dubois et al. 1999). In order to confirm this view, the mean cell volume and the background current of NG108-15 cells were measured under different experimental conditions, after blockade of specific volume regulating mechanisms and ion channels. When the external NaCl concentration was decreased, the reversal potential of the background current was shifted toward negative values and the membrane conductance decreased. Opposite effects were observed when the NaCl concentration was increased. Substitution of external Na+ with various monovalent cations altered the mean cell volume by: Rb+, +17%; Cs+, +15%; K+, +10%; Li+, -6%; choline, -9%; N-methylglucamine, -25% . The reversal potential of the background current and the membrane conductance were altered by these Na+ substitutes in such a way that the cell volume increased linearly with the background current at -60 mV. Substitution of external Cl- with various monovalent anions altered the mean cell volume by: I-, +4%; Br-, 0%; NO-, -3%; F-, -5%; isethionate, -30%; gluconate, -50%. Cl- substitutes did not significantly alter the background current at -60 mV, except F- which increased it by 39%. These results suggest that 1. the cell volume is dependent on ion fluxes through background channels; 2. electrogenic cation fluxes are larger than anionic ones and the background current is proportional to the difference between these fluxes; 3. whereas external cations do not interfere with anion fluxes, external anions alter cation fluxes.     

High-conductance K+ channels in guinea pig gallbladder epithelium]

Since secretion of electrolytes may be regulated by membrane potential difference, ion channels were studied using patchclamp technique. We have identified, in cell-attached configuration, inward-rectifying channels: the zero-current potential corresponded to the K+ equilibrium potential calculated from intracellular K+ activity. Using inside-out configuration and symmetric 145 mM KCl salines, i/V curve was linear, channel conductance was about 170 pS and the reversal potential 0 mV. The channels were selective for K+ over Na+, N-methylglucamine and anions and were activated by membrane depolarization.     

Characteristics of inositol trisphosphate-mediated Ca2+ release from permeabilized hepatocytes

Ca2+ release triggered by inositol trisphosphate (Ins(1,4,5)P3) has been measured in saponin-permeabilized hepatocytes with 45Ca2+ or Quin 2. The initial rate of Ca2+ release was not greatly affected by the incubation temperature (175 +/- 40 pmol X s-1 X mg dry weight-1, at 30 degrees C versus 133 +/- 24 pmol X s-1 X mg dry weight-1 at 4 degrees C). The amount of Ca2+ released by Ins(1,4,5)P3 was not affected by pH (6.5-8.0). La3+ (100 microM) markedly inhibited the effect of 1 microM Ins(1,4,5)P3. The possibility that La3+ chelates Ins(1,4,5)P3 cannot be excluded since the effect of La3+ could be overcome by increasing the Ins(1,4,5)P3 concentration. Ins(1,4,5)P3-mediated Ca2+ release showed a requirement for permeant cations in the incubation medium. Optimal release was observed with potassium gluconate. Other monovalent cations, with the exception of Li+, can substitute for K+. Permeant anions, at concentrations above 40 mM, inhibited Ca2+ release produced by Ins(1,4,5)P3. Cl-, Br-, I-, and SO2-4 were equally effective as inhibitors. Ins(1,4,5)P3 also caused the release of 54Mn2+ and 85Sr2+ accumulated by the permeabilized hepatocytes. Our results are consistent with Ins(1,4,5)P3 promoting the membrane translocation of divalent cations through an ion channel rather than an ion carrier. The translocation of positive charge through this channel is balanced by ancillary movements of monovalent cations and anions across the reticular membranes. The transport systems responsible for these compensatory ion movements may represent a potential site for the regulation of the hormone-mediated Ca2+ signal.     

