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PubMedDate not supplied

Adaptation of inner medullary collecting duct vacuolar H-adenosine triphosphatase to chronic acid or alkali loads in the rat.

Acidosis increases and alkalosis decreases proton secretion in the inner medullary collecting duct (IMCD). We examined the mechanism of this adaptation by studying the immunocytochemical distribution of the vacuolar H-adenosine triphosphatase (ATPase) in the IMCD from rats subjected to acid or alkali loads for a mean duration of 4 and 9 days. For immunocytochemical staining, a monoclonal antibody to the 31-kD subunit of the bovine kidney vacuolar H-ATPase was used. Intercalated cells were present only in the initial IMCD, and the principal cells and IMCD cells showed no appreciable H-ATPase staining under any experimental conditions. We found significant adaptive changes in the distribution of H-ATPase in the intercalated cells of the IMCD. H-ATPase staining in acid-loaded rats shifted from cytoplasmic vesicles to apical plasma membrane, whereas in alkali-loaded rats cytoplasmic vesicular staining was enhanced and staining of plasma membrane disappeared. These adaptive changes were most prominent on day 4 of acid-loaded and days 4 and 9 of alkali-loaded rats. Our results indicate that translocation of the H-ATPase pump between cytoplasmic vesicles and apical plasma membrane of the intercalated cells is an important mechanism is adaptation of the IMCD to chronic acid base perturbations.

Acidosis↗
PubMed1993

Cholinergic stimulation of the Na+/K+ adenosine triphosphatase as revealed by microphysiometry.

The activation of a wide range of cellular receptors has been detected previously using a novel instrument, the microphysiometer. In this study microphysiometry was used to monitor the basal and cholinergic-stimulated activity of the Na+/K+ adenosine triphosphatase (ATPase) (the Na+/K+ pump) in the human rhabdomyosarcoma cell line TE671. Manipulations of Na+/K+ ATPase activity with ouabain or removal of extracellular K+ revealed that this ion pump was responsible for 8.8 +/- 0.7% of the total cellular energy utilization by those cells as monitored by the production of acid metabolites. Activation of the pump after a period of inhibition transiently increased the acidification rate above baseline, corresponding to increases in intracellular [Na+] ([Na+]i) occurring while the pump was off. The amplitude of this transient was a function of the total [Na+]i excursion in the absence of pump activity, which in turn depended on the duration of pump inhibition and the Na+ influx rate. Manipulations of the mode of energy metabolism in these cells by changes of the carbon substrate and use of metabolic inhibitors revealed that, unlike some other cells studied, the Na+/K+ ATPase in TE671 cells does not depend on any one mode of metabolism for its adenosine triphosphate source. Stimulation of cholinergic receptors in these cells with carbachol activated the Na+/K+ ATPase via an increase in [Na+]i rather than a direct activation of the ATPase.

Biophysical Phenomena↗
PubMed1995

Secretin causes H+/HCO3- secretion from pig pancreatic ductules by vacuolar-type H(+)-adenosine triphosphatase.

BACKGROUND/AIMS: Secretin stimulates pancreatic ductules to secrete HCO3- into pancreatic juice and H+ into interstitial fluid. The aim of the present study was first to examine whether ductular H+ secretion is inhibited by micromolar concentrations of bafilomycin A1, which blocks vacuolar H(+)-adenosine triphosphatase by specific action, and secondly to test for evidence of ductular Na+/HCO3- cotransport. METHODS: Ductular H+ secretion was estimated from the rate of intracellular pH recovery after acid-loading (24 mmol/L NH4Cl) microdissected pancreatic ductules from pig, mounted in a flow-through perfusion chamber on the stage of a fluorescent microscope. Intracellular pH was measured using the fluorescent pH indicator 2'7'-bis (carboxyethyl)-5,6-carboxyfluorescein and dual-wave-length excitation of fluorescence. The ducts were superfused perfused with either HCO3(-)-free HEPES-containing buffers or HCO3(-)-containing buffers. RESULTS: Secretin (10(-8) mol/L) induced a net H+ secretion of 1.87 +/- 0.23 mumol.mL cell vol-1.min-1 that was blocked by 10(-6) mol/L bafilomycin A1 and was unaffected by Na+ substitution with choline using HEPES superfusion buffers. Secretin-stimulated ductules superfused with bicarbonate-containing, Cl(-)-free buffers showed Na(+)-dependent and 4,4'-diisothiocyanostilbene-2, 2'-disulfonic acid-inhibitable alkalinization of intracellular pH. CONCLUSIONS: Secretin causes H+/HCO3- secretion from pancreatic ductules by a mechanism involving vacuolar-type H(+)-adenosine phosphatase. Pancreatic ductules also show Na+/HCO3- cotransport, which may account for a small fraction of secreted bicarbonate.

