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PubMed1979

Anionic detergents as divalent cation ionophores across black lipid membranes.

Three ionic detergents commonly used in membrane-bound protein isolation and reconstitution experiments, SDS, cholate, and DOC, are shown to act as divalent cation ionophores when incorporated into black lipid membranes made from either oxidized cholesterol or a mixture of phosphatidylcholine and cholesterol (PC/cholesterol = 5:1 mg). At a concentration greater than or equal to 1 microM, SDS shows large selectivity differences between cations and anions and among the different cations tested (Ba2+, Ca2+, Sr2+, Mg2+, and Mn2+). Deoxycholate and cholate at concentrations greater than 4 X 10(-4) M and 10(-3) M, respectively, also act as divalent cation ionophores. The selectivity sequence measured for these two detergents is evidence for a strong ionic interaction between the divalent cation and the anionic charged groups on the detergent. In the case of cholate, the conductance depends on the third or fourth power of the cholate concentration and shows a linear dependence on CaCl2 concentration. The conductance for deoxycholate depends onthe sixth or seventh power of the DOC concentration and is also linearly dependent on the CaCl2 concentration. In an oxidized cholesterol black lipid membrane in the presence of 5 mM CaCl2, small concentrations of LaCl3 (less then 1 microM) inhibit the ionophoric activity of each of the detergents tested. Evidence is presented to show that this inhibitory effect is a nonspecific effect on oxidized cholesterol BLM's, and is not due to a direct effect of La3+ on detergent-mediated transport.

Cations, Divalent↗

PubMed1991

Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin.

We have characterized a unique divalent cation binding site on bacteriorhodopsin which controls the blue-to-purple transition in the purple membrane of Halobacterium halobium. To identify this site we first showed the correlation between the binding of one Ca2+ per bacteriorhodopsin and the amount of blue membrane converted to purple membrane. When the free Ca2+ was reduced below 1 microM, and the pH was set below 5.0 with 0.5 mM citrate, only binding to this high-affinity site was observed, and we could separate its effect from the effect of other divalent cations binding to the membrane under other conditions. Second, the titration of purple membrane showed that protons are taken up in two distinct steps, about 13 with a pKa of 4-5 and an additional 2 protons with a pKa of 2.75, in 5 mM MgSO4. The latter is identical to the pKa for the purple-to-blue transition in 5 mM MgSO4. Taken together, these observations strongly suggest a direct role for cations in the regulation of the bacteriorhodopsin color under normal conditions. We have also found that the intrinsic pKa for the purple-to-blue transition is about 2.05, suggesting this is the pKa of the group or groups that, when protonated, lead to the blue membrane. Previously published data can now be interpreted to suggest that the cation regulates an active site near the retinal chromophore. A binding site for the divalent cation that includes Asp-212 and interactions with the protonated Schiff base, Asp-85, Tyr-57, Tyr-185, and Arg-82 is proposed.

Journal Article↗

PubMed1981

The influence of divalent cations on the stability of human rotavirus.

The influence of divalent cations on the stability of human rotavirus was investigated using the indirect immunofluorescence (FA) technique in LLC-MK2 cells to titrate infectivity. Rotavirus infectivity was stabilized by calcium and strontium ions in solution but not by magnesium ions. Rotavirus isolates were found to be much less stable at 37 degrees C than at + 4 degrees C or 20 degrees. A study of virus morphology at intervals during the course of the experiment and treatment with the chelating agents EDTA and EGTA suggests that loss of infectivity coincides with the removal of the outer capsid layer and that calcium may be required to maintain virus integrity.

Animals↗

PubMed1976

Control of tumbling in bacterial chemotaxis by divalent cation.

