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PubMed1994

Triton channels are sensitive to divalent cations and protons.

Addition of Triton X-100 to planar bilayers composed of dioleoyl phosphatidyl choline, diphytanoyl phosphatidyl choline or mono-oleoyl glycerol induces single channel-like events when electrical conductivity across the bilayer is measured. Addition of divalent cations or protons causes channels to disappear; single channel conductance of remaining channels is not significantly altered; addition of EDTA or alkali (respectively) reverses the effect. It is concluded that sensitivity to divalent cations and protons need not be dependent on specific channel proteins or pore-forming toxins, but may be a feature of any aqueous pore across a lipid milieu.

Calcium↗
PubMed1981

Dependence of human platelet functional responses on divalent cations: aggregation and secretion in heparin- and hirudin-anticoagulated platelet-rich plasma and the effects of chelating agents.

The dependence of ADP- and epinephrine-induced platelet aggregation and secretion on extracellular divalent cations was examined by quantitating these responses in citrate-, heparin-, and hirudin-anticoagulated platelet-rich plasma. ADP-induced 14C-5HT secretion in heparin-PRP and hirudin-PRP was generally decreased, relative to that in citrate-PRP, without corresponding reductions in aggregation, whereas in response to epinephrine, both aggregation and secretion were decreased in heparin-PRP, and abolished in hirudin-PRP. In heparin-PRP, but not in hirudin-PRP, the degree to which these responses were altered was highly variable among normal subjects, and was dependent on the anticoagulant concentration. Addition of citrate restored the extent of ADP-induced secretion and of epinephrine-induced aggregation and secretion in heparin-PRP to that observed in citrate-PRP, and increased the extent of ADP-induced secretion in hirudin-PRP. Addition of EDTA or EGTA, however, had no effect of ADP-induced secretion in heparin-PRP. These results suggest that ADP-induced aggregation and secretion, as well as responses to ADP vs. epinephrine, have different dependencies on extracellular or surface-bound divalent cations. The variable responses observed in heparin-PRP may reflect direct interactions of heparin with platelets, and this variability may account for the conflicting results of previous studies.

Adenosine Diphosphate↗
PubMed1983

Divalent cations and temperature dependent block of impulse propagation at the frog neuromuscular junction.

End-plate potentials were recorded from superficial muscle fibers of the frog sartorius nerve-muscle preparation. Exposure of the preparation to a medium containing a high divalent cation concentration, produced a temperature dependent failure of neuromuscular transmission. Failure of transmission developed in an "all-or-none" mode and was reversed by decreasing the bath temperature or divalent cation concentration. This blockage of the neurotransmission is attributed to a presynaptic block of impulse propagation.

Animals↗
PubMed2026

Gdt1, Gdt2 and the P-type ATPase Pmr1 regulate divalent cations (Ca²⁺ and Mn²⁺) in the fission yeast Schizosaccharomyces pombe.

In eukaryotes, calcium (Ca²⁺) and manganese (Mn²⁺) ion homeostasis in the early secretory pathway is crucial for protein glycosylation, cell wall biosynthesis, and cell structure. To clarify the roles of the UPF0016 family proteins Gdt1 and Gdt2 in the regulation of divalent cations, we performed genetic and phenotypic analyses on single-gene deletion mutants (Δgdt1, Δgdt2 and Δpmr1) and double-gene deletion mutants in Schizosaccharomyces pombe. In the presence of CaCl₂ and MnCl₂, Δgdt1 cells exhibit marked hypersensitivity, indicating that Gdt1 is a major contributor to divalent cation regulation; in contrast, