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D C Eaton

Publications and source records attributed to D C Eaton.

At least 73 records · Page 4Linked to original sources
PubMed1992

Inhibition of apical Na+ channels in rabbit cortical collecting tubules by basolateral prostaglandin E2 is modulated by protein kinase C.

UNLABELLED: We used the cell-attached patch clamp technique to investigate the interaction of exogenous prostaglandins (PG), intracellular [Ca2+]i, and protein kinase C (PKC) on the high selectivity, 4 pS Na+ channel found in the principal cell apical membrane of rabbit cortical collecting tubule (CCT) cultures grown on collagen supports with 1.5 microM aldosterone. Application of 0.5 microM PGE2 to the basolateral membrane decreased mean NP0 (number of channels times the open probability) for apical Na+ channels by 46.5% (n = 9). There was no consistent change in NP0 after apical 0.5 microM PGE2 (n = 12) or after apical or basolateral 0.5 microM PGF2 alpha (n = 8). Release of [Ca2+]i stores with 0.25 microM thapsigargin (n = 7), or activation of apical membrane PKC with apical 0.1 microM 4 beta-phorbol-12-myristate-13-acetate (n = 5) or 10 microM 1-oleyl-2-acetylglycerol (n = 4) also decreased NP0. Depletion of [Ca2+]i stores (0.25 microM thapsigargin pretreatment) (n = 7) or inhibition of apical PKC (100 microM D-sphingosine pretreatment) (n = 8) abolished the inhibitory effects of basolateral PGE2. CONCLUSIONS: (a) apical Na+ transport in rabbit CCT principal cells is modulated by basolateral PGE2; (b) the mechanism involves release of IP3-sensitive, [Ca2+]i stores; and (c) Ca(2+)-dependent activation of apical membrane PKC, which then inhibits apical Na+ channels.

Animals↗
PubMed1991

Cyclic GMP-activated channel activity in renal epithelial cells (A6).

We studied the effects of guanosine 3',5'-cyclic monophosphate (cGMP) and nitroprusside on ion channels in the apical membrane of confluent A6 cells (a distal nephron cell line) cultured on permeable supports for 10-14 days using patch clamp techniques. In cell-attached patches without any detectable channel activity, activity of a non-selective cation channel with a single-channel conductance of 1 pS was observed after adding nitroprusside. After adding cGMP to the cytosolic surface of inside-out patches with no detectable channel activity, we observed single channel activity similar to the channel observed after adding nitroprusside. These observations imply that nitroprusside activates a non-selective cation channel with small single channel conductance (1 pS) via an increase in cGMP which activates the channel.

Cell Membrane↗
PubMed1991

Potassium permeable channels in primary cultures of rabbit cortical collecting tubule.

Rabbit cortical collecting tubule (RCCT) primary cultures, were grown on permeable, collagen supports with 1.5 microM aldosterone. Single K+ permeable channels in principal cell apical membranes were examined. At applied patch pipette potential (Vapp) from -60 to +60 mV (cell interior with respect to pipette interior), outward currents (cell to pipette) with a unitary conductance of 8 to 10 pS were seen in cell-attached (N = 31) and excised inside-out (N = 15) patches. At resting membrane potential (Vapp = 0 mV), mean open probability (Po = 0.85 +/- 0.16) decreased by 50% with 0.75 mM luminal BaCl2 exposure. In cell-attached patches, a second type of outward current was seen only at extreme depolarization, Vapp greater than +80 mV (N = 9). Usually in the closed state (Po less than 0.0005) at no applied potential, Po for this 150 pS channel increased dramatically with depolarization and/or raising cytoplasmic Ca2+. With a calculated K+ equilibrium potential of -84 mV, excised patch reversal potentials were less than -50 mV for both the above channel types, indicating high selectivity for K+ over Na+. In cultures grown without aldosterone low conductance K+ channels were rarely observed, while mineralocorticoid status did not appear to affect high conductance K+ channel frequency. Finally, a 30 pS cation channel was found to be nonselective for K+ over Na+, and insensitive to voltage, intracellular Ca2+ or luminal Ba2+. We conclude that: 1) Principal cell apical membranes from aldosterone-stimulated, RCCT primary cultures contain (a) low conductance, Ba(2+)-inhibitable and (b) high conductance, Ca2+/voltage-dependent K+ channels; and c) nonselective cation channels. 2) The low conductance K+ channel may play an important physiologic role in native RCCT mineralocorticoid-controlled K+ secretion, while the latter two channels' functions are unknown, although similar channels have been suggested to play a role in cell volume regulation.

Aldosterone↗
PubMed1991

Effects of vasopressin and cAMP on single amiloride-blockable Na channels.

To determine the mechanism by which vasopressin increases sodium transport in sodium-transporting, tight epithelia, we examined single amiloride-blockable Na channels in membrane patches from cultured distal nephron cells (A6) either before or after treatment with arginine vasopressin. Pretreatment of cells with vasopressin (40 mU/ml) for 40-50 min increases NPo (N, the number of Na channels; Po, the open probability of an individual Na channel). The increase in NPo is due to an increase in the number of conductive Na channels with little or no change in the open probability of individual Na channels. Pretreatment of cells for 1 h with 1 mM N6,2'-O-dibutyryladenosine 3', 5'-cyclic monophosphate (DBcAMP) also increased NPo. The increase in NPo caused by DBcAMP pretreatment is also due to the increase in the number of conductive Na channels with no change in the open probability of individual Na channels. Cells pretreated with cholera toxin (CTX; 250 ng/ml) for 4 h appeared similar to cells that had been treated with vasopressin or DBcAMP; that is, the number of Na channels per patch increased with little or no effect on the open probability of individual Na channels. For patches from many untreated cells, when the frequency of occurrence is plotted against the number of channels in an individual patch, the histogram consists of a single peak with a number of channels per patch of 2.0 +/- 1.5 (+/- SD, 126 patches). After pretreatment of cells with vasopressin, DBcAMP, or CTX, the same histogram contains two peaks after vasopressin of 1.8 +/- 1.2 and 9.2 +/- 1.5 (+/- SD, 38 and 53 patches, respectively). These observations suggest that pretreatment of cells with vasopressin, DBcAMP, or CTX may act by promoting insertion of clusters of new sodium channels.

Amiloride↗
PubMed1991

cAMP-induced potassium channel activity in apical membrane of cultured A6 kidney cells.

In the present study, we report an adenosine 3',5'-cyclic monophosphate (cAMP)-induced potassium channel in the apical membrane of cultured A6 kidney cells grown on impermeable supports. The channel is present in approximately 10% of untreated cell-attached patches. After treatment with 1 mM dibutyryl-cAMP, the channel is present in greater than 70% of the same patches. The characteristics of this channel are 1) the channel is highly selective for potassium; 2) the channel has a unit conductance of 13 +/- 2 pS; 3) the probability of a channel opening increases in the presence of membrane permeable analogues of cAMP and with increasing depolarization of the cell interior; 4) channels are blocked by Ba2+; 5) the channel loses activity rapidly in excised patches; and 6) the channel has at least one open and two closed states. The mean open time is 3.5 +/- 1.0 ms, whereas the mean durations of the closed states are 3.2 +/- 1.4 and 29.4 +/- 3.4 ms. The channels could mediate potassium secretion in A6 cells, if the channels are normally present under transporting conditions; however, surface expression of the channels appears to depend on growth substrate and the state of cellular differentiation, since the channels are not observed in cells grown on permeable supports.

Barium↗
PubMed1991

Amiloride-sensitive sodium channels in rabbit cortical collecting tubule primary cultures.

Patch-clamp methodology was applied to principal cell apical membranes of rabbit cortical collecting tubule (CCT) primary cultures grown on collagen supports in the presence of aldosterone (1.5 microM). The most frequently observed channel had a unit conductance of 3-5 pS, nonlinear current-voltage (I-V) relationship, Na permeability (PNa)-to-K permeability (PK) ratio greater than 19:1, and inward current at all applied potentials (Vapp) less than +80 mV (n = 41). Less frequently, an 8- to 10-pS channel with a linear I-V curve, PNa/PK less than 5:1, and inward current at Vapp less than +40 mV was also observed (n = 7). Luminal amiloride (0.75 microM) decreased the open probability (Po) for both of these channels. Mean open time for the high-selectivity Na+ channel was 2.1 +/- 0.5 s and for the low-selectivity Na+ channel was 50 +/- 12 ms. In primary cultures grown without aldosterone the high-selectivity Na+ channel was rarely observed (1 of 32 patches). Lastly, a 26- to 35-pS channel, nonselective for Na+ over K+, was not activated by cytoplasmic Ca2+ or voltage nor inhibited by amiloride (n = 17). We conclude that under specific growth conditions, namely permeable transporting supports and chronic mineralocorticoid hormone exposure, principal cell apical membranes of rabbit CCT primary cultures contain 1) both high-selectivity and low-selectivity, amiloride-inhibitable Na+ channels and 2) amiloride-insensitive, nonselective cation channels.

