PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Cations, Divalent”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 577 records · Page 32Linked to original sources
PubMed1975

Growth and mineral metabolism in very low birth weight infants. II. Effects of calcium supplementation on growth and divalent cations.

Infants of two groups, one of 16, one of 14 infants, who weighed less than 1.3 kg at birth (mean 1.01 +/- 0.05 kg), were studied from age 14 days until they reached 1.8 kg body weight. Infants were pair-matched for gestational age and birth weight and one member was randomly allocated to two treatment groups. Infants in group A received no calcium supplement and those in group B received calcium lactate, 800 mg/kg/24 hr hr, in divided doses with each feed. All were fed "Improved" SMA, 200 ml/kg/24 hr, 160 cal/kg/24 hr, and were given a multivitamin preparation containing 500 IU vitamin D2/dose. The infants' weekly length gain did not differ between groups (1.08 +/- 0.04 cm/week vs 1.11 +/- 0.04 cm/week; mean +/- SEM). Mean weight and head cercumference increments also were similar (group A, 163 +/- 6 g/week; 1.12 +/- 0.03 cm/week; group B, 170 +/- 6 g/week and 1.18 +/- 0.03 cm/week). An increase in blood pH from 7.33 +/- 0.01 to 7.41 +/- 0.01 (P less than 0.01) in group A babies was associated with a decrease in PCO2 from 44.2 +/- 1.0 to 38.9 +/- 1.4 mm Hg. Values remained unchanged with age in group B babies...

Birth Weight↗
PubMed1988

Corticotropin-releasing factor receptors in mouse spleen: identification, autoradiographic localization, and regulation by divalent cations and guanine nucleotides.

The radioligand [125I-Tyro]ovine CRF [( 125I] oCRF) was used to identify, characterize, and localize CRF receptors in a crude homogenate of mouse spleen. The binding was linear with increasing membrane protein concentration, saturable, and of high affinity. Scatchard analysis of [125I]oCRF saturation curves revealed a high affinity component with an apparent dissociation constant of 0.26 nM and a maximum receptor concentration of 8.74 fmol/mg protein. The relative affinities of various CRF-related and unrelated peptides at the [125I]oCRF-binding site in spleen correlate well with their reported potencies in eliciting ACTH release from the pituitary and their relative affinities for CRF receptors in brain. Consistent with a coupling of splenic CRF receptors to a guanine nucleotide regulatory protein, the binding of [125I]oCRF was increased by magnesium ions and decreased by guanine nucleotides in both mouse spleen and brain. Saturation analysis of [125I]oCRF binding at 0, 1, and 10 mM MgCl2, 10 mM MgCl2 plus 200 microM GTP, and 10 mM MgCl2 plus 50 microM 5'-guanylimidodiphosphate indicated that high affinity [125I]oCRF binding in both brain and spleen requires Mg2+; however, subtle differences were observed in the degree of sensitivity and mechanisms by which Mg2+ and guanine nucleotides regulated specific binding of [125I]oCRF to brain and spleen. Autoradiographic studies indicated that [125I]oCRF-binding sites were primarily localized to the red pulp and marginal zone regions of the spleen, which are known to contain high concentrations of macrophages. The absence of [125I]oCRF-binding sites in the periarteriolar and peripheral follicular white pulp regions suggests that neither T nor B lymphocytes have specific CRF-binding sites. In summary, we have identified a high affinity, magnesium-dependent, and guanine nucleotide-sensitive binding site for CRF in mouse spleen which appears to be localized primarily in splenic macrophages.

Animals↗
PubMed2000

The effect of divalent cations on the membrane properties and pharmacokinetics in rat of the lipid A analogue E5531.

To obtain information on the effects of Ca2+ on the membrane properties of the lipid A analogue E5531, we have determined the aggregate size, zeta potential, membrane fluidity, micropolarity and permeability of the E5531 membrane as a function of Ca2+ levels. Within the molar ratios of [Ca2+]/[E5531] = 1 and 3, Ca2+ increased the zeta potential of the E5531 membrane but had no effect on aggregate size (approximately 20 nm). Within the above ratios, Ca2+ decreased the membrane fluidity, as measured by micropolarity of E5531 and increased the phase transition temperature. The pharmacokinetics in rats for these samples with different membrane fluidity, prepared by changing the pre-dose formulation concentration of Ca2+, was determined and a correlation between membrane fluidity and pharmacokinetics was clearly observed. It thus appears that Ca2+ effects the membrane fluidity of E5531 as well as its pharmacokinetics in rats.

Animals↗
PubMed2003

Inhibition of Mg2+-dependent adhesion of polymorphonuclear leukocytes by serum hemopexin: differences in divalent-cation dependency of cell adhesion in the presence and absence of serum.