Amiloride↗
PubMed1990

Reversible inhibition of sodium and potassium-dependent adenosine triphosphatase by the pyridine derivative, AU-1421 during turnover cycle.

A novel pyridine derivative, (Z)-5-methyl-2-[2-(1-naphthyl)ethenyl]-4-piperidonopyridine hydrochloride, AU-1421, was found to produce reversible inhibition of the dog kidney sodium and potassium ion-dependent adenosine triphosphatase [(Na,K)-ATPase] with I50 values of about 50 microM. The reversible inhibition was observed when the enzyme was added directly to the enzyme assay media in the presence of saturating concentrations of the enzyme ligands, Na+, K+, Mg2+ and ATP ("turnover conditions"). In the present study, we focused on the reversible inhibition without preincubation of the enzyme with AU-1421. This inhibition was competitive with respect to K+. The K(+)-pNPPase activity of the same preparation was also inhibited by AU-1421 with I50 values of about 90 microM, and this manner was also competitive with respect to K+. ATP enhanced the AU-1421 inhibition of (Na,K)-ATPase, suggesting that AU-1421 also bound to the enzyme-substrate complex. AU-1421 inhibition of (Na,K)-ATPase was not antagonized by ouabain, suggesting the difference of the binding sites between AU-1421 and ouabain. It is therefore proposed that AU-1421 reversibly interacts at or near the K+ site during turnover conditions.

4-Nitrophenylphosphatase↗
PubMed1980

The primary structure of the calcium-transporting adenosine triphosphatase of rabbit skeletal sarcoplasmic reticulum. Soluble tryptic peptides from the succinylated carboxymethylated protein.

The isolation and the determination of the amino-acid sequences of the soluble tryptic peptides, derived by cleavage at arginine residues, of the succinylated (3-carboxypropionylated) S-carboxymethylated adenosine triphosphatase protein of rabbit skeletal sarcoplasmic reticulum are described. Treatment of the protein with succinic anhydride gave a derivative that was readily digested with trypsin, yielding two distinct sets of peptides. One set comprises large, relatively hydrophobic, peptides that are highly aggregated (or insoluble) in aqueous solution and that have been identified, by several criteria, with the portion of the protein embedded in the lipid bilayer in the sarcoplasmic reticulum. The second set, which is described here, comprises peptides that have properties typical of those derived from soluble globular proteins and that constitute that part of the protein external to the lipid bilayer. The sequences of these soluble tryptic peptides contain 586 unique residues. Details of the isolation of the peptides and the determination of the sequences are contained in Supplementary Publication SUP 50102 (88 pages) which has been deposited with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

Amino Acid Sequence↗
PubMed1990

Inhibition of protein kinase C, (sodium plus potassium)-activated adenosine triphosphatase, and sodium pump by synthetic phospholipid analogues.

The effects and modes of action of certain antineoplastic phospholipid analogues (racemic 1-O-octadecyl-2-O-methyl glycero-3-phosphocholine, BM 41.440, JH-1, CV-3988, and HePC) on (sodium plus potassium)-activated adenosine triphosphatase (Na,K-ATPase) and sodium pump activities were investigated. Inhibition of Na,K-ATPase in purified rat brain synaptosomal membranes by these lipids, in contrast to ouabain, was subject to membrane surface dilution and unaffected by whether the reaction was started with KCl, NaCl, or ATP. Kinetic analysis indicated that the analogues, again dissimilar to ouabain, were likely to interact directly or indirectly with sodium-binding sites of Na,K-ATPase located at the intracellular surface of the plasma membrane, a conclusion also supported by studies using the inside-out vesicles of human erythrocyte membranes. The studies also showed that ouabain (but not the lipids) increased the affinity constant of Na,K-ATPase for K+, whereas the lipids (but not ouabain) increased that for Na+. The lipids also inhibited 86Rb uptake by intact human leukemia HL60 cells at potencies quite comparable to those seen for inhibition of purified protein kinase C or Na,K-ATPase. It is suggested that Na,K-ATPase (sodium pump) might represent a hitherto unrecognized site of action for the lipid analogues, and that the antineoplastic effects of the agents might be due to, in part, inhibition of both protein kinase C and Na,K-ATPase and perhaps other membrane-associated enzymes.

Biological Transport, Active↗
PubMed1993

Modulation of sodium-potassium adenosine triphosphatase in cultured bovine retinal pigment epithelium by potassium.