Chemotaxis is migration of organisms to higher concentrations of attractant or lower concentrations of repellent. Understanding the switch than controls whether the flagella rotate counterclockwise for swimming or clockwise for tumbling (thrashing about without making much forward progress) is central to understanding chemotaxis of peritrichous bacteria, since chemotaxis results from selective suppression of tumbles. Depletion of divalent cation by chelating agents in the presence of A23187, an ionophore that conveys divalent cation across membrane, causes incessant tumbling in Bacillus subtilis. Small additions of MgCl2 prevent this tumbling. In this tumbling condition, the bacteria which normally swim extensively when given attractant, do not respond even to 10 mM alanine, a strong attractant. MnCl2, by contrast to others potentiated by the ionophore. Permanent cations, including tetraphenylarsonium ion and triphenylmethylphosphonium ion, cause permanent swimming, even in the presence of A23187 and chelating agents. We propose that divalent cation, probably Mg2+ ion, binds to the switch to cause swimming and that, in the absence of divalent cation at the switch, the bacterium tumbles.

Alanine↗

PubMed1976

Regulation of glutaminase B in Escherichia coli. III. Control by nucleotides and divalent cations.

Glutaminase B from Escherichia coli is modulated by nucleotides and divalent cations. ATP and ADP inhibit glutaminase B whereas AMP and divalent cations activate it. Inhibition and activation required preincubation of the nucleotides with glutaminase B at 4 degrees. Mg2+, Mn2+, and Ca2+ activated the enzyme and prevented the inhibition by ATP. Dialysis in the presence of an activator ligand reversed the ATP inhibition of glutaminase B. The modulation of glutaminase B by energy charge is similar to that observed with other catabolic enzymes. We suggest that a pattern of reciprocal regulation of glutaminase B and glutamine synthetase by adenine nucleotides prevents the formation of a "futile cycle" of amide synthesis and degradation.

Calcium↗

PubMed1995

Effects of divalent cations on exocytosis and endocytosis from single mouse pancreatic beta-cells.

1. The effects of the divalent cations Ca2+, Ba2+ and Sr2+ on exocytosis and endocytosis from single isolated mouse pancreatic beta-cells were investigated by monitoring changes in cell capacitance. 2. The immediate increase in capacitance elicited by a single depolarization from -70 to +20 mV was dependent on the divalent cation species, with Ca2+ (8.2 +/- 1.1 fF pC-1) > Ba2+ (1.0 +/- 0.2 fF pC-1) > Sr2+ (0.7 +/- 0.2 fF pC-1) in perforated-patch recordings. 3. In Ba2+ solutions alone there was subsequently an additional slow increase in capacitance (to 4.3 +/- 1.1 fF pC-1). This second phase of exocytosis was unaffected by preincubation with colcemid (20 microM, 45 min) or cytochalasin D (10 microM, 15 min), suggesting that interaction of secretory granules with microtubules or microfilaments is not involved. 4. An increase in cell capacitance was elicited by depolarization in Ba2+ solutions when intracellular Ca2+ was buffered with 10 mM EGTA. Infusion of the beta-cell with Ba2+ also stimulated exocytosis although the rate was much slower (1.1 +/- 0.2 fF s-1; 8 microM free Ba2+) than for Ca2+ (39 +/- 5 fF s-1; 2 microM free Ca2+). These data indicate that Ba2+ does not evoke secretion by promoting Ca2+ release from internal stores. 5. The lower efficacy of Ba2+ in supporting exocytosis may be related to the fact that this cation does not activate calmodulin-dependent processes and the slow second phase of secretion may result from this ion being removed only slowly from the cytoplasm. 6. Endocytosis was faster in Sr2+ than in Ca2+ or Ba2+ solution, and the speed increased when the external concentration of all three divalent cation species was raised. The ability of Ba2+ to support endocytosis suggests calmodulin-dependent processes are not involved. These data suggest membrane retrieval is regulated differently from exocytosis in beta-cells.

Animals↗

PubMed1975

Effects of divalent cations on binding of aminoglycoside antibiotics to human serum proteins and to bacteria.

