Fatigue depresses maximal in vitro skeletal muscle Na+-K+-ATPase activity in untrained and trained individuals

2002 ◽  
Vol 93 (5) ◽  
pp. 1650-1659 ◽  
Author(s):  
Steve F. Fraser ◽  
Jia L. Li ◽  
Michael F. Carey ◽  
Xiao N. Wang ◽  
Termboon Sangkabutra ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Phosphatase Activity ◽  
Important Determinant ◽  
Vastus Lateralis ◽  
Ouabain Binding ◽  
Isokinetic Contractions ◽  
Lower Ratio ◽  
Muscle Biopsies ◽  
Training State

This study investigated whether fatiguing dynamic exercise depresses maximal in vitro Na+-K+-ATPase activity and whether any depression is attenuated with chronic training. Eight untrained (UT), eight resistance-trained (RT), and eight endurance-trained (ET) subjects performed a quadriceps fatigue test, comprising 50 maximal isokinetic contractions (180°/s, 0.5 Hz). Muscle biopsies (vastus lateralis) were taken before and immediately after exercise and were analyzed for maximal in vitro Na+-K+-ATPase (K+-stimulated 3- O-methylfluoroscein phosphatase) activity. Resting samples were analyzed for [3H]ouabain binding site content, which was 16.6 and 18.3% higher ( P < 0.05) in ET than RT and UT, respectively (UT 311 ± 41, RT 302 ± 52, ET 357 ± 29 pmol/g wet wt). 3- O-methylfluoroscein phosphatase activity was depressed at fatigue by −13.8 ± 4.1% ( P < 0.05), with no differences between groups (UT −13 ± 4, RT −9 ± 6, ET −22 ± 6%). During incremental exercise, ET had a lower ratio of rise in plasma K+ concentration to work than UT ( P < 0.05) and tended ( P = 0.09) to be lower than RT (UT 18.5 ± 2.3, RT 16.2 ± 2.2, ET 11.8 ± 0.4 nmol · l−1 · J−1). In conclusion, maximal in vitro Na+-K+-ATPase activity was depressed with fatigue, regardless of training state, suggesting that this may be an important determinant of fatigue.

Chronic intermittent hypoxia and incremental cycling exercise independently depress muscle in vitro maximal Na+-K+-ATPase activity in well-trained athletes

2005 ◽  
Vol 98 (1) ◽  
pp. 186-192 ◽  
Author(s):  
R. J. Aughey ◽  
C. J. Gore ◽  
A. G. Hahn ◽  
A. P. Garnham ◽  
S. A. Clark ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Vastus Lateralis ◽  
Incremental Exercise ◽  
Peak Oxygen Consumption ◽  
Vastus Lateralis Muscle ◽  
Minor Effect ◽  
Moderate Altitude ◽  
Ouabain Binding ◽  
Before And After

Athletes commonly attempt to enhance performance by training in normoxia but sleeping in hypoxia [live high and train low (LHTL)]. However, chronic hypoxia reduces muscle Na+-K+-ATPase content, whereas fatiguing contractions reduce Na+-K+-ATPase activity, which each may impair performance. We examined whether LHTL and intense exercise would decrease muscle Na+-K+-ATPase activity and whether these effects would be additive and sufficient to impair performance or plasma K+ regulation. Thirteen subjects were randomly assigned to two fitness-matched groups, LHTL ( n = 6) or control (Con, n = 7). LHTL slept at simulated moderate altitude (3,000 m, inspired O2 fraction = 15.48%) for 23 nights and lived and trained by day under normoxic conditions in Canberra (altitude ∼600 m). Con lived, trained, and slept in normoxia. A standardized incremental exercise test was conducted before and after LHTL. A vastus lateralis muscle biopsy was taken at rest and after exercise, before and after LHTL or Con, and analyzed for maximal Na+-K+-ATPase activity [K+-stimulated 3- O-methylfluorescein phosphatase (3- O-MFPase)] and Na+-K+-ATPase content ([3H]ouabain binding sites). 3- O-MFPase activity was decreased by −2.9 ± 2.6% in LHTL ( P < 0.05) and was depressed immediately after exercise ( P < 0.05) similarly in Con and LHTL (−13.0 ± 3.2 and −11.8 ± 1.5%, respectively). Plasma K+ concentration during exercise was unchanged by LHTL; [3H]ouabain binding was unchanged with LHTL or exercise. Peak oxygen consumption was reduced in LHTL ( P < 0.05) but not in Con, whereas exercise work was unchanged in either group. Thus LHTL had a minor effect on, and incremental exercise reduced, Na+-K+-ATPase activity. However, the small LHTL-induced depression of 3- O-MFPase activity was insufficient to adversely affect either K+ regulation or total work performed.