PURPOSE: The aim of the study was to examine the extracellular potassium concentration [K+]o as a modulator of the retinal pigment epithelium (RPE) contribution to ion homeostasis in the subretinal space by measuring sodium-potassium adenosine triphosphatase (Na+/K+ ATPase) pump number and activity in cultured bovine RPE in the presence of different concentrations of extracellular potassium. METHODS: Pump number was quantified by measuring specific binding of 3H-ouabain to bovine RPE exposed to low (0.5-2.5 mmol) or control (5.0 mmol) [K+]o over 72 hr. Na+/K+ ATPase activity in low and control [K+]o was quantified by measurement of 86Rb+ uptake. RESULTS: Low [K+]o increased RPE pump number in a dose- and time-dependent manner, with lesser effects on denser than on sparser cultures. [K+]-modulation of pump number was reversible and did not occur in the presence of the protein synthesis inhibitor cycloheximide. In RPE exposed to low [K+]o for 72 hr, pump activity was decreased compared with the control but increased toward control levels when re-exposed to control [K+]o. The total potassium transported per cell was 60% of control in low [K+]o but increased to slightly above control when re-exposed to control [K+]o. CONCLUSIONS: In cultured RPE cells, both Na+/K+ ATPase pump number and pump activity are affected by changes in [K+]o, with greater modulation in sparser cultures. If similar events occur in situ, the sodium pump in RPE may respond to changes in subretinal potassium ion concentration, especially if the RPE cell number is reduced as in aging or disease.

Animals↗
PubMed1969

Membrane adenosine triphosphatase of Escherichia coli: activation by calcium ion and inhibition by monovalent cations.

Membrane ghost preparations of Escherichia coli K-12 obtained by osmotic lysis of lysozyme-induced spheroplasts were found to possess both Mg(++)- and Ca(++)-activated adenosine 5'-triphosphatase (ATPase, EC 3.6.1.3) activities. Maximal activities of 1.0 to 1.5 mumoles of orthophosphate released per min per mg of protein were obtained at pH 9.0 with a molar Mg(++) to adenosine 5'triphosphate (ATP) ratio of 2:5 and at pH 9.9 with a molar Ca(++) to ATP ratio of 1:5. These ATPase activities were not altered by ouabain, fluoride, N-ethylmaleimide, 2,4-dinitrophenol, cyanide, or dithionite, but were inhibited by low concentrations of azide, p-chloromercuribenzoate, and pentachlorophenol. Mg(++) ATPase was more susceptible to inhibition by azide than was Ca(++) ATPase. Fifty per cent inactivation of both activities was observed when membrane ghost preparations were preincubated at 66 C for 10 min. The Mg(++) and Ca(++) ATPase activities of these preparations were not additive, but did respond independently to inhibition by monovalent cations. Ca(++) ATPase was found to be very sensitive to inhibition by K(+), Na(+), Li(+), Rb(+), and Cs(+); Mg(++) ATPase was relatively insensitive to these ions. One possible interpretation of the results presented in this paper is that the membrane of E. coli possesses an ATPase which is activated by either Mg(++) or Ca(++) and that activation by Ca(++) increases the susceptibility of this enzyme to inhibition by monovalent cations. Increased susceptibility of E. coli membrane ATPase to inhibition by monovalent cations such as Na(+) and K(+) as a consequence of Ca(++) activation could represent a regulatory mechanism.

Adenine Nucleotides↗
PubMed1994

Human gastric H,K-adenosine triphosphatase beta-subunit is a major autoantigen in atrophic corpus gastritis. Expression of the recombinant human glycoprotein in insect cells.

BACKGROUND: Sera from patients with atrophic corpus gastritis with pernicious anemia frequently contain parietal cell autoantibodies. We have previously demonstrated that the human H,K-adenosine triphosphatase (H,K-ATPase) alpha-subunit constitutes a major autoantigen. The present study investigates whether the human H,K-ATPase beta-subunit is an autoantigen, too, METHODS: The gene of the human beta-subunit was expressed in insect cells by a baculovirus expression system. The reactivity of sera from 42 patients towards the recombinant glycoprotein was analyzed by means of an enzyme-linked immunosorbent assay. RESULTS: Thirty-nine of the 42 sera (93%) scored positive. Autoantibody binding in 41 sera (98%) was eliminated when unglycosylated beta-subunit was used as antigen, and antibody binding in the last serum was decreased by 30%. CONCLUSIONS: The results indicate that the beta-subunit is indeed a major autoantigen and that carbohydrates are involved in binding of the autoantibodies.

Adult↗