Binding of gentamicin and related deoxystreptamine-containing aminoglycoside antibiotics to proteins in human serum can vary significantly with changes in experimental conditions. The concentrations of divalent cations are important variables, and binding increases progressively as the concentrations of calcium and magnesium decrease. Maximal binding of deoxystreptamine-containing aminoglycosides to human serum is approximately 70% in the absence of divalent cations. The binding of (3)H-labeled gentamicin to Pseudomonas aeruginosa increases and its bactericidal activity against P. aeruginosa is enhanced in the absence of divalent cations. In contrast, binding of (3)H-labeled gentamicin to Escherichia coli and bactericidal activity against E. coli do not vary significantly in the presence and in the absence of divalent cations. Interference with uptake of gentamicin provides a plausible explanation for the observation that the minimal inhibitory concentration of gentamicin for P. aeruginosa increases as the concentration of calcium or magnesium in bacteriological media increases. Although significant binding of deoxystreptamine-containing aminoglycosides to plasma proteins does not occur under normal physiological conditions in man, the possibility remains that variations in protein binding of these aminoglycosides might be significant under pathological conditions.

Aminoglycosides↗

PubMed1976

The effect of mono- and divalent cations on the quantum yields for electron transport in chloroplasts.

We have previously shown (Gross, E.L. and Hess, S.C. (1973) Arch. Biochem. Biophys 159, 832-836) that low concentrations of monovalent cations (3-10 mM) caused changes in chlorophyll a fluorescence indicative of a transfer of excitation energy from Photosystem II to Photosystem I. These effects were reversed by divalent cations or higher concentrations of monovalent cations. In this study, we have examined the effects of cations on the relative quantum yields for Photosystem II (dichlorophenolindophenol reduction) and Photosystem I (diphenylcarbazone disproportionation) with the following results. (1) Low concentrations of monovalent cations decreased the quantum yield for dichlorophenolindophenol reduction and increased that for diphenylcarbazone disproportionation. These results confirm that cations promote excitation energy transfer to Photosystem I. (2) Higher concentrations of monovalent cations (30-100 mM) had no effect on electron transport. Therefore, the increases in chlorophyll a fluorescence observed at these concentrations may be due to a decrease in the rate constant for radiationless decay. (3) In the absence of Tricine, divalent cations also promote energy transfer from the light harvesting pigments to Photosystem I. However, a direct inhibition of Photosystem I and divalent cations can reverse the Tricine effects.m II photochemistry cannot be rules out. (4) Tricine biases the system in favor of Photosystem I and divalent cations can reverse the Tricine effects.

Calcium↗

PubMed1994

Interaction of divalent cations with germ cell specific sulfogalactosylglycerolipid and the effects on lipid chain dynamics.

Sulfogalactosylglycerolipid (SGG) is a sulfoglycolipid found ubiquitously in the plasma membrane of mammalian male germ cells. Although its exact cellular function(s) is unknown, it is speculated that SGG may play a role in cation transport, which may be important in sperm-egg interaction. Given the significant role of Ca2+ in many fertilization-related events, the purpose of this study was to determine whether Ca2+ interaction with the negatively charged sulfate group of SGG results in changes to the SGG lipid chain molecular dynamics and to compare these lipid dynamics with those resulting from Na+, Mg2+, or Sr2+ interaction with SGG. Pressure-tuning Fourier transform infrared spectroscopy was used in this study. The results obtained showed that all three divalent cations interacted electrostatically with the sulfate moiety of hydrated SGG, although with varying degrees of strength. It was found that the hydrocarbon chains of hydrated SGG-Na+ multilamellar bilayers were interdigitated, thus increasing disorderedness of the terminal CH3 group of the hydrocarbon chains. The presence of each of the three divalent cations abolished this interdigitation state. Presumably, this is through the cross-linking interaction of each divalent cation with the sulfate groups of neighboring lipid molecules. Moreover, divalent cation interaction was found to increase the lipid chain dynamics of SGG, with Mg2+ inducing the greatest chain disorder followed by Ca2+ and then Sr2+. An increase in chain disorder would increase the bilayer fluidity. Such a phenomenon may prove relevant to the changes observed in the sperm plasma membrane during fertilization-related events.

Animals↗

PubMed1994

Effect of divalent cations on the molecular structure of the GroEL oligomer.

