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PubMed2002

Permeant but not impermeant divalent cations enhance activation of nondesensitizing alpha(7) nicotinic receptors.

Neuronal alpha(7) nicotinic acetylcholine receptors (nAChRs) are permeable to Ca(2+) and other divalent cations. We characterized the modulation of the pharmacological properties of nondesensitizing mutant (L(247)T and S(240)T/L(247)T) alpha(7) nAChRs by permeant (Ca(2+), Ba(2+), and Sr(2+)) and impermeant (Cd(2+) and Zn(2+)) divalent cations. alpha(7) receptors were expressed in Xenopus oocytes and studied with two-electrode voltage clamp. Extracellular permeant divalent cations increased the potency and maximal efficacy of ACh, whereas impermeant divalent cations decreased potency and maximal efficacy. The antagonist dihydro-beta-erythroidine (DHbetaE) was a strong partial agonist of L(247)T and S(240)T/L(247)T alpha(7) receptors in the presence of divalent cations but was a weak partial agonist in the presence of impermeant divalent cations. Mutation of the "intermediate ring" glutamates (E(237)A) in L(247)T alpha(7) nAChRs eliminated Ca(2+) conductance but did not alter the Ca(2+)-dependent increase in ACh potency, suggesting that site(s) required for modulation are on the extracellular side of the intermediate ring. The difference between permeant and impermeant divalent cations suggests that sites within the pore are important for modulation by divalent cations.

Acetylcholine↗
PubMed1988

Divalent cation involvement in the action of Clostridium perfringens type A enterotoxin. Early events in enterotoxin action are divalent cation-independent.

Clostridium perfringens type A enterotoxin (CPE) is a membrane-active cytotoxin. There are a number of recognized early steps in CPE cytotoxicity including binding of CPE to a protein receptor, insertion of CPE into membranes, and CPE-mediated induction of changes in membrane permeability for small molecules such as ions and amino acids. Further support for the existence of these early steps and further characterization of these events are presented in this report. We now report that these early steps in CPE action are largely independent of extracellular divalent cations. It is also shown that 3H-nucleotide release, known to be a later CPE effect, is Ca2+-dependent. A model for CPE cytotoxicity is suggested involving CPE action as a two-step process with Ca2+-independent early steps and Ca2+-dependent late steps.

Aminoisobutyric Acids↗
PubMed2001

Aggregation of nucleosomes by divalent cations.

Conditions of precipitation of nucleosome core particles (NCP) by divalent cations (Ca(2+) and Mg(2+)) have been explored over a large range of nucleosome and cation concentrations. Precipitation of NCP occurs for a threshold of divalent cation concentration, and redissolution is observed for further addition of salt. The phase diagram looks similar to those obtained with DNA and synthetic polyelectrolytes in the presence of multivalent cations, which supports the idea that NCP/NCP interactions are driven by cation condensation. In the phase separation domain the effective charge of the aggregates was determined by measurements of their electrophoretic mobility. Aggregates formed in the presence of divalent cations (Mg(2+)) remain negatively charged over the whole concentration range. They turn positively charged when aggregation is induced by trivalent (spermidine) or tetravalent (spermine) cations. The higher the valency of the counterions, the more significant is the reversal of the effective charge of the aggregates. The sign of the effective charge has no influence on the aspect of the phase diagram. We discuss the possible reasons for this charge reversal in the light of actual theoretical approaches.

Animals↗
PubMed1987

Modulation of rat brain cytosolic phosphatidate phosphohydrolase: effect of cationic amphiphilic drugs and divalent cations.