Aldosterone↗
PubMed1990

Regulation of the amiloride-blockable sodium channel from epithelial tissue.

The first step in net active transepithelial transport of sodium in tight epithelia is mediated by the amiloride-blockable sodium channel in the apical membrane. This sodium channel is the primary site for discretionary control of total body sodium and, therefore, investigating its regulatory mechanisms is important to our understanding of the physiology of fluid and electrolyte balance. Because essentially all of the regulatory sites on the channel are on the intracellular surface, patch clamp methods have proven extremely useful in the electrophysiological characterization of the sodium channel by isolating it from other channel proteins in the epithelial membrane and by allowing access to the intracellular surface of the protein. We have examined three different regulatory mechanisms. (1) Inhibition of channel activity by activation of protein kinase C; (2) activation of the channel by agents which activate G-proteins; and (3) modulation of channel kinetics and channel number by mineralocorticoids. Activation of protein kinase C by phorbol esters or synthetic diacylglycerols reduces the open probability of sodium channels. Protein kinase C can be activated in a physiological context by enhancing apical sodium entry. Actions which reduce sodium entry (low luminal sodium concentrations or the apical application of amiloride) increase channel open probability. The link between sodium entry and activation of protein kinase C appears to be mediated by intracellular calcium activity linked to sodium via a sodium/calcium exchange system. Thus, the intracellular sodium concentration is coupled to sodium entry in a negative feedback loop which promotes constant total entry of sodium. Activation of G-proteins by pertussis toxin greatly increases the open probability of sodium channels. Since channels can also be activated by pertussis toxin or GTP gamma S in excised patches, the G-protein appears to be closely linked in the apical membrane to the sodium channel protein itself. The mechanism for activation of this apical G-protein, when most hormonal and transmitter receptors are physically located on the basolateral membrane, is unclear. Mineralocorticoids such as aldosterone have at least two distinct effects. First, as expected, increasing levels of aldosterone increase the density of functional channels detectable in the apical membrane. Second, contrary to expectations, application of aldosterone increases the open probability of sodium channels. Thus aldosterone promotes the functional appearance of new sodium channels and promotes increased sodium entry through both new and pre-existant channels.

Aldosterone↗
PubMed1990

Effects of insulin and phosphatase on a Ca2(+)-dependent Cl- channel in a distal nephron cell line (A6).

A Cl- channel with a small single-channel conductance (3 pS) was observed in cell-attached patches formed on the apical membrane of cells from the distal nephron cell line (A6) cultured on permeable supports. The current-voltage (I-V) relationship from cell-attached patches or inside-out patches with 1 microM cytosolic Ca2+ strongly rectified with no inward current at potentials more negative than ECl. However, the rectification decreased (i.e., inward current increased) when the cytosolic Ca2+ concentration ([Ca2+]i) was increased above 1 microM. If [Ca2+]i is increased to 800 microM, the I-V relationship became linear. Besides the change in the I-V relationship, an increase in [Ca2+]i also increases the open probability of the channel. Regardless of the recording condition, the channel has one open and one closed state. Both closing and opening rates were dependent on [Ca2+]i; an increase of [Ca2+]i decreased the closing rate and increased the opening rate. The Ca2+ dependence of transition rates at positive membrane potentials (cell interior with respect to external surface) were much larger than the dependence at negative intracellular potentials. The I-V relationship of chloride channels in inside-out patches from cells pretreated with insulin was linear even with 1 microM [Ca2+]i, while channel currents from cells under similar conditions but without insulin still strongly rectified. Alkaline phosphatase applied to the intracellular surface of inside-out patches altered the outward rectification of single channels in a manner qualitatively similar to that of insulin pretreatment. These observations suggest that phosphorylation/dephosphorylation of the channel modulates the sensitivity of the Cl- channel to cytosolic Ca2+ and that insulin produces its effect by promoting dephosphorylation of the channel.

Animals↗
PubMed1990

Chloride channels in the apical membrane of a distal nephron A6 cell line.

In this report, single-channel recording methods were used to determine whether there are Cl- conductive pathways in the apical membrane of cultured renal distal nephron cells (A6). Two different types of single Cl- channels were observed. In cell-attached patches, one had a unit conductance of 3 pS, whereas the unit conductance of the other was 8 pS. In cell-attached patches, the currents associated with the 3-pS Cl- channel outwardly rectified, whereas the current voltage relationship for the 8-pS Cl-channel was linear. The 3-pS Cl- channel has one open and one closed state; the 8-pS Cl- channel has one open and two closed states. The open probability of the 3-pS Cl- channel was voltage dependent (increasing with depolarization of the membrane) but even at very depolarized potentials (+140 mV) remained small (always less than 0.1). On the other hand, the open probability of the 8-pS Cl- channel was large (approximately 0.8) and voltage independent. The closing rate of the 3-pS Cl- channel was decreased when the patch membrane was depolarized, whereas the opening rate was increased. In contrast, the closing rate of the 8-pS Cl- channel decreased with depolarization, but the opening rates were voltage independent. The outward rectification of the 3-pS channel was markedly reduced in inside-out patches when high calcium concentrations (10-800 microM) were present on the intracellular surface. The open probability of the 3-pS Cl- channel is increased by membrane permeable analogues of adenosine 3',5'-cyclic monophosphate primarily by decreasing the mean closed time.

Animals↗
PubMed1989

Expression of amiloride-blockable sodium channels in Xenopus oocytes.

This report describes the expression of a sodium-selective, amiloride-blockable conductance in Xenopus oocytes that have been injected with RNA prepared from a distal nephron cell line (A6). After injecting the RNA into mature oocytes (stage V or VI) and incubating the oocytes for 2-4 days, the oocytes were examined for amiloride-blockable current. The RNA induced a substantial amiloride-blockable current. Uninjected or water-injected oocytes had no measurable amiloride-blockable current. RNA prepared from aldosterone-treated A6 cells was much more effective in inducing amiloride-blockable sodium current than RNA prepared from aldosterone-depleted A6 cells. Oocytes injected with RNA prepared from mineralocorticoid-depleted cells appeared very similar to water-injected oocytes. The amiloride-blockable current in oocytes has a reversal potential of approximately +50 - +60 mV, which varies 61 mV/decade change in external sodium concentration, suggesting that the current is highly selective for sodium over other ions. In addition, the concentration of amiloride that produces half block of the current is 48 +/- 8 nM. Thus the current expressed in oocytes appears very similar to sodium-selective currents observed from the apical membranes of various tight epithelial tissues.

Amiloride↗
PubMed1989

Effects of luminal Na+ on single Na+ channels in A6 cells, a regulatory role for protein kinase C.

UNLABELLED: Na+ "self-inhibition" in tight epithelia describes the reduction in apical Na+ permeability observed with increasing luminal Na+ concentration. Patch clamp was used to examine regulation of self-inhibition at the level of single Na+ channels. After cell-attached patches (pipette solution, 129 mM NaCl) were obtained on amphibian distal nephron cells (A6), the 129 mM NaCl (high Na+) apical bath outside of the patch was replaced with 3 mM NaCl (low Na+). Within minutes there was an increase in open channel probability (Po) and the appearance of one to five "new" channels in patch membranes. A similar increase occurred when apical Na+ entry was blocked by luminal amiloride (10 microM). A23187 (1 microM), a calcium ionophore, added after low Na+ exchange, abolished the rise in channel activity. Increased Po and new channels, induced by either luminal Na+ or amiloride, were also reversed by either 4B-phorbol 12-myristate 13-acetate (PMA; 0.1 microM) or 1-oleyl-2-acetyl glycerol (OAG; 10 microM) over 15-30 min. 4 alpha-Phorbol (0.1 microM), an inactive phorbol, did not reduce channel activity. D-Sphingosine (100 microM), a protein kinase C (PKC) inhibitor, increased Po and new channels. CONCLUSIONS: 1) modulation of apical Na+ permeability by luminal Na+ does not require direct interaction of Na+ with the channel protein but, rather, appears to involve an intracellular regulatory pathway, 2) relieving self-inhibition alters both the number and kinetics of single Na+ channels, 3) the effect of low Na+ must be modulated via decreased apical Na+ entry and intracellular Na+, since amiloride yielded similar results, 4) changes in intracellular Na+ probably affect Na+ channel activity via cytosolic Ca2+, 5) the effects of decreasing luminal Na+ are reversed by PKC activators and mimicked by PKC inhibitors suggesting a possible role for PKC in Na+ self-inhibition.