Structural analysis, by chemical cross-linking with glutardialdehyde (GA), and by urea denaturation, was carried out for the chaperonin oligomer GroEL14 from Escherichia coli. The cross-linking reaction of GroEL14 presents two phases: a rapid intralayer cross-linking reaction, which first occurs between the monomers of individual GroEL7 heptameric rings, and a slow interlayer cross-linking reaction, which later occurs between the two stacked heptameric rings of the GroEL14 oligomer. The biphasic behavior of the cross-linking reaction indicates that the surfaces of contact between GroEL monomers within individual heptameric rings are more extensive than the surfaces of contact between the two GroEL7 rings of the oligomer. Millimolar amounts of the divalent cations Mg2+, Mn2+, Ca2+, or Zn2+, but not of monovalent ions, increase the velocity of both intra- and interlayer cross linking. Divalent cations increase the stability of the native GroEL14 oligomer in urea. In contrast, Mg2+ activates ATP hydrolysis by GroEL14, with an activation constant in the micromolar range, while Ca2+ does not significantly assist ATP hydrolysis. It is concluded that divalent cations affect the structure of GroEL14 in particular the contacts between monomers within the GroEL7 heptameric layers. The effect of divalent cations on the structure of the chaperonin molecule is quantitatively and qualitatively distinct from that of magnesium ions on the chaperonin ATPase activity.

Adenosine Triphosphatases↗

PubMed1999

Divalent cations modulate N-methyl-D-aspartate receptor function at the glycine site.

The modulation of the N-methyl-D-aspartate (NMDA) receptor (NMDAR) by divalent cations was examined using (+)-5-methyl-10, 11-dihydro-5H-dibenzo[a,d]cyclohepten 5,10-imine maleate ([(3)H]MK-801) binding as a functional indicator of NMDAR function. Ca(2+) and Mg(2+) produce a biphasic effect on the binding of [(3)H]MK-801 to the NMDAR channel in extensively washed adult rat brain membranes. Concentrations of Ca(2+) and Mg(2+) between 1 and 600 microM potentiate binding, but higher concentrations inhibit binding. The potentiating effect of Ca(2+) and Mg(2+) on [(3)H]MK-801 binding is due to an increase in the maximal number of binding sites (B(max)) with no effect on binding affinity (K(d)). Ca(2+)- and Mg(2+)induced potentiation is the result of an apparent increase in the affinity of the NMDAR for glycine. The ontogeny of NMDAR potentiation by Ca(2+) and Mg(2+) was also investigated. The number of [(3)H]MK-801 binding sites associated with divalent cation potentiation are present at low levels shortly after birth, and increase to peak level at 17 days of age before declining to adult levels. The potency of Ca(2+) and Mg(2+) to stimulate [(3)H]MK-801 binding did not change as a function of age. Lead (Pb(2+)) and zinc (Zn(2+)), potent inhibitors of the NMDAR, antagonize NMDAR potentiation by Ca(2+) and Mg(2+). These findings indicate that divalent cations differentially regulate NMDAR function by modulation of the glycine site. The NMDAR glycine site may be important in the regulation of glutamatergic neurotransmission by physiologically and toxicologically relevant cations.

Animals↗

PubMed2005

Effect of divalent cations on ion fluxes and leaf photochemistry in salinized barley leaves.

Photosynthetic characteristics, leaf ionic content, and net fluxes of Na(+), K(+), and Cl(-) were studied in barley (Hordeum vulgare L) plants grown hydroponically at various Na/Ca ratios. Five weeks of moderate (50 mM) or high (100 mM) NaCl stress caused a significant decline in chlorophyll content, chlorophyll fluorescence characteristics, and stomatal conductance (g(s)) in plant leaves grown at low calcium level. Supplemental Ca(2+) enabled normal photochemical efficiency of PSII (F(v)/F(m) around 0.83), restored chlorophyll content to 80-90% of control, but had a much smaller (50% of control) effect on g(s). In experiments on excised leaves, not only Ca(2+), but also other divalent cations (in particular, Ba(2+) and Mg(2+)), significantly ameliorated the otherwise toxic effect of NaCl on leaf photochemistry, thus attributing potential targets for such amelioration to leaf tissues. To study the underlying ionic mechanisms of this process, the MIFE technique was used to measure the kinetics of net Na(+), K(+), and Cl(-) fluxes from salinized barley leaf mesophyll in response to physiological concentrations of Ca(2+), Ba(2+), Mg(2+), and Zn(2+). Addition of 20 mM Na(+) as NaCl or Na(2)SO(4) to the bath caused significant uptake of Na(+) and efflux of K(+). These effects were reversed by adding 1 mM divalent cations to the bath solution, with the relative efficiency Ba(2+)>Zn(2+)=Ca(2+)>Mg(2+). Effect of divalent cations on Na(+) efflux was transient, while their application caused a prolonged shift towards K(+) uptake. This suggests that, in addition to their known ability to block non-selective cation channels (NSCC) responsible for Na(+) entry, divalent cations also control the activity or gating properties of K(+) transporters at the mesophyll cell plasma membrane, thereby assisting in maintaining the high K/Na ratio required for optimal leaf photosynthesis.