Circulating and nonadherent polymorphonuclear leukocytes (PMNs) become activated to attain adhesive state in an integrin-dependent manner by various stimuli, and perform a variety of microbicidal functions such as phagocytosis and superoxide production. We found that, in the absence of serum, a physiological concentration of hemopexin has a strong inhibitory action on Mg(2+)-dependent adhesion of PMA-activated PMNs to fibrinogen- and serum-coated surfaces. Under these conditions, Ca(2+) had no effect on Mg(2+)-dependent adhesion or the adhesion-inhibitory activity of hemopexin. In contrast, PMNs suspended in serum containing sufficient amounts of hemopexin to inhibit adhesion showed marked adherence, which was inhibited by EGTA. Next, we prepared a small-molecule fraction of serum by ultrafiltration followed by boiling. PMA-activated PMNs was found to adhere in the presence of both hemopexin and the small-molecule fraction, and the adhesion was enhanced by exogenous Ca(2+). EGTA abolished the effect of the small molecule fraction. The data suggest that serum contains adhesion-promoting factor(s) which allows PMNs to adhere despite the presence of hemopexin and that Ca(2+) is required for adhesion-promoting activity. Further study of hemopexin may provide clues for new therapeutic strategies aimed at interfering with PMN adhesion to control inflammation and tissue injury.

Animals↗
PubMed1979

Divalent cation transport in kidney slices. I. Properties of calcium transport in slices of rat kidney cortex and the effects of diuretics.

Correlative studies on transports of Ca2+ and Na+ and the properties of Ca2+ transport were carried out in rat kidney cortex slices. Ouabain had no effect on the Ca2+ transport but did inhibit the Na+ transport extensively. With addition of 2,4-dinitrophenol to the incubation medium, or under the anaerobic conditions, the effluxes of Ca2+ and Na+ were inhibited while the Ca2+ influx was enhanced significantly. Sulfhydryl inhibitors such as ethacrynic acid, mersalyl and p-chloromercuribenzoic acid suppressed Ca2+ efflux and stimulated Ca2+ influx. When the slices of kidney cortex were treated with these inhibitors, there was a reduction in the content of cellular ATP. The present results suggest that Ca2+ transport may be partly independent of Na+ transport, and that Ca2+ efflux may require energy-yielding processes.

Adenosine Triphosphate↗
PubMed1980

Divalent cation transport in kidney slices II. Magnesium transport in kidney cortex slices and effects of diuretics.

We examined the properties of Mg2+ transport in rat kidney cortex slices and the effects of diuretics were also studied. Incubation with 1 mM 2,4-dinitrophenol, or under anaerobic conditions, sharply inhibited Mg2+ influx, while markedly stimulating Mg2+ efflux. Under conditions of hypothermia, partial inhibition of Mg2+ influx and significant enhancement of Mg2+ efflux were observed. Mg2+ influx was not affected by ouabain, by altering CaCl2 concentration in the medium, or by a change of Ca2+ content in the slices. Incubation with 1 mM ethacrynic acid or mersalyl depressed Mg2+ influx and stimulated Mg2+ efflux, p-chloromercuribenzoic acid (5 X 10(-4) M) had a similar effect and furosemide had no effect on Mg2+ transport. These results suggest that Mg2+ influx is mediated by an energy-dependent process which is dissociated from ouabain-sensitive Na+ transport and Ca2+ flux. Sulfhydryl groups may be involved in the process of Mg2+ influx.

Animals↗
PubMed1982

Inactivation and reactivation of rat liver 3-hydroxy-3-methylglutaryl-CoA-reductase phosphatases: effect of phosphate, pyrophosphate and divalent cations.

Incubation of four purified rat liver HMG-CoA-reductase phosphatases (Gil, G., Sitges, M. and Hegardt, F.G. (1981) Biochim. Biophys. Acta 663, 211-221) with Mn2 or Mg2 caused a concentration-dependent activation of enzyme activities. The maximum effect for Mn2 was at 5 mM for all phosphatases. Fe2 caused inactivation only in reductase phosphatases IIa and IIb. Ca2 10 mM showed a slight effect of inactivation. Phosphate, pyrophosphate and adenine nucleotides inhibited the four reductase phosphatases, this process being concentration-dependent. cAMP did not inhibit the four phosphatases at all in the range of 0.01-8 mM. Preincubation of reductase phosphatases with PPi and subsequent dilution did not diminish the inactivation effect, showing that this ion inhibits the enzyme prior to the binding to the substrate. Phosphorylated sugars, but not free sugar, inactivated the four reductase phosphatases. PPi-inactivated enzymes were reactivated by Mg2 or Mn2, this process being time-dependent. The four phosphatases had different patterns of reactivation. Phosphatases Ib and IIb (low-molecular mass forms) were shown to be different enzymes as judged by: their divergent behaviour when inhibited with Fe2; their PPi response; kinetics of reactivation by Mg2 or Mn2 or PPi-inactivated enzymes; and thermal stability. A metalloenzyme character is suggested for reductase phosphatases.

