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At least 829 records · Page 46Linked to original sources
PubMed1990

Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase.

The TFP1 gene of the yeast Saccharomyces cerevisiae encodes two proteins: the 69-kilodalton (kD) catalytic subunit of the vacuolar proton-translocating adenosine triphosphatase (H(+)-ATPase) and a 50-kD protein. The 69-kD subunit is encoded by the 5' and 3' thirds of the TFP1 coding region, whereas the 50-kD protein is encoded by the central third. Evidence is presented that both the 69-kD and 50-kD proteins are obtained from a single translation product that is cleaved to release the 50-kD protein and spliced to form the 69-kD subunit.

Animals↗
PubMed1986

Lead does not affect calmodulin-induced activation of calcium-dependent adenosine triphosphatase in human red blood cell membranes.

The effects of lead (Pb) on the calmodulin activation of human red blood cell membrane calcium-dependent adenosine triphosphatase (Ca-ATPase) were studied in vitro. It was not possible to exclude EGTA from the hemolyzing buffer and retain Ca-ATPase activity and therefore exact concentrations of Pb in the incubation are not known. Nonetheless, nanomolar concentrations of Pb stimulated Ca-ATPase with or without exogenous calmodulin and none of the Pb concentrations tested (1 nM-100 microM) interfered with the calmodulin stimulation of the enzyme. High concentrations of Pb (greater than 10 microM) inhibited Ca-ATPase activity. It is possible that low concentrations of Pb can interfere with calcium dependent processes but the calcium-regulatory protein, calmodulin, is not susceptible to interference by Pb under the conditions used here.

Calcium-Transporting ATPases↗
PubMed1981

Effect of triiodothyronine on (Na+ G K+)-adenosine triphosphatase and (Na+ + Mg2+)-dependent phosphorylated intermediate in rat salivary glands.

The present studies concern the effect of triiodothyronine (T3) on rat salivary (Na+ + K+)-adenosine triphosphatase (NaK-ATPase). The results indicate that T3 selectively increased submandibular and parotid NaK-ATPase units with a single, large dose of T3, different dosage of T3, three successive doses of T3 given on alternate days, and "physiological" doses of T3 with daily injection for 2 weeks. Sublingual NaK-ATPase was insensitive to T3 in the above experiments. The effect of T3 on submandibular and parotid NaK-ATPase is selective since Mg-ATPase and 5'-nucleotidase showed no significant differences under different thyroid status. The lack of response of NaK-ATPase to reverse T3, further substantiates the specificity of T3 on salivary NaK-ATPase.

Animals↗
PubMedDate not supplied

Histochemical localization of phosphatases in the pig placenta: II. Potassium-dependent and potassium-independent p-nitrophenyl phosphatases at high pH; relation to sodium-potassium-dependent adenosine triphosphatase.

Histochemical localization by Mg2+ capture methods of K+-dependent, ouabain-sensitive phosphatase activity in the pig placenta shows that strong Na+,K+-dependent adenosine triphosphatase (Na+,K+-ATPase) activity is restricted to the basal zone of the columnar epithelium covering the areolar chorionic villi. It is proposed that active Na+ absorption at this epithelium may be the source of the ouabain-sensitive, fetal-side-positive potential difference which can be measured across the placental membrane in vitro. The one-step procedure for Na+,K+-ATPase localization is unsatisfactory in this organ as any specific ATPase reaction is swamped by activity probably attributable to uteroferrin and other non-specific phosphatases.

4-Nitrophenylphosphatase↗
PubMed1984

Centrally-induced vasopressor responses to sodium-potassium adenosine triphosphatase inhibitor, ouabain, may be mediated via angiotensin II in the anteroventral third ventricle in the brain.