Glucose supplements increase human muscle in vitro Na+-K+-ATPase activity during prolonged exercise

2007 ◽  
Vol 293 (1) ◽  
pp. R354-R362 ◽  
Author(s):  
H. J. Green ◽  
T. A. Duhamel ◽  
K. P. Foley ◽  
J. Ouyang ◽  
I. C. Smith ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Prolonged Exercise ◽  
Serum Insulin ◽  
Vastus Lateralis ◽  
Oral Glucose ◽  
Vastus Lateralis Muscle ◽  
Ouabain Binding ◽  
Similar Time ◽  
Phosphatase Assay

Regulation of maximal Na+-K+-ATPase activity in vastus lateralis muscle was investigated in response to prolonged exercise with (G) and without (NG) oral glucose supplements. Fifteen untrained volunteers (14 males and 1 female) with a peak aerobic power (V̇o2peak) of 44.8 ± 1.9 ml·kg−1·min−1; mean ± SE cycled at ∼57% V̇o2peak to fatigue during both NG (artificial sweeteners) and G (6.13 ± 0.09% glucose) in randomized order. Consumption of beverage began at 30 min and continued every 15 min until fatigue. Time to fatigue was increased ( P < 0.05) in G compared with NG (137 ± 7 vs. 115 ± 6 min). Maximal Na+-K+-ATPase activity (Vmax) as measured by the 3- O-methylfluorescein phosphatase assay (nmol·mg−1·h−1) was not different between conditions prior to exercise (85.2 ± 3.3 or 86.0 ± 3.9), at 30 min (91.4 ± 4.7 vs. 91.9 ± 4.1) and at fatigue (92.8 ± 4.3 vs. 100 ± 5.0) but was higher ( P < 0.05) in G at 90 min (86.7 ± 4.2 vs. 109 ± 4.1). Na+-K+-ATPase content (βmax) measured by the vanadate facilitated [3H]ouabain-binding technique (pmol/g wet wt) although elevated ( P < 0.05) by exercise (0<30, 90, and fatigue) was not different between NG and G. At 60 and 90 min of exercise, blood glucose was higher ( P < 0.05) in G compared with NG. The G condition also resulted in higher ( P < 0.05) serum insulin at similar time points to glucose and lower ( P < 0.05) plasma epinephrine and norepinephrine at 90 min of exercise and at fatigue. These results suggest that G results in an increase in Vmax by mechanisms that are unclear.

Impaired muscle Ca2+ and K+ regulation contribute to poor exercise performance post-lung transplantation

2003 ◽  
Vol 95 (4) ◽  
pp. 1606-1616 ◽  
Author(s):  
Michael J. McKenna ◽  
Steve F. Fraser ◽  
Jia L. Li ◽  
Xiao N. Wang ◽  
Michael F. Carey ◽  
...  
Keyword(s):  
Oxygen Consumption ◽  
Atpase Activity ◽  
Phosphatase Activity ◽  
Vastus Lateralis ◽  
Buffering Capacity ◽  
Peak Oxygen Consumption ◽  
Vastus Lateralis Muscle ◽  
Ouabain Binding ◽  
Potassium Regulation ◽  
Lung Transplant Recipients

Lung transplant recipients (LTx) exhibit marked peripheral limitations to exercise. We investigated whether skeletal muscle Ca2+ and K+ regulation might be abnormal in eight LTx and eight healthy controls. Peak oxygen consumption and arterialized venous plasma [K+] (where brackets denote concentration) were measured during incremental exercise. Vastus lateralis muscle was biopsied at rest and analyzed for sarcoplasmic reticulum Ca2+ release, Ca2+ uptake, and Ca2+-ATPase activity rates; fiber composition; Na+-K+-ATPase (K+-stimulated 3- O-methylfluorescein phosphatase) activity and content ([3H]ouabain binding sites); as well as for [H+] and H+-buffering capacity. Peak oxygen consumption was 47% less in LTx ( P < 0.05). LTx had lower Ca2+ release (34%), Ca2+ uptake (31%), and Ca2+-ATPase activity (25%) than controls ( P < 0.05), despite their higher type II fiber proportion (LTx, 75.0 ± 5.8%; controls, 43.5 ± 2.1%). Muscle [H+] was elevated in LTx ( P < 0.01), but buffering capacity was similar to controls. Muscle 3- O-methylfluorescein phosphatase activity was 31% higher in LTx ( P < 0.05), but [3H]ouabain binding content did not differ significantly. However, during exercise, the rise in plasma [K+]-to-work ratio was 2.6-fold greater in LTx ( P < 0.05), indicating impaired K+ regulation. Thus grossly subnormal muscle calcium regulation, with impaired potassium regulation, may contribute to poor muscular performance in LTx.

Effects of prior exercise and a low-carbohydrate diet on muscle sarcoplasmic reticulum function during cycling in women

2006 ◽  
Vol 101 (3) ◽  
pp. 695-706 ◽  
Author(s):  
T. A. Duhamel ◽  
H. J. Green ◽  
J. G. Perco ◽  
J. Ouyang
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Vastus Lateralis ◽  
Phase 1 ◽  
Vastus Lateralis Muscle ◽  
Low Carbohydrate Diet ◽  
Hill Slope ◽  
Low Carbohydrate ◽  
Exercise Induced

The effects of exercise and diet on sarcoplasmic reticulum Ca2+-cycling properties in female vastus lateralis muscle were investigated in two groups of women following four different conditions. The conditions were 4 days of a low-carbohydrate (Lo CHO) and glycogen-depleting exercise plus a Lo CHO diet (Ex + Lo CHO) ( experiment 2) and 4 days of normal CHO (Norm CHO) and glycogen-depleting exercise plus Norm CHO (Ex + Norm CHO) ( experiment 1). Peak aerobic power (V̇o2peak) was 38.1 ± 1.4 (SE); n = 9 and 35.6 ± 1.4 ml·kg−1·min−1; n = 9, respectively. Sarcoplasmic reticulum properties measured in vitro in homogenates (μmol·g protein−1·min−1) indicated exercise-induced reductions ( P < 0.05) in maximal Ca2+-ATPase activity (0 > 30, 60 min > fatigue), Ca2+ uptake (0 > 30 > 60 min, fatigue), and Ca2+ release, both phase 1 (0, 30 > 60 min, fatigue) and phase 2 (0 > 30, 60 min, fatigue; 30 min > fatigue) in Norm CHO. Exercise was without effect in altering the Hill slope ( nH), defined as the slope of relationship between Ca2+-ATPase activity and Ca2+ concentration. No differences were observed between Norm CHO and Ex+Norm CHO. Compared with Norm CHO, Lo CHO resulted in a lower ( P < 0.05) Ca2+ uptake, phase 1 Ca2+ release (30 min), and nH. Ex + Lo CHO resulted in a greater ( P < 0.05) Ca2+ uptake and nH compared with Lo CHO. The results demonstrate that Lo CHO alone can disrupt SR Ca2+ cycling and that, with the exception of Ca2+ release, a glycogen-depleting session of exercise before Lo CHO can reverse the effects.

Depressed Na+-K+-ATPase activity in skeletal muscle at fatigue is correlated with increased Na+-K+-ATPase mRNA expression following intense exercise

2005 ◽  
Vol 289 (1) ◽  
pp. R266-R274 ◽  
Author(s):  
A. C. Petersen ◽  
K. T. Murphy ◽  
R. J. Snow ◽  
J. A. Leppik ◽  
R. J. Aughey ◽  
...  
Keyword(s):  
Gene Expression ◽  
Atpase Activity ◽  
Mrna Expression ◽  
Binding Sites ◽  
Time Course ◽  
Acute Exercise ◽  
Vastus Lateralis ◽  
Vastus Lateralis Muscle ◽  
Ouabain Binding ◽  
Atpase Gene

We investigated whether depressed muscle Na+-K+-ATPase activity with exercise reflected a loss of Na+-K+-ATPase units, the time course of its recovery postexercise, and whether this depressed activity was related to increased Na+-K+-ATPase isoform gene expression. Fifteen subjects performed fatiguing, knee extensor exercise at ∼40% maximal work output per contraction. A vastus lateralis muscle biopsy was taken at rest, fatigue, 3 h, and 24 h postexercise and analyzed for maximal Na+-K+-ATPase activity via 3- O-methylfluorescein phosphatase (3- O-MFPase) activity, Na+-K+-ATPase content via [3H]ouabain binding sites, and Na+-K+-ATPase α1-, α2-, α3-, β1-, β2- and β3-isoform mRNA expression by real-time RT-PCR. Exercise [352 (SD 267) s] did not affect [3H]ouabain binding sites but decreased 3- O-MFPase activity by 10.7 (SD 8)% ( P < 0.05), which had recovered by 3 h postexercise, without further change at 24 h. Exercise elevated α1-isoform mRNA by 1.5-fold at fatigue ( P < 0.05). This increase was inversely correlated with the percent change in 3- O-MFPase activity from rest to fatigue (%Δ3- O-MFPaserest-fatigue) ( r = −0.60, P < 0.05). The average postexercise (fatigue, 3 h, 24 h) α1-isoform mRNA was increased 1.4-fold ( P < 0.05) and approached a significant inverse correlation with %Δ3- O-MFPaserest-fatigue ( r = −0.56, P = 0.08). Exercise elevated α2-isoform mRNA at fatigue 2.5-fold ( P < 0.05), which was inversely correlated with %Δ3- O-MFPaserest-fatigue ( r = −0.60, P = 0.05). The average postexercise α2-isoform mRNA was increased 2.2-fold ( P < 0.05) and was inversely correlated with the %Δ3- O-MFPaserest-fatigue ( r = −0.68, P < 0.05). Nonsignificant correlations were found between %Δ3- O-MFPaserest-fatigue and other isoforms. Thus acute exercise transiently decreased Na+-K+-ATPase activity, which was correlated with increased Na+-K+-ATPase gene expression. This suggests a possible signal-transduction role for depressed muscle Na+-K+-ATPase activity with exercise.

Inactivation of human muscle Na+-K+-ATPase in vitro during prolonged exercise is increased with hypoxia

2004 ◽  
Vol 96 (5) ◽  
pp. 1767-1775 ◽  
Author(s):  
S. D. Sandiford ◽  
H. J. Green ◽  
T. A. Duhamel ◽  
J. G. Perco ◽  
J. D. Schertzer ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Prolonged Exercise ◽  
Vastus Lateralis ◽  
Neuromuscular Fatigue ◽  
Peak Oxygen Consumption ◽  
Membrane Excitability ◽  
M Wave ◽  
Oxygen Fraction ◽  
Inspired Oxygen

This study investigated the effects of prolonged exercise performed in normoxia (N) and hypoxia (H) on neuromuscular fatigue, membrane excitability, and Na+-K+-ATPase activity in working muscle. Ten untrained volunteers [peak oxygen consumption (VV̇o2 peak) = 42.1 ± 2.8 (SE) ml·kg-1·min-1] performed 90 min of cycling during N (inspired oxygen fraction = 0.21) and during H (inspired oxygen fraction = 0.14) at ∼50% of normoxic VV̇o2 peak. During N, 3- O-methylfluorescein phosphatase activity (nmol·mg protein-1·h-1) in vastus lateralis, used as a measure of Na+-K+-ATPase activity, decreased ( P < 0.05) by 21% at 30 min of exercise compared with rest (101 ± 53 vs. 79.6 ± 4.3) with no further reductions observed at 90 min (72.8 ± 8.0). During H, similar reductions ( P < 0.05) were observed during the first 30 min (90.8 ± 5.3 vs. 79.0 ± 6.3) followed by further reductions ( P < 0.05) at 90 min (50.5 ± 3.9). Exercise in N resulted in reductions ( P < 0.05) in both quadriceps maximal voluntary contractile force (MVC; 633 ± 50 vs. 477 ± 67 N) and force at low frequencies of stimulation, namely 10 Hz (142 ± 16 vs. 86.7 ± 10 N) and 20 Hz (283 ± 32 vs. 236 ± 31 N). No changes were observed in the amplitude, duration, and area of the muscle compound action potential (M wave). Exercise in H was without additional effect in altering MVC, low-frequency force, and M-wave properties. It is concluded that, although exercise in H resulted in a greater inactivation of Na+-K+-ATPase activity compared with N, neuromuscular fatigue and membrane excitability are not differentially altered.

Muscle sarcoplasmic reticulum Ca2+ cycling adaptations during 16 h of heavy intermittent cycle exercise

2005 ◽  
Vol 99 (3) ◽  
pp. 836-843 ◽  
Author(s):  
G. P. Holloway ◽  
H. J. Green ◽  
T. A. Duhamel ◽  
S. Ferth ◽  
J. W. Moule ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Vastus Lateralis ◽  
Phase 1 ◽  
Hill Coefficient ◽  
Kinetic Properties ◽  
Cycle Exercise ◽  
Tissue Samples ◽  
The Hill

The repetition-dependent effects of a repetitive heavy exercise protocol previously shown to alter muscle mechanic behavior (Green HJ, Duhamel TA, Ferth S, Holloway GP, Thomas MM, Tupling AR, Rich SM, and Yau JE. J Appl Physiol 97: 2166–2175, 2004) on muscle sarcoplasmic reticulum (SR) Ca2+-transport properties, measured in vitro, were examined in 12 untrained volunteers [peak aerobic power (V̇o2 peak) = 44.3 ± 0.66 ml·kg−1·min−1]. The protocol involved 6 min of cycle exercise performed at ∼91% V̇o2 peak once per hour for 16 h. Tissue samples were obtained from the vastus lateralis before (B) and after (A) exercise at repetitions 1 (R1), 2 (R2), 9 (R9), and 16 (R16). Reductions ( P < 0.05) in maximal Ca2+-ATPase activity ( Vmax) of 26 and 12% with exercise were only observed at R1 and R16, respectively. Vmax remained depressed ( P < 0.05) at R2 (B) but not at R9 (B) and R16 (B). No changes were observed in two other kinetic properties of the enzyme, namely the Hill coefficient (defined as the slope of the relationship between Ca2+-ATPase activity and free Ca2+ concentration) and the Ca50 (defined as the free Ca2+ concentration needed to elicit 50% Vmax). Changes in Ca2+ uptake (measured at 2,000 nM) with exercise and recovery generally paralleled Vmax. The apparent coupling ratio, defined as the ratio between Ca2+ uptake and Vmax, was unaffected by the intermittent protocol. Reductions ( P < 0.05) in phase 1 Ca2+ release (32%) were only observed at R1. No differences were observed between B and A for R2, R9, and R16 or between B and B for R1, R2, R9, and R16. The changes in phase 2 Ca2+ release were as observed for phase 1 Ca2+ release. It is concluded that the SR Ca2+-handling properties, in general, display rapid adaptations to repetitive exercise.

scholarly journals Effects of fatigue and training on sarcoplasmic reticulum Ca2+ regulation in human skeletal muscle

2002 ◽  
Vol 92 (3) ◽  
pp. 912-922 ◽  
Author(s):  
Jia L. Li ◽  
Xiao N. Wang ◽  
Steve F. Fraser ◽  
Michael F. Carey ◽  
Tim V. Wrigley ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Human Skeletal Muscle ◽  
Fiber Type ◽  
Vastus Lateralis ◽  
Human Muscle ◽  
Training Status ◽  
Type Ii ◽  
Muscle Biopsies ◽  
And Training

Little is known about fatigue and training effects on sarcoplasmic reticulum (SR) function in human muscle, and we therefore investigated this in eight untrained controls (UT), eight endurance-trained (ET), and eight resistance-trained athletes (RT). Muscle biopsies (vastus lateralis) taken at rest and after 50 maximal quadriceps contractions (180°/s, 0.5 Hz) were analyzed for fiber composition, metabolites and maximal SR Ca2+ release, Ca2+ uptake, and Ca2+-ATPase activity. Fatigue reduced ( P < 0.05) Ca2+ release (42.1 ± 3.8%, 43.4 ± 3.9%, 31.3 ± 6.1%), Ca2+ uptake (43.0 ± 5.2%, 34.1 ± 4.6%, 28.4 ± 2.8%), and Ca2+-ATPase activity (38.6 ± 4.2%, 48.5 ± 5.7%, 29.6 ± 5.0%), in UT, RT, and ET, respectively. These decreases were correlated with fatigability and with type II fiber proportion ( P < 0.05). Resting SR measures were correlated with type II proportion ( r ≥ 0.51, P < 0.05). ET had lower resting Ca2+ release, Ca2+ uptake, and Ca2+-ATPase ( P < 0.05) than UT and RT ( P < 0.05), probably because of their lower type II proportion; only minor effects were found in RT. Thus SR function is markedly depressed with fatigue in controls and in athletes, is dependent on fiber type, and appears to be minimally affected by chronic training status.

Prolonged exercise to fatigue in humans impairs skeletal muscle Na+-K+-ATPase activity, sarcoplasmic reticulum Ca2+ release, and Ca2+ uptake

2004 ◽  
Vol 97 (4) ◽  
pp. 1414-1423 ◽  
Author(s):  
James A. Leppik ◽  
Robert J. Aughey ◽  
Ivan Medved ◽  
Ian Fairweather ◽  
Michael F. Carey ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
G Protein ◽  
Uptake Rate ◽  
Prolonged Exercise ◽  
Transport Processes ◽  
Vastus Lateralis Muscle ◽  
Ouabain Binding ◽  
Exercise In Humans

Prolonged exhaustive submaximal exercise in humans induces marked metabolic changes, but little is known about effects on muscle Na+-K+-ATPase activity and sarcoplasmic reticulum Ca2+ regulation. We therefore investigated whether these processes were impaired during cycling exercise at 74.3 ± 1.2% maximal O2 uptake (mean ± SE) continued until fatigue in eight healthy subjects (maximal O2 uptake of 3.93 ± 0.69 l/min). A vastus lateralis muscle biopsy was taken at rest, at 10 and 45 min of exercise, and at fatigue. Muscle was analyzed for in vitro Na+-K+-ATPase activity [maximal K+-stimulated 3- O-methylfluorescein phosphatase (3- O-MFPase) activity], Na+-K+-ATPase content ([3H]ouabain binding sites), sarcoplasmic reticulum Ca2+ release rate induced by 4 chloro- m-cresol, and Ca2+ uptake rate. Cycling time to fatigue was 72.18 ± 6.46 min. Muscle 3- O-MFPase activity (nmol·min−1·g protein−1) fell from rest by 6.6 ± 2.1% at 10 min ( P < 0.05), by 10.7 ± 2.3% at 45 min ( P < 0.01), and by 12.6 ± 1.6% at fatigue ( P < 0.01), whereas 3[H]ouabain binding site content was unchanged. Ca2+ release (mmol·min−1·g protein−1) declined from rest by 10.0 ± 3.8% at 45 min ( P < 0.05) and by 17.9 ± 4.1% at fatigue ( P < 0.01), whereas Ca2+ uptake rate fell from rest by 23.8 ± 12.2% at fatigue ( P = 0.05). However, the decline in muscle 3- O-MFPase activity, Ca2+ uptake, and Ca2+ release were variable and not significantly correlated with time to fatigue. Thus prolonged exhaustive exercise impaired each of the maximal in vitro Na+-K+-ATPase activity, Ca2+ release, and Ca2+ uptake rates. This suggests that acutely downregulated muscle Na+, K+, and Ca2+ transport processes may be important factors in fatigue during prolonged exercise in humans.

Effect of Aldosterone on the Human Erythrocyte Sodium-Potassium Pump in vitro

1983 ◽  
Vol 64 (2) ◽  
pp. 183-186 ◽  
Author(s):  
N. Stern ◽  
F. Beck ◽  
J. Sowers
Keyword(s):  
Atpase Activity ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Ouabain Binding ◽  
Physiological Concentration ◽  
Sodium Potassium ◽  
Human Erythrocyte Membranes ◽  
Erythrocyte Sodium ◽  
Sodium Potassium Pump

1. The effects of aldosterone in vitro on the Na+,K+-dependent ATPase activity of isolated human erythrocyte membranes and on rubidium (86Rb) uptake and [3H]ouabain binding of intact erythrocytes were studied. 2. ATPase activity was nearly doubled (0.061 ± 0.006 to 0.110 ± 0.01 μmol of Pl h−1 mg−1 of protein) by the addition of a physiological concentration of aldosterone (2.7 × 10-10 mol/l). Higher concentrations had no greater effect. 3. Aldosterone had no significant effect on 86Rb uptake or [3H]ouabain binding. 4. Erythrocytes contain aldosterone at concentrations similar to that in plasma. The effect of aldosterone on ATPase is probably maximal.

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