A mechanosensitive K+ channel in heart cells. Activation by arachidonic acid

Mechanosensitive ion channels have been described in many types of cells. These channels are believed to transduce pressure signals into intracellular biochemical and physiological events. In this study, the patch-clamp technique was used to identify and characterize a mechanosensitive ion channel in rat atrial cells. In cell-attached patches, negative pressure in the pipette activated an ion channel in a pressure-dependent manner. The pressure to induce half-maximal activation was 12 +/- 3 mmHg at +40 mV, and nearly full activation was observed at approximately 20 mmHg. The probability of opening was voltage dependent, with greater channel activity at depolarized potentials. The mechanosensitive channel was identical to the K+ channel previously shown to be activated by arachidonic acid and other lipophilic compounds, as judged by the outwardly rectifying current-voltage relation, single channel amplitude, mean open time (1.4 +/- 0.3 ms), bursty openings, K+ selectivity, insensitivity to any known organic inhibitors of ion channels, and pH sensitivity. In symmetrical 140 mM KCl, the slope conductance was 94 +/- 11 pS at +60 mV and 64 +/- 8 pS at -60 mV. Anions and cations such as Cl-, glutamate, Na+, Cs+, Li+, Ca2+, and Ba2+ were not permeant. Extracellular Ba2+ (1 mM) blocked the inward K+ current completely. GdCl3 (100 microM) or CaCl2 (100 microM) did not alter the K+ channel activity or amplitude. Lowering of intracellular pH increased the pressure sensitivity of the channel. The K+ channel could be activated in the presence of 5 mM intracellular [ATP] or 10 microM glybenclamide in inside-out patches. In the absence of ATP, when the ATP-sensitive K+ channel was active, the mechanosensitive channel could further be activated by pressure, suggesting that they were two separate channels. The ATP-sensitive K+ channel was not mechanosensitive. Pressure activated the K+ channel in the presence of albumin, a fatty acid binding protein, suggesting that pressure and arachidonic acid activate the K+ channel via separate pathways.     

Ion-transporting properties and ATPase activity of (Na+ + K+)-ATPase large subunit incorporated into bilayer lipid membranes

A purified (Na+ + K+)-ATPase large subunit obtained from microsomes by water-alcohol extraction was incorporated into a bilayer lipid membrane. The protein formed in the membrane conductance channels which were sensitive to ouabain and selective for monovalent cations. ATP activated these channels in the presence of sodium and potassium ions. When sodium ions were eliminated ATP did not change the conductance of the modified membrane whereas p-nitrophenyl phosphate increased it. The (Na+ + K+)-ATPase large subunit incorporated into bilayer lipid membrane possessed an ATPase activity. The presence of a potential on the membrane was a necessary condition for the enzyme incorporated into a bilayer lipid membrane to show high ATPase activity. Increasing the potential above 100 mV resulted in the closing of conductance channels.     

Membrane Potentials in the Xylem in Roots of Intact Plants

The membrane potential differences (PDs) of root cells of intact,illuminated Trifolium repens L. and Lolium perenne L. have beenmeasured. In T. repens the PDs were the same for all cell typesexcept for the xylem vessels, which were more positive, andfor some cells immediately adjacent to the xylem vessels whichwere 10 mV more negative. The mean PD for all cells was emdash164.6 ± 0.6 mV and the mean for cells adjacent to thexylem vessels with elevated PDs was 178.4 ± 2.4 mV. Whenthe electrode tip was in a xylem vessel a low but stable PD(mean = emdash 89.9 mV) was recorded. The results for L. perennewere similar except that there were no cells with elevated PDsadjacent to the xylem vessels. An inhibitor of ion transport from the root to the shoot, p-fluorophenylalanine(p-FPA), caused a depolarization of 10 mV in the cell PDs butin the xylem vessels the depolarization was 50 mV. The possibility that the elevated PDs of cells adjacent to thexylem vessels are related to the transport of ions into thevessels is discussed.     

Permeation and interaction of monovalent cations with the cGMP-gated channel of cone photoreceptors

We measured the ion selectivity of cGMP-dependent currents in detached membrane patches from the outer segment of cone photoreceptors isolated from the retina of striped bass. In inside-out patches excised from either single or twin cones the amplitude of these currents, under symmetric ionic solutions, changed with the concentration of cGMP with a dependence described by a Hill equation with average values, at +80 mV, of Km = 42.6 microM and n = 2.49. In the absence of divalent cations, and under symmetric ionic solutions, the I-V curves of the currents were linear over the range of -80 to +80 mV. The addition of Ca altered the form of the I-V curve to a new function well described by an empirical equation that also describes the I-V curve of the photocurrent measured in intact photoreceptors. The monovalent cation permeability sequence of the cGMP-gated channels in the absence of divalent ions was PK > PNa = PLi = PRb > PCs (1.11 > 1.0 = 0.99 = 0.96 > 0.82). The conductance selectivity sequence at +80 mV was GNa = GK > GRb > GCs > GLi (1.0 = 0.99 > 0.88 > 0.74 > 0.60). The organic cations tetramethylammonium (TMA) and arginine partially blocked the current, but the larger ion, arginine, was permeant, whereas the smaller ion, TMA, was not. The amplitude of the outward current through the channels increased with the concentration of monovalent cations on the cytoplasmic membrane surface, up to a saturating value. The increase was well described by the adsorption isotherm of a single ion binding site within the channel with average binding constants, at +80 mV, of 104 mM for Na and 37.6 mM for Li. By assuming that the ion channel contains a single ion binding site in an energy trough separated from each membrane surface by an energy barrier, and using Eyring rate theory, we simulated I-V curves that fit the experimental data measured under ionic concentration gradients. From this fit we conclude that the binding site interacts with one ion at a time and that the energy barriers are asymmetrically located within the membrane thickness. Comparison of the quantitative features of ion permeation and interaction between the cGMP-gated channels of rod and cone photoreceptors reveals that the ion binding sites are profoundly different in the two types of channels. This molecular difference may be particularly important in explaining the differences in the transduction signal of each receptor type.     