Central cardiovascular effects of the sodium-potassium adenosine triphosphatase (Na+, K+-ATPase) inhibitor, ouabain, were investigated by injecting it intracerebroventricularly (ICV) using conscious Wistar rats. Ouabain, 0.1-10 micrograms injected ICV, produced dose-related pressor responses attaining peak elevations after about 5 min. To investigate the underlying mechanisms of these central pressor responses, angiotensin II blockers were injected ICV before the injections of ouabain. 1-Sar, 8-Ile angiotensin II (ang IIa), 50 micrograms, given 3 min before the ouabain, abolished the pressor responses to ouabain, 5 micrograms. Angiotensin I converting enzyme inhibitor (CEI, captopril), 100 micrograms, also significantly attenuated the pressor responses to ouabain. Since previous results with ICV injections of ouabain suggested that the pressor responses are mediated via a release of brain angiotension II, and the site of action of brain angiotensin II is believed to be the anteroventral third ventricle (AV3V) area of the brain, ICV injections of ouabain were repeated using rats whose AV3V areas had been destroyed electrically. The pressor responses were smaller in the AV3V lesioned rats than in sham-operated rats. The abdominal sympathetic nerve activity was recorded using three conscious, normotensive Wistar rats. ICV injections of ouabain, 5 micrograms, elicited pressor responses as described above and these were accompanied by a corresponding increase in the nerve firing, lasting for 5-7 min. These responses were again abolished by pretreatment with an angiotensin II antagonist. These results suggest that centrally administered ouabain elicits vasopressor responses which increase peripheral sympathetic nerve activity.(ABSTRACT TRUNCATED AT 250 WORDS)

1-Sarcosine-8-Isoleucine Angiotensin II↗
PubMed2002

Effect of ethanol on regulation of (Na + K)-adenosine triphosphatase by aldosterone and dexamethasone in cultured renal papillary collecting duct cells.

Chronic ethanol exposure causes alterations in biologic membranes of different cell types. (Na + K) adenosine triphosphatase (ATPase), a membrane-bound enzyme inhibited by the acute presence of ethanol, increases its activity in rat kidney after chronic ethanol consumption. The aim of this investigation was to evaluate the effect of ethanol on the modulation of (Na + K)-ATPase by glucocorticoids and mineralocorticoids in renal papillary collecting duct cells. Cultured renal papillary collecting duct cells were exposed to a medium containing 150 mM ethanol plus either 100 nM aldosterone or 10 nM dexamethasone. Control groups were cultured in the absence of ethanol and/or the hormones. Mg(2+)-ATPase was used as control enzyme. The activity of ATPases was measured by ATP hydrolysis. Ethanol increased the activities of (Na + K)-ATPase and Mg(2+)- ATPase in 29 and 33% of controls, respectively; only (Na + K)-ATPase activity was elevated in the presence of aldosterone or dexamethasone, whereas Mg(2+)-ATPase was unaltered by these hormones. The effects of aldosterone and dexamethasone on (Na + K)-ATPase activity were augmented by ethanol in 50 and 19% of controls, respectively. These results suggest that ethanol treatment enhances the upregulation of (Na + K)-ATPase activity by both aldosterone and dexamethasone, in cultured renal papillary collecting duct cells.

Adenosine Triphosphate↗
PubMed1979

On the mechanism of Ca2+-dependent adenosine triphosphatase of sarcoplasmic reticulum. Occurrence of two types of phosphoenzyme intermediates in the presence of KCl.

The steady state kinetics of ATP hydrolysis by partially purified adenosine triphosphatase preparations of sarcoplasmic reticulum was investigated at 0 degrees C and pH 7.0 in 2.0 mM MgCl2, 20 microM [gamma-32P]ATP, 20 microM CaCl2, and various concentrations of KCl in the presence and absence of 12% dimethyl sulfoxide. The steady state phosphoenzyme formed under these conditions could be resolved kinetically into ADP-sensitive and ADP-insensitive forms. These steady state kinetic data were analyzed according to a scheme in which the ADP-sensitive and ADP-insensitive phosphoenzymes occur sequentially, and Pi is derived from the latter. The KCl-dependent turnover rate of the ADP-insensitive phosphoenzyme that was estimated according to this scheme was in good agreement with the directly measured hydrolysis rate constant of the ADP-insensitive phosphoenzyme. In addition, the time course of the decomposition of the total amount of phosphoenzyme, measured after a steady state level was reached in 20 mM KCl and further phosphorylation was prevented by addition of excess ethylene glycol bis(beta-aminoethyl ether)N,N,N',N'-tetraacetic acid, was also in agreement with that calculated according to this scheme using values of the rate constants estimated from the amounts of the ADP-sensitive and ADP-insensitive phosphoenzymes and the rate of ATP hydrolysis. These results, together with our previous findings, support the view that this scheme describes the mechanism of ATP hydrolysis in the presence of KCl.

Adenosine Triphosphate↗