Cations, Divalent↗

PubMed1988

Taurine and nifedipine protect retinal rod outer segment structure altered by removal of divalent cations.

A protective effect of taurine on morphological alterations induced in isolated ROS by remotion of divalent cations is described. ROS damage is not observed when sodium or chloride is replaced by impermeant ions or in the presence of nifedipine (10 microM). An increased accumulation of 22Na but not of 36Cl occurs in retinas incubated in divalent cation free medium. Taurine (5-25 mM) provides a concentration-dependent protection to ROS structure. Taurine is also able to reduce the increased 22Na influx to control values. These results suggest a protective action of taurine probably involving an interaction with calcium sites on ROS membranes which regulate sodium permeability.

Amino Acids↗

PubMed1990

Selective alterations in presynaptic cytomatrix protein organization induced by calcium and other divalent cations that modulate exocytosis.

Rises in intracellular calcium cause several events of physiological significance, including the regulated release of neuronal transmitters. In this study, the effects of divalent cations on the structural organization of cytomatrix in presynaptic terminals was examined. [35S]Methionine-radiolabeled guinea pig retinal ganglion cell cytomatrix proteins were axonally transported [in slow component b (SCb) of axonal transport] to the neuron terminals in the superior colliculus. When the peak of radiolabeled cytomatrix proteins reached the terminals, synaptosomes containing the radiolabeled cytomatrix proteins were prepared. Approximately 40% of each SCb protein was soluble after hypoosmotic lysis of the radiolabeled synaptosomes in the presence of divalent cation chelators. Lysis of synaptosomes in the presence of calcium ions over a range of concentrations, however, caused a dramatic decrease in solubility of the presynaptic SCb proteins. The cytoplasmic effects may result from a calcium-dependent condensation of cytoplasm around presynaptic terminal membrane systems. There are two major presynaptic SCb proteins (at 60 and 35 kDa), that exhibited exceptional behavior: they remained as soluble in the presence of calcium as under control conditions, suggesting that they were relatively unaffected by the mechanism causing the decrease in SCb protein solubility. Also examined were the effects of other alkaline earth and transition metal divalent cations on the presynaptic SCb proteins.

Animals↗

PubMed1991

Divalent Cations Modulate the Inhibitory Substrate Properties of Murine Glia-derived J1-160 and J1-180 Extracellular Matrix Glycoproteins for Neuronal Adhesion.