The delivery of salts to the xylem. Three types of anion conductance in the plasmalemma of the xylem parenchyma of roots of barley

To explore possible pathways for anions to enter the xylem in the root during the transport of salts to the shoot, we used the patch-clamp method on protoplasts prepared from the xylem parenchyma of barley (Hordeum vulgare L.) plants. K(+) currents were suppressed by tetraethylammonium or N-methylglucamine in the solutions in the pipette and the bath, and the permeating anions were Cl(-) or NO(3)(-). We recorded the activities of three distinct anion conductances: (a) an inwardly rectifying anion channel (X-IRAC), characterized by activation at hyperpolarization and open times of up to several seconds; (b) a quickly activating anion conductance (X-QUAC), important for anion efflux at voltages between -50 mV and the equilibrium potential of the prevailing anion; and (c) a slowly activating anion conductance (X-SLAC), activating above -100 mV. Both X-IRAC and X-QUAC were permeable for Cl(-) and NO(3)(-); X-QUAC was also permeable for malate. The occurrence of X-IRAC became more frequent with an increase in cytoplasmic Ca(2+), while the occurrence of X-QUAC decreased. Anion currents through X-SLAC, and particularly through X-QUAC, were estimated to be large enough to account for reported rates of xylem loading, which is in accordance with the notion that xylem loading is a passive process.     

Potassium Translocation into the Root Xylem

Abstract: Potassium is the most abundant cation in cells of higher plants and plays vital roles in plant growth and develop ment. Since the soil is the only source of potassium, plant roots are well adapted to exploit the soil for potassium and supply it to the leaves. Transport across the root can be divided into three stages: uptake into the root symplast, transport across the symplast and release into the xylem. Uptake kinetics of potassium have been studied extensively in the past and sug gested the presence of high and low affinity systems. Molecular and electrophysiological techniques have now confirmed the existence of discrete transporters encoded by a number of genes. Surprisingly, detailed characterisation of the transpor ters using reverse genetics and heterologous expression shows that a number of the transporters (AKT and AtKUP family) func tion both in the low (μM) and high (mM) K⁺ range. Electrophy siological studies indicate that K⁺ uptake by roots is coupled to H⁺, to drive uptake from micromolar K⁺. However, thus far only Na⁺ coupled K⁺ transport has been demonstrated (HKT1). Ion channels play a major role in the exchange of potassium be tween the symplast and the xylem. An outward rectifying chan nel (KORC) mediates potassium release. Cloning of the gene en coding this channel (SKOR) shows that it belongs to the Shaker super-family. Both electrophysiological and genetic studies demonstrate that K⁺ release through this channel is controlled by the stress hormone abscisic acid. Interestingly, xylem par enchyma cells of young barley roots also contain a number of in ward rectifying K⁺ channels that are controlled by G-proteins. The involvement of G-proteins emphasises once more that po tassium transport at the symplast/xylem boundary is under hor monal control. The role of the electrical potential difference across the symplastxylem boundary in controlling potassium release is discussed.     

Characterization of ion channels on the surface membrane of adult rat skeletal muscle.

The channels present on the surface membrane of isolated rat flexor digitorum brevis muscle fibers were surveyed using the patch clamp technique. 85 out of 139 fibers had a novel channel which excluded the anions chloride, sulfate, and isethionate with a permeability ratio of chloride to sodium of less than 0.05. The selectivity sequence for cations was Na+ = K+ = Cs+ greater than Ca++ = Mg++ greater than N-Methyl-D-Glucamine. The channel remained closed for long periods, and had a large conductance of approximately 320 pS with several subconductance states at approximately 34 pS levels. Channel activity was not voltage dependent and the reversal potential for cations in muscle fibers of approximately 0 mV results in the channel's behaving as a physiological leakage conductance. Voltage activated potassium channels were present in 65 of the cell attached patches and had conductances of mostly 6, 12, and 25 pS. The voltage sensitivity of the potassium channels was consistent with that of the delayed rectifier current. Only three patches contained chloride channels. The scarcity of chloride channels despite the known high chloride conductance of skeletal muscle suggests that most of the chloride channels must be located in the transverse tubular system.     