Adenine Nucleotides↗
PubMed1993

Blockade of sodium channels by divalent cations in rat gastric smooth muscle.

Using the whole-cell clamp method, the Na+ channel currents in smooth muscle cells of the rat stomach fundus were studied. After blocking K+ channel currents, step depolarizations from the holding potential of -90 mV induced fast-activating, fast-inactivating inward currents (fast currents), which were followed by slowly-inactivating inward currents (slow currents). Using a nominally Ca(2+)-free bath solution, depolarization steps up to +20 mV induced only the fast currents, and depolarization steps to over +30 mV evoked outward currents. The fast current was inhibited by tetrodotoxin (TTX) or by removal of external Na+, thereby indicating that this was a Na+ channel current. The outward current was inhibited by nifedipine or by 0.1 mM Ca2+, thus, this current was a Cs+ current passing through Ca2+ channels. In the presence of 5 mM Ni2+, the Na+ current was reduced to about 15% of the control. When the rightward shift in the I-V relations was taken into account, the Na+ current was about 30% of the control. Mn2+ was less potent than Ni2+, and Cd2+ was more potent than Ni2+ or Mn2+, as a Na+ channel blocker. Plots of peak current amplitude, as a function of Cd2+ concentration, showed that one Cd ion was required to block one Na+ channel (KD: 55.7 microM). Thus, properties of the Na+ channel found in this smooth muscle cells are similar to those in vertebrate cardiac cells, in that the channel is relatively resistant to TTX and is sensitive to Cd2+.

Animals↗
PubMed1989

Effect of divalent cations on the structure of dipalmitoylphosphatidylcholine and phosphatidylcholine/phosphatidylglycerol bilayers: an 2H-NMR study.

The interactions of CaCl2 or MgCl2 with multilamellar phospholipid bilayers were studied by 2H-NMR. Two model membrane systems were used: (1) dipalmitoylphosphatidylcholine (DPPC) bilayers and (2) bilayers composed of a mixture of phosphatidylcholine and phosphatidylglycerol at a molar ratio of 5:1. Addition of 0.25 M CaCl2 to DPPC bilayers resulted in significant uniform increase of the order parameters of the lipid side chains; the effect of 0.25 M MgCl2 was insignificant. Both phosphatidylcholine and phosphatidylglycerol components of the mixed bilayers were affected by the presence of 0.25 M CaCl2 and, to a much smaller degree, by MgCl2. The addition of Ca2+ induced significantly larger increase of the order parameters of the phosphatidylcholine component. The results are consistent with the long-range effects of Ca2+ binding on the packing of the lipid membranes.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1989

Calmodulin-dependent adenylate cyclase activity in rat cerebral cortex: effects of divalent cations, forskolin and isoprenaline.

The role of calcium-calmodulin (Ca2+-CaM) in the modulation of beta-adrenergic adenylate cyclase activity in rat cerebral cortex has been studied. In addition, the effects of manganese (Mn2+) and forskolin on CaM-dependent enzyme activity were investigated. At 2 mM magnesium (Mg2+) low concentrations of Ca2+ stimulated the enzyme activity (Ka 0.25 +/- 0.08 microM), whereas higher Ca2+ levels (greater than 2 microM) inhibited the activity. No activating effect of Ca2+ was observed in CaM-depleted membranes, but the inhibitory effect persisted and the stimulatory action of Ca2+ could be restored by addition of exogenous CaM. The ability of Ca2+ to activate the enzyme was reduced by increasing concentrations of Mg2+. At 10 mM Mg2+ the apparent Ka of Ca2+ was 0.55 +/- 0.16 microM and half-maximal inhibition was observed at 80-120 microM Ca2+. A synergistic effect was observed between Ca2+ and isoprenaline on the adenylate cyclase activity. Calcium did not alter the apparent Ka of isoprenaline (0.9 +/- 0.27 microM) and isoprenaline did not change the apparent Ka of Ca2+. However, isoprenaline decreased the apparent Ka of CaM; 0.11 +/- 0.07 micrograms vs. 0.32 +/- 0.1 micrograms (0.5 ml assay mixture)-1, with and without isoprenaline, respectively. A synergistic effect was also observed between Ca2+ and forskolin, but no change in their apparent Ka values was found. Furthermore, Mn2+ was found to activate the enzyme through CaM. These data demonstrate that Ca2+ -CaM potentiates beta-adrenergic adenylate cyclase activity and thus is able to modulate neurotransmitter stimulation in cortex. Furthermore, both forskolin and Mn2+ affect CaM-dependent enzyme activity. Forskolin potentiates Ca2+-CaM stimulation, while Mn2+ increases the activity by activating the enzyme through CaM.

Adenylyl Cyclases↗