The role of distinct membrane components of the enzyme in the ouabain sensitivity of Na+/K+ ATPase]

Purified plasma membranes from a cell line derived from the murine plasmocytoma MOPC 173 exhibited a 50% inhibition of the Na+K+ ATPase by 120 muM ouabain. EDTA treatment of such membranes induced a drop in the ouabain concentration needed for 50% inhibition to 0.4 muM. Supernatants obtained after EDTA treatment were able to complement with Ca(++) + Mg++ the washed EDTA treated membranes which recover their original resistance.     

Purification from a total cellular lysate of a protein modifying the sensitivity of Na+/K+ ATPase to ouabain]

A protein (32,000 dalton) has been purified from M2FS cells derived from the murine plasmocytoma MOPC 173. Like tropomyosin, this protein when added with Ca++ to EDTA-treated plasma membranes prepared from the same cell, induced a drastic increase in the Na+/K+ atpase resistance to ouabain.     

Contribution of the Na+/K+-pump to the membrane potential

The inward movement of sodium ions and the outward movement of potassium ions are passive and the reverse movements against the electrochemical gradients require the activity of a metabolism-driven Na+/K+-pump. The activity of the Na+/K+-pump influences the membrane potential directly and indirectly. Thus, the maintenance of a normal electrical function requires that the Na+/K+-pump maintain normal ionic concentrations within the cell. The activity of the Na+/K+-pump also influences the membrane potential directly by generating an outward sodium current that is larger when the Na+/K+-pump activity is greater. The activity of the Na+/K+-pump is regulated by several factors including the intracellular sodium concentration and the neuromediators norepinephrine and acetylcholine. The inhibition of the Na+/K+-pump can lead indirectly to the development of inward currents that may cause repetitive activity. Therefore, the Na+/K+-pump modifies the membrane potential in different ways both under normal and abnormal conditions and influences in an essential way many cardiac functions, including automaticity, conduction and contraction. Key words. Active transport of ions; cardiac tissues; electroneutral and electrogenic Na+/K/-pump; control of Na+/K+-pump; normal and abnormal electrical events.     

Thermal activation of the cyclic AMP stimulated sodium transport across isolated toad bladder and Na+/K+ ATPase in toad bladder homogenates

Zusammenfassung Der Temperaturkoeffizient für den durch das zyklische AMP und Theophyllin stimulierten Natriumtransport in der isolierten Krötenblase wurde analysiert. Die Enzympumpe wurde stärker beeinflusst als die mukosale Permeabilität und die Aktivität von Na⁺/K⁺ ATPase korrespondiert mit der Energie der Pumpenaktivität.     

Role of tropomyosin in the sensitivity of (Na+ + K+) ATPase to ouabain]

EDTA treatment of isolated plasma membranes from MF2S cells increased 1,000 fold the sensitivity of (Na+ + K+) ATPase activity to ouabain. The original sensitivity of the enzyme to the drug is recovered after addition of tropomyosin together with Ca++ ions to the treated membranes.     

Age dependent changes in Na+−K+, activated ATPase activity of locust rectum

Summary Na⁺–K⁺, activated ATPase showed an increase in activity at the beginning of the 5th instar and adult life. This was followed by a relatively constant level of activity which, in larval preparations only, was not maintained but decreased with the onset of metamorphosis.     

A molecular recognition hypothesis for nonpeptides: Na+ K+ ATPase and endogenous digitalis-like peptides

The molecular recognition hypothesis for peptides is that binding sites of ligands and their receptors are encoded by short, complementary segments of DNA. A corollary hypothesis for nonpeptide ligands posited here is that peptide replicas may be encoded by the DNA segment complementary to the receptor binding sites for nonpeptides. This corollary was tested for digitalis, a family of cardiotonic and natriuretic steroids including ouabain. A hexapeptide (ouabain-like peptide, OLP) complementary to a ouabain binding site on sodium/potassium dependent adenosine triphosphatase (Na⁺ K⁺ ATPase) exhibited activity in a digitalis bioassay. Antisera to the complementary peptide (OLP) stained the neurohypophysis in an immunocytochemical procedure. The complementary peptide was found to share an identical 4-amino acid region with the 39-amino acid glycopeptide moiety of the vasopressin-neurophysin precursor. This glycopeptide was isolated from pituitary extracts; it exhibited digitalis-like activity in the submicromolar range and cross-reacted with complementary peptide antibodies. Another digitalis-like substance with high activity also was detected in the extracts. These results demonstrate that the vasopressin-neurophysin glycopeptide has digitalis-like activity. Moreover, the findings are consistent with the hypothesis that peptide mimetics of nonpeptides are encoded in the genome. Received 23 November 1998; received after revision 18 January 1999; accepted 19 February 1999     