Inactivation of batrachotoxin-modified Na+ channels in GH3 cells. Characterization and pharmacological modification

Batrachotoxin (BTX)-modified Na+ currents were characterized in GH3 cells with a reversed Na+ gradient under whole-cell voltage clamp conditions. BTX shifts the threshold of Na+ channel activation by approximately 40 mV in the hyperpolarizing direction and nearly eliminates the declining phase of Na+ currents at all voltages, suggesting that Na+ channel inactivation is removed. Paradoxically, the steady-state inactivation (h infinity) of BTX-modified Na+ channels as determined by a two-pulse protocol shows that inactivation is still present and occurs maximally near -70 mV. About 45% of BTX-modified Na+ channels are inactivated at this voltage. The development of inactivation follows a sum of two exponential functions with tau d(fast) = 10 ms and tau d(slow) = 125 ms at -70 mV. Recovery from inactivation can be achieved after hyperpolarizing the membrane to voltages more negative than -120 mV. The time course of recovery is best described by a sum of two exponentials with tau r(fast) = 6.0 ms and tau r(slow) = 240 ms at -170 mV. After reaching a minimum at -70 mV, the h infinity curve of BTX-modified Na+ channels turns upward to reach a constant plateau value of approximately 0.9 at voltages above 0 mV. Evidently, the inactivated, BTX-modified Na+ channels can be forced open at more positive potentials. The reopening kinetics of the inactivated channels follows a single exponential with a time constant of 160 ms at +50 mV. Both chloramine-T (at 0.5 mM) and alpha-scorpion toxin (at 200 nM) diminish the inactivation of BTX-modified Na+ channels. In contrast, benzocaine at 1 mM drastically enhances the inactivation of BTX-modified Na+ channels. The h infinity curve reaches minimum of less than 0.1 at -70 mV, indicating that benzocaine binds preferentially with inactivated, BTX-modified Na+ channels. Together, these results imply that BTX-modified Na+ channels are governed by an inactivation process.     

Comparative effects of deficit irrigation and alternate partial root-zone irrigation on xylem pH, ABA and ionic concentrations in tomatoes

Comparative effects of partial root-zone irrigation (PRI) and deficit irrigation (DI) on xylem pH, ABA, and ionic concentrations of tomato (Lycopersicon esculentum L.) plants were investigated in two split-root pot experiments. Results showed that PRI plants had similar or significantly higher xylem pH, which was increased by 0.2 units relative to DI plants. Nitrate and total ionic concentrations (cations+anions), and the proportion of cations influenced xylem pH such that xylem pH increases as nitrate and total ionic concentrations decrease, and the proportion of cations increases. In most cases, the xylem ABA concentration was similar for PRI and DI plants, and a clear association between increases in xylem pH with increasing xylem ABA concentration was only found when the soil water content was relatively low. The concentrations of anions, cations, and the sum of anions and cations in PRI were higher than in the DI treatment when soil water content was relatively high in the wetted soil compartment. However, when water content in both soil compartments of the PRI pots were very low before the next irrigation, the acquisition of nutrients by roots was reduced, resulting in lower concentrations of anions and cations in the PRI than in the DI treatment. It is therefore essential that the soil water content in the wet zone should be maintained relatively high while that in the drying soil zone should not be very low, both conditions are crucial to maintain high soil and plant water status while sustaining ABA signalling of the plants.     

Origins of the Electrical Potential Difference between the Xylem Sap of Maize Roots and the External Solution

The effects of 2,4-dinitrophenol, of changes in the temperatureand concentration of the ambient solution and of variationsin salt status on the electrical potential difference betweenthe xylem exudate of maize roots and the ambient solution havebeen examined. The results are discussed in the light of someof the factors which could give rise to a potential differencebetween the sap and the solution. The rapid response of thepotential difference to dinitrophenol and to changes in temperaturesuggest that, at least in part, it arises directly from metabolicprocesses. Rapid changes in the potential difference broughtabout by addition of salts may be attributed to differentialrates of movement of anions and cations in the initial uptakeprocess. Over longer periods the potential difference appearsto be dependent on the concentration, but not the compositionof the ambient solution, and on the salt status of the roots.The salt status influences the relative rates at which anionsand cations are transported to the xylem sap, and a correlationhas been found between the potential difference and the ratioof the rates of movement of chloride or sulphate to potassiumto the sap. The implications of these findings on the elucidationof the pathways whereby ions are transported to the sap arediscussed.