Amiloride↗
PubMed1988

Cytomegalovirus: sodium entry and development of cytomegaly in human fibroblasts.

A possible relationship between net Na+ entry and the development of CMV-induced cytomegaly (cell enlargement) was investigated in human fibroblasts derived from skin-muscle and thyroid tissue. We found that inhibiting cellular Na+ uptake, either by pharmacological means (amiloride, an inhibitor of Na+/H+ exchange) or by replacement of extracellular Na+ (by N-methyl-D-glucamine or choline), inhibited the development of cytomegaly. Furthermore, we noted a temporal parallelism between the development of cytomegaly and enhancement of ouabain-sensitive (O-S) 86Rb+ uptake. O-S 86Rb+ uptake is a monitor for the activity of the sodium pump resident in the plasmalemma of the fibroblasts. The enhanced O-S 86Rb+ uptake reflects either an increased intracellular Na+ concentration or an increased number of sodium pump complexes per fibroblast. Amiloride inhibited the enhancement of O-S 86Rb+ uptake, as well as cytomegaly development. Addition of amiloride at selected times after infection suggested that the same phase of virus replication was sensitive to the inhibitory effect of this drug on the enhancement of O-S 86Rb+ uptake and on the development of cytomegaly. There was also a similar pattern of inhibition of O-S 86Rb+ uptake and cytomegaly with increasing concentrations of amiloride. Thus, there may be a relationship between CMV-induced Na+ entry through activation of the Na+/H+ exchanger and development of cytomegaly.

Amiloride↗
PubMed1987

Inhibition of sodium currents by local anesthetics in chloramine-T-treated squid axons. The role of channel activation.

In order to test the requirement of Na channel inactivation for the action of local anesthetics, we investigated the inhibitory effects of quaternary and tertiary amine anesthetics on normally inactivating and noninactivating Na currents in squid axons under voltage clamp. Either the enzymatic mixture pronase, or chloramine-T (CT), a noncleaving, oxidizing reagent, was used to abolish Na channel inactivation. We found that both the local anesthetics QX-314 and etidocaine, when perfused internally at 1 mM, elicited a "tonic" (resting) block of Na currents, a "time-dependent" block that increased during single depolarizations, and a "use-dependent" (phasic) block that accumulated as a result of repetitive depolarizations. All three effects occurred in both control and CT-treated axons. As in previous reports, little time-dependent or phasic block by QX-314 appeared in pronase-treated axons, although tonic block remained. Time-dependent block was greatest and fastest at large depolarizations (Em greater than +60 mV) for both the control and CT-treated axons. The recovery kinetics from phasic block were the same in control and CT-modified axons. The voltage dependence of the steady state phasic block in CT-treated axons differed from that in the controls; an 8-10% reduction of the maximum phasic block and a steepening and shift of the voltage dependence in the hyperpolarizing direction resulted from CT treatment. The results show that these anesthetics can bind rapidly to open Na channels in a voltage-dependent manner, with no requirement for fast inactivation. We propose that the rapid phasic blocking reactions in nerve are consequences primarily of channel activation, mediated by binding of anesthetics to open channels, and that the voltage dependence of phasic block arises directly from that of channel activation.

Anesthetics, Local↗
PubMed1986

Effects of saxitoxin analogues and ligand competition on sodium currents of squid axons.

Saxitoxin (STX) and several STX analogues from dinoflagellates (genus Protogonyaulax) block sodium conductance in squid giant axons with variable potencies. Toxins, analyzed under voltage clamp, are 21-sulfosaxitoxin, 21-sulfosaxitoxin 11 alpha-hydroxysulfate, 21-sulfosaxitoxin 11 beta-hydroxysulfate, (B1, C1, C2, respectively) and gonyautoxins 2 and 3. The potency sequence for the toxins examined is STX greater than gonyautoxin 3 greater than B1 greater than C2 greater than gonyautoxin 2 much greater than C1. Guanidine, when substituted for sodium in external seawater, reduced the potency of STX to block inward current but did not affect tetrodotoxin activity. Methylguanidine also reduced the ability of STX to block outward sodium current. Inhibitory constants for guanidine and methylguanidine were 116 and 187 mM, respectively. Competition can be explained by binding at or near the toxin binding site but not by surface potential alteration.