The effects of three cationic amphiphilic drugs on rat brain cytosolic phosphatidate phosphohydrolase and their mechanisms of action were studied utilizing membrane-bound, emulsified, and emulsified sonicated phosphatidate as substrates. With the membrane-bound substrate, chlorpromazine, desmethylimipramine, and propranolol inhibited the activity in a dose-dependent fashion with an IC50 of 30-50 microM. In the presence of the emulsified substrate, chlorpromazine was a more potent inhibitor than desmethylimipramine or propranolol but 200 microM was needed for 50% inhibition of activity. Addition of heat-inactivated microsomes to the emulsified substrate, to simulate the conditions with the membrane-bound substrate, did not alter this value. Both Mg2+ and Ca2+ stimulated the enzyme activity but only Ca2+ counteracted the effect of chlorpromazine. Kinetic studies indicate that chlorpromazine acts as a noncompetitive inhibitor of the enzyme. Emulsified sonicated phosphatidate was a good substrate at low (less than 10 microM) concentrations. It was a poor substrate at 1 mM, but at this concentration chlorpromazine stimulated the activity instead of inhibiting. This drug altered the integrity of phosphatidate vesicle membranes as visualized by electron microscopy. The different results obtained with the three types of substrate indicate the importance of the configuration of phosphatidate for the expression of enzyme activity and for its susceptibility to the action of cationic amphiphilic drugs.

Animals↗
PubMed1986

(Na+ + K+)-ATPase in artificial lipid vesicles: influence of the concentration of mono- and divalent cations on the pumping rate.

(Na+ + K+)-ATPase from kidney outer medulla was incorporated into artificial dioleoylphosphatidylcholine vesicles. Transport activity was induced by adding ATP to the external medium. A voltage-sensitive dye was used to detect the ATP-driven potassium extrusion in the presence of valinomycin. The observed substrate-protein interactions of the reconstituted (Na+ + K+)-ATPase largely agree with that from native tissues. An agreement between ATP hydrolysis and transport activity is given for concentration dependences of sodium, potassium, magnesium and calcium ions. The only significant deviations were observed in the influence of pH. Protons were found to have different influence on transport, enzymatic activity and phosphorylation of the enzyme. The transport studies showed a twofold interaction of protons with the protein: competition with sodium at the cytoplasmic ion binding sites, a non competitive inhibition of transport which is not correlated with protein phosphorylation.

Animals↗
PubMed2000

Separation of chloride and sulfate ions in univalent and divalent cation forms from aqueous streams.

The precipitation and separation of chloride and sulfate in several cation forms (sodium, potassium, magnesium, calcium, strontium, and barium) from aqueous streams were studied using isopropylamine (IPA) and ethylamine (EA) as precipitation solvents. The precipitation fractions (P) of the tested chloride salts at 5000 and 10,000 ppm by both IPA and EA over the studied range of solvents volume ratio (V(R)) were relatively identical (18-60%) and their small variations were within their experimental uncertainty. The P of combined sulfate at 1000 ppm (56-99.5%) and chloride at 5000 ppm (28-62%) in the form of calcium by IPA over the studied range of V(R) were appreciably higher than the P of sulfate (10-98.5%) from calcium sulfate in the absence of calcium chloride, or the P of chloride (18-58%) from calcium chloride in the absence of calcium sulfate. The P of chloride from oil-field-produced waters at 106,654 ppm (20-88%) by both IPA and EA were higher than the P of chloride from diluted produced water at 20,000 (17-68%) and 10,000 ppm (16-65%) over the studied range of V(R). The small amounts of sulfate present in the produced waters (e.g., 435 ppm) were completely removed at V(R) of 0.1 (the first stage of precipitation). Consistency tests performed on the acquired data indicated a good level of experimental consistency. Two model equations (2-Suffix and 3-Suffix) derived from thermodynamic principles of solid-liquid equilibrium (SLE) criteria were employed to correlate the acquired data. While both equations were adequate for correlating the precipitation data, the 3-Suffix equation was more accurate.

Algorithms↗
PubMed1990

The stability of polypurine tetraplexes in the presence of mono- and divalent cations.

