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  • 1
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 770 (1984), S. 203-209 
    ISSN: 0005-2736
    Schlagwort(e): (Na^+ + K^+)-ATPase ; (Rat skeletal muscle) ; Fluorescent probe ; Na^+ pump determination ; Phosphatase
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Medizin , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 860 (1986), S. 708-712 
    ISSN: 0005-2736
    Schlagwort(e): (Na^+ + K^+)-ATPase ; (Rat skeletal muscle) ; Exercise ; K^+ transport ; Training ; [^3H]Ouabain binding
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Medizin , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 686 (1982), S. 253-256 
    ISSN: 0005-2736
    Schlagwort(e): (Rat soleus muscle) ; Aging ; Ouabain-binding site ; Receptor number
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Medizin , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 111 (1983), S. 319-325 
    ISSN: 0006-291X
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 111 (1983), S. 319-325 
    ISSN: 0006-291X
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Amsterdam : Elsevier
    Journal of Molecular and Cellular Cardiology 19 (1987), S. 589-594 
    ISSN: 0022-2828
    Schlagwort(e): 3-O-MFPase ; Cardiomyopathy ; Hamster ; Na, K-ATPase ; Na, K-pump
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Medizin
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 7
    Digitale Medien
    Digitale Medien
    Springer
    Basic research in cardiology 92 (1997), S. 57-59 
    ISSN: 1435-1803
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Conclusions Myocardial and skeletal muscular K homeostasis is of importance for the integrity of myocardial function. Myocardial K homeostasis is affected by ischemia. Cardiac failure as well as diuretic therapy may individually and combined lead to dysfunction of K homeostasis. ACE inhibitors and β-adrenoceptor antagonists can beneficially affect K homeostasis explaining the decrease in mortality seen in heart failure patients treated with such drugs. Knowledge concerning the regulation of Na,K-ATPase and its link to K handling may render new insight in the pathophysiology of cardiac disease, and may hence lead to novel therapeutic interventions based on a rational approach.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 8
    ISSN: 1435-1803
    Schlagwort(e): Na,K-ATPase ; 3 H-ouabain binding sites ; cardiac glycosides ; myocardium ; ischemia
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Na,K-ATPase concentration was measured by vanadata facilitated3H-ouabain binding to intact samples taken from various parts of porcine and canine myocardium. In porcine and canine heart3H-ouabain binding site concentration in ventricles was 1.4–2.5 times larger than in atria. Evaluation of3H-ouabain binding kinetics revealed no major difference between atria and ventricles: Equilibrium was obtained after the same incubation time in right atrium (RA) as in left ventricle (LV), both in porcine and canine heart. Unspecific uptake and retention of3H-ouabain was for porcine heart RA and LV 1.5 and 1.4, respectively, and for canine heart RA and LV, both 1.2% filling (i.c., volume (ml) of incubation medium3H-radioactivity taken up per mass unit (g wet wt.) of tissue multiplied by 100). The apparent dissociation constant (K d ) was 1.4×10−8 and 1.9×10−8 in porcine RA and LV and 2.6×10−8 and 6.1×10−8 mol/l in canine RA and LV. Loss of specifically bound3H-ouabain during the washout procedure occurred with a half-life time (T1/2) of 16.7 in RA and LV of porcine heart and 91.2 and 151.6h in RA and LV of canine heart. Duly corrected for these errors of the method-factor 1.16 and 1.13, respectively, for porcine RA and LV, and factor 1.11 and 1.13 for canine RA and LV, total3H-ouabain binding site concentration was found to be 553±74 and 1037±45 pmol/g wet wt. (means±SEM, n=5) in porcine RA and LV, and 569±37 and 1410±40 pmol/g wet wt. (means ±SEM, n=5) in the canine RA and LV. These values were confirmed by measurements of3H-digoxin binding to the porcine heart. The present quantification of myocardial Na, K-ATPase gives values up to 154 times higher than measurements based upon Na,K-ATPase activities in membrane fractions where the recovery of Na,KK-ATPase may be less than 1% due to loss during purification. A higher Na,K-ATPase concentration is found in small animals than in large animals. A relationship between higher concentration of Na, K-ATPase and larger pressure work in ventricles compared to atria is suggested. Myocardial3H-ouabain binding sites were found to be stable for 20 min of ischemia, followed by 1h of reperfusion, supporting the concept that myocyte injury induced by short term ischemia may be reversible and that reperfusion may result in normalization.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 9
    ISSN: 1435-1803
    Schlagwort(e): Na,K-ATPase ; 3H-ouabain binding ; heart failure ; tachycardia ; potassium ; calcium
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary The present study evaluates3H-ouabain binding site (Na,K-ATPase) concentration in left ventricular myocardium of dogs with heart failure induced by tachycardia as a result of ventricular pacing. Samples of left ventricle were obtained from 10 dogs exposed to pacing of 240 beats/min for 3 to 4 weeks and eight sham-operated controls. Na,K-ATPase was quantified using vanadate facilitated3H-ouabain binding to intact samples. At time of sacrifice paced dogs showed clinical signs of heart failure, a significant 257% increase in left ventricular end diastolic pressure and a significant 46% decrease in left ventricular dP/dt compared with control. There was no significant change in left ventricular mass.3H-ouabain binding concentration was significantly reduced by 16%. Evaluation of3H-ouabain binding kinetics revealed no significant difference between myocardium from paced and control dogs: Equilibrium binding conditions were at the various concentrations used obtained after similar incubation time; nonspecific uptake and retention of3H-ouabain was 0.9–0.8% of total uptake and retention obtained in the standard assay; apparent dissociation constant (KD) was 6.5×10−8–6.6×10−8mol/l; loss of specifically bound3H-ouabain during washout at 0°C occurred with a half-life time (T3/2) of 120 and 121h. Hence, total3H-ouabain binding site concentration in left ventricular myocardium was (mean±SEM) 1110±56 and 1317±68 pmol/g wet weight, 8.54±0.43 and 10.05±0.52 pmol/mg protein, and the total amount of3H-ouabain binding sites in the entire left ventricle 121±6 and 162±8 nmol in paced (n=10) and control (n=8) dogs (p〈0.05), respectively. In conclusion, the present study reports a significant reduction in left ventricular myocardium3H-ouabain binding site concentration in tachycardia induced heart failure. This observation supports the concept of a relationship between Na,K-ATPase concentration and contractile capacity and may be of pathophysiological importance in tachycardia and heart failure.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 10
    Digitale Medien
    Digitale Medien
    Springer
    Basic research in cardiology 90 (1995), S. 323-331 
    ISSN: 1435-1803
    Schlagwort(e): Na+ ; K+-ATPase ; Ca2+-ATPase ; rat ventricular myocardium
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Assays for complete quantification of Na+, K+-and Ca2+-ATPase in crude homogenates of rat ventricular myocardium by determination of K+-and Ca2+-dependentp-nitrophenyl phosphatase (pNPPase) activities were evaluated and optimized. Using these assays the total K+-and Ca2+-dependentpNPPase activities in ventricular myocardium of 11–12 week-old rats were found to be 2.98±0.10 and 0.29±0.02 μmol×min−1×g−1 wet wt. (mean±SEM) (n=5), respectively. Coefficient of variance of interindividual determinations was 7 and 12%, respectively. The total Na+, K+-and Ca2+-ATPase concentrations were estimated to 2 and 10 nmol×g−1 wet wt., respectively. Evaluation of a putative developmental variation revealed a biphasic age-related change in the rat myocardial Ca2+-dependentpNPPase activity with an increase from birth to around the third week of life followed by a decrease. By contrast, the K+-dependentpNPPase activity of the rat myocardium showed a decrease from birth to adulthood. It was excluded that the changes were simple out-come of variations in water and protein content of myocardium. Expressed per heart, the K+-and Ca2+-dependentpNPPase activity gradually increased to a plateau. The present assay for Na+, K+-ATPase quantification has the advantage over [3H] ouabain binding of being applicable on the ouabain-resistant rat myocardium, and is more simple and rapid than measurements of K+-dependent 3-0-methylfluorescein phosphatase (3-0-MFPase) in crude tissue homogenates. Furthermore, with few modifications thepNPPase assay allows quantification of Ca2+-ATPase on crude myocardial homogenates. Age-dependent changes in K+-and Ca2+-dependentpNPPase activities are of developmental interest and indicate the importance of close age match in studies of quantitative aspects of Na+, K+-and Ca2+-ATPase in excitable tissues.
    Materialart: Digitale Medien
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