J1-160 and J1-180 are developmentally late appearing J1 extracellular matrix glycoproteins derived from oligodendrocytes. They prevent adhesion of neurons (but not of astrocytes or fibroblasts) when offered as a substrate in mixture with laminin (Pesheva et al., J. Cell Biol., 109, 1765 - 1778, 1989). In the present study we have examined the influence of divalent cations on the inhibitory substrate properties of J1-160/180 glycoproteins towards adhesion of neurons. By metal chelate affinity chromatography, we show that J1-180, but not J1-160, binds Ca2+, while both J1 components are capable of binding Zn2+ and other divalent metal ions. Divalent cation binding was observed by gel filtration, aggregation assays with coated latex beads and electron microscopic examination to elicit aggregation of the molecules. Divalent cation binding also affects their non-permissive substrate properties towards neurons from early postnatal mouse cerebellum. Without divalent cations, J1-160 and J1-180 are inhibitory for substrate adhesion of neurons independently of the adhesive substrate present (laminin or poly-l-lysine). This effect is neutralized when J1-180 is preincubated with Ca2+ or Zn2+ prior to coating as substrate. In contrast, preincubation with Ca2+ ions does not affect the inhibitory substrate properties of J1-160 under these conditions. These observations show that J1-160/180 molecules may undergo self-aggregation in a divalent cation-dependent mechanism, which correlates with the neutralization of their inhibitory effect on neuronal adhesion. The aggregation state of the molecules may thus influence the process of myelination by a homophilic binding mechanism and determine the effectiveness of neurite extension during central nervous system development and under traumatic conditions in the adult.

Journal Article↗

PubMed2002

Atomic force microscopy study of the effects of Mg(2+) and other divalent cations on the end-to-end DNA interactions.

Atomic force microscopy (AFM) was applied to directly visualize the end-to-end DNA interaction mediated by magnesium cations. We took advantage of the APS-mica, allowing the preparation of samples in a broad range of monovalent and divalent cations to separate the effects of Mg(2+) and Na(+) cations on the interaction of restriction DNA fragments with cohesive end. The AFM data clearly show that DNA restriction fragments with cohesive ends form substantial amount of circles in the presence of Mg(2+) cations, suggesting that Mg(2+) cations stabilize the interaction of cohesive ends. This effect depends on the MgCl(2) concentration, so that the yield of circles approaches 18% in the presence of 50 mM MgCl(2). Furthermore, we demonstrate that this conferred cohesive end stability is specific for divalent cations, as substitution of MgCl(2) with NaCl leads to a near complete loss of cohesive end stability. We further demonstrate that cohesive end stabilization is achieved by substituting Mg(2+) with Ca(2+), Mn(2+), or Zn(2+). The data obtained suggest that the end stabilization mediated by divalent cations is primarily the result of inter-base interactions rather than bridging of phosphate moieties.

Cations, Divalent↗

PubMed1980

Influence of monovalent and divalent cations on the surface area of phosphatidylglycerol monolayers.

A theory is presented on the electrostatic properties of the surface area of phosphatidyl-glycerol monolayers spreading at an air-water interface in the presence of monovalent and divalent cations. In the present theory, the adsorption of monovalent and divalent cations to the membranes is taken into account, besides the dissociation of protons, as possible cause of the change of surface charge density with the variation of pH or ion concentrations. It is also pointed out that, in the presence of structure-making ions such as Li+ and Na+, the nearest-neighbour interactions between proton dissociation sites become important for the monolayers in the gel state to yield a sharp expansion of the surface area with the increase of pH. The present theory shows quantitative agreements with previously-observed data.

Cations, Divalent↗

PubMed1978

The adsorption of divalent cations to phosphatidylcholine bilayer membranes.

Electrophoretic mobility and 31P NMR measurements were combined to test whether the combination of the Henry, Boltzmann and Grahame equations is capable of describing the adsorption of divalent cations of phosphatidylcholine membranes. Cobalt was chosen for this study because, of all the common divalent cations, its effects on the 31P NMR spectrum of phosphatidylcholine membranes are easiest to interpret. Both the 31P NMR data on the adsorption of cobalt and the zeta potential data calculated from the electrophoretic mobility in the presence of cobalt are well described by the combination of these three equations. Electrophoretic mobility measurements were also performed with a number of other divalent cations and the zeta potentials were, in all cases, well described by the combination of these three equations. The binding deduced from such measurements decreases in the sequence: Mn2+, Mg2+, Ca2+, Co2+, Ni2+, Sr2+, Ba2+. If we assume that a lipid molecule occupies an area of 60 A2 and that there is a 1 : 1 stoichiometry for the binding of the divalent ions to phosphatidylcholine, the dissociation constants are, respectively: 0.3, 1.0, 1.0, 1.2, 1.2, 2.8, 3.6 M.

Adsorption↗