Amphibian Proteins↗
PubMed1986

ATP-dependent proton transport in human renal medulla.

An electrogenic proton-translocating ATPase (H+-ATPase) has been described in turtle urinary bladder and bovine and rat renal medulla. In the present study, a membrane fraction with ATP-dependent H+ transport activity was isolated from human renal medulla. Intravesicular acidification was assessed by acridine orange absorbance changes. Proton transport was abolished by N-ethylmaleimide but not oligomycin or vanadate, differentiating this H+-ATPase from mitochondrial F0-F1 H+-ATPase and gastric H+-K+-ATPase. In addition, vesicular proton uptake was demonstrated to be independent of sodium and potassium cotransport. Proton translocation rate increased when transmembrane potential was clamped with valinomycin supporting an electrogenic mechanism. Hydrogen ion transport was dependent on the presence of chloride or bromide, since substitution by fluoride or nitrate markedly decreased intravesicular acidification. The transport characteristics of this proton-translocating ATPase are similar to those described for turtle urinary bladder and bovine and rat renal medulla, which have been assumed to play a role in urinary acidification by the medullary collecting duct.

Acridine Orange↗
PubMed1986

Single-channel recordings from two types of amiloride-sensitive epithelial Na+ channels.

We report here the first evidence in intact epithelial cells of unit conductance events from amiloride-sensitive Na+ channels. The events were observed when patch-clamp recordings were made from the apical surface of cultured epithelial kidney cells (A6). Two types of channels were observed: one with a high selectivity to Na+ and one with relatively low selectivity. The characteristics of the low-selectivity channel are as follows: single-channel conductance ranged between 7 and 10 pS (mean = 8.4 +/- 1.3), the current-voltage (I-V) relationship displayed little if any nonlinearity over a range of +/- 80 mV (with respect to the patch pipette) and the channel Na+/K+ selectivity was approximately 3-4:1. Amiloride, a cationic blocker of the channel, reduced channel mean open time and increased channel mean closed times as the voltage of the cell interior was made more negative. Amiloride induced channel flickering at increased negative potentials (intracellular potential with respect to the patch) but did not alter the single-channel conductance or the I-V relationship from that observed in control patches. The characteristics of the high-selectivity channel are: a single-channel conductance of 1-3 pS (mean = 2.8 +/- 1.2), the current-voltage relationship is markedly nonlinear with a Na+/K+ selectivity greater than 20:1. The mean open and closed times for the two types of channels are quite different, the high-selectivity channel being open only about 10% of the time while the low-selectivity channel is open about 30% of the time.

Amiloride↗
PubMed1986

Regulation of single sodium channels in renal tissue: a role in sodium homeostasis.

The kidney is responsible for the maintenance of an organism's body solute and water balance (i.e., Na+ homeostasis). The distal nephron and the cortical collecting duct (CCD) (an example of a tight epithelium) are important sites of regulatory control over the rate of Na+ reabsorption. The Na+ channel, a specialized protein located in the apical membrane of CCD cells, is the specific site of transepithelial Na+ movement. Na+ entry into the cell across the apical membrane occurs by passive diffusion of Na+ down an electrochemical gradient. We have used the patch-voltage clamp method to examine single-channel conductance events of the amiloride-sensitive apical Na+ channel in A6 cells, a model of CCD. Two types of Na+ channel were identified. One type was characterized by low selectivity (Na+ to K+) and high conductance, the other by high selectivity and low conductance. The type and frequency of channel observed depended on the transporting state of the epithelium. In a tissue with poor transport rates, the low-selectivity type of channel was prevalent (the other type of channel was present, but in a very low density). Therefore, the poorly transporting tissue had an overall low apical Na+ conductance. In a tissue with high transport rates, the highly selective channel appeared to be predominant. In this case the net result was a highly Na+ conductive apical membrane.

Biological Transport↗