The ultrastructure of brown adipose tissue in perinatal rats

Zusammenfassung Die prä- und postnatale Entwicklung des braunen Fettes von Ratten wurde untersucht unter besonderer Berücksichtigung der Matrixkörper der Mitochondrien. Diese Einschlusskörper erreichen im Zeitpunkt der Geburt hinsichtlich Grösse und Zahl ein Maximum und verschwinden dann innerhalb von 1–2 Tagen. In vivo und in vitro Experimente mit verschiedenen Umgebungstemperaturen, mit Noradrenalin, Theophyllin, einem-Rezeptorenblocker (Trasicor^®) und Dibutyryl-Adenosinmonophosphat weisen alle darauf hin, dass die physiologischen postnatalen Veränderungen im braunen Fett wenigstens zum Teil mit dem plötzlichen Temperaturabfall zusammenhängen und hormonal ausgelöst werden. Die Matrixkörper sind unter allen Versuchsbedingungen an den Strukturveränderungen der Mitochondrien beteiligt.     

Inhibition of microsomal Na+ K+ ATPase of the brain by extracts of Mansonia altissima]

Water extracts of the bark of Mansonia altissima var altissima inhibit the activity of the Na+, K+-ATPase of Rabbit brain microsomes. The kinetics of hydrolysis of ATP show non-competitive inhibition analogous to that produced by ouabain.     

Na,K ATPase activity during early postnatal development of the rat submandibular gland

Summary The activity of the ouabain-sensitive Na, K ATPase was measured in membrane fractions of the submandibular gland of 1-, 7-, 14- and 21-day-old rats. This activity increased with age and reached adult levels by 21 days.     

Na, K ATPase activity during early postnatal development of the rat submandibular gland

The activity of the ouabain-sensitive Na, K ATPase was measured in membrane fractions of the submandibular gland of 1-, 7-, 14- and 21-day-old rats. This activity increased with age and reached adult levels by 21 days.     

Purification of a membrane protein modifying the sensitivity of Na+/K+ ATPase to ouabain from a supernatant of plasma membrane treated with EDTA]

A membrane protein of M. W. 32,000 D and pI 5 has been purified from EDTA-treated plasma membrane supernatants by Page without detergents. These membranes are purified from the MF2S cell line issued from the murine plasmacytoma MOPC 173. The purified protein was able to induce a 300 fold increase in the Na+/K+ ATPase resistance to ouaba?n thus mimicking the original resistance of the enzyme to the drug.     

The (Na+ + K+)-ATPase activity in brain of Quaking mice.

The (Na+ 4 K+)- and Mg2+-dependent ATPase distribution in several brain areas has been investigated in Quaking mutant mice characterized by myelin deficiency. A marked decrease of (Na+ + K+)-ATPase activity has been found in limbic structures, hypothalamus and cerebellum. The Mg2+-dependent activity did not change. A possible involvement of the impairment of the (Na+ + K+)-ATPase activity in the seizure susceptibility of this mice is discussed.     

Effect of cholesterol oxidation on (Na+, K+) ATPase activity of erythrocyte membranes

Summary By incubation of human erythrocyte ghosts with cholesterol oxidase (EC 1.1.3.6) part of the cholesterol of the membrane is replaced by 4-cholesten-3-one. This alteration in the sterol composition is accompanied by an inhibition of the (Na⁺, K⁺) ATPase of the erythrocyte membrane.Acknowledgments. This study was supported by the Deutsche Forschungsgemeinschaft Bonn-Bad Godesberg and the Sonderforschungsbereich 90 of the University of Heidelberg. We thank Mr.J. Schmidt and MissI. Geldmacher for skilful technical assistance.     

Reversal by lecithin of the amobarbital-induced inhibition of microsomal (Na+K)-activated ATPase

Résumé L'amobarbital de soude inhibe l'activité du (Na+K)-ATPase du réticule sarcoplasmique isolé. Cette inhibition peut être évitée par l'addition de lécithine purifiée. La lécithine pré-incubée en présence de l'amobarbital inhibe (Na+K)-ATPase.     

The steroid hormone synthesis in the brown adipose tissue of mice

Zusammenfassung Braunes Fettgewebe adrenalektomierter und kastrierter weisser Mäuse synthetisiert in vitro 17-hydroxy-11-desoxycorticosteron in einer Menge 1,7–2,5µg/100 mg des Fettgewebes/h, wenn dem Inkubationsmedium Mäusehypophyse zugesetzt wird. Zugabe von ACTH bewirkt keine Stimulierung des braunen Fettgewebes.