As with other guanine-rich sequences, poly[d(GGA)], poly[d(GA)] and poly[d(GAA)] probably form four-stranded or tetraplex structures. Thermal denaturation profiles were measured for these polymers at pH8 in the presence of Na+, NH4+, K+, Cs+, Mg2+, Ca2+ and Ba2+. For poly[d(GA)], Na+, NH4+, K+ stabilize the tetraplex to similar extents and the Tm increases with increasing ionic strength. In contrast the Tms with Mg2+, Ca2+ and Ba2+ are significantly different and reach maxima at about 5mM of cation. The tetraplex from poly [d(GAA)] behaves in a similar manner. Thermal denaturation profiles for poly[d(GGA)] yield transitions whose hyperchromicity depends both on the concentration and nature of the ion. A reversible cooperative transition is not observed at concentrations greater than 0.15M K+, 1mM Ca2+ or 0.3 mM Ba2+ and hysteresis is evident at some concentrations. These results are consistent with the idea that K+ and ions of a similar size can form a coordination complex with the 6-Keto group of eight guanines (G8-DNA). Unlike the tetraplex polymer this G8-DNA does not melt cooperatively.

Cations, Divalent↗
PubMed1996

Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed in mammalian cells.

1. Complementary DNAs for the ATP-gated ion channel subunits P2X1 (from human bladder) and P2X2 (from rat phaeochromocytoma (PC12) cells) were used to express the receptors in human embryonic kidney cells by stable transfection, and in Chinese hamster ovary cells by viral infection. 2. Membrane currents evoked by ATP were recorded by the whole-cell patch clamp method. The reversal potential of the current was measured with various intracellular and extracellular solutions and used to compute the relative permeability of the P2X receptor channels. 3. There was no difference between the two receptors with respect to their permeability to monovalent organic cations. The relative permeabilities (PX/PNa) were 2.3, 1.0, 1.0, 0.95, 0.72, 0.5, 0.29, 0.16, 0.04 and 0.03 for guanidinium, potassium, sodium, methylamine, caesium, dimethylamine, 2-methylethanolamine, tris(hydroxymethyl)-aminomethane, tetraethylammonium and N-methyl-D-glucamine, respectively (values for P2X2 receptor). 4. The calcium permeability of P2X1 receptors was greater than that of P2X2 receptors. Under biionic conditions (112 mM calcium outside, 154 mM sodium inside), PCa/PNa values were 3.9 and 2.2, respectively (corrected for ionic activities). 5. ATP-evoked currents in cells expressing the P2X2 receptor were strongly inhibited when the extracellular calcium concentration was increased (0.3-30 mM); the action of ATP could be restored by increasing the ATP concentration. ATP-evoked currents in cells expressing the P2X1 receptor were not inhibited by such increases in the extracellular calcium concentration.

Adenosine Triphosphate↗
PubMed1985

Magnesium transport in murine S49 lymphoma cells: pharmacology and divalent cation selectivity.

The murine S49 lymphoma cell transports Mg2+ by a system distinct from systems responsible for Ca2+ influx (J. Physiol. London 337: 351-371, 1983). We have now determined the ability of various cations, anions, and drugs to modulate Mg2+ influx. Neither sulfate, nitrate, phosphate, nor bicarbonate altered Mg2+ influx. Among cations only T1+, Ba2+, Zn2+, Mn2+, Sc3+, and La3+ potently inhibited Mg2+ influx without causing obvious cell toxicity. Seventeen other cations were ineffective at maximal nontoxic concentrations. T1+ inhibition (Ki = 300 micron) is noncompetitive and apparently derives from its ability to dissipate membrane potential. The noncompetitive nature of and the rather poor inhibition constants for Ca2+ (Ki approximately equal to 5 mM) and Mn2+ (Ki = 200 micron) indicate that neither cation is an effective physiological antagonist of Mg2+ influx. Only Ba2+ exhibited competitive inhibition of Mg2+ influx (Ki = 1 mM). Cisplatin and Ca2+ channel antagonists also did not inhibit Mg2+ influx. These data further differentiate Mg2+ transport systems from those for Ca2+. In addition, the selectivity series for group IIa cation inhibition of influx (Mg2+ greater than Ba2+ much greater than Ca2+ greater than or equal to Sr2+) has not been observed previously in biological systems and is indicative of a very high anionic field strength at the Mg2+ recognition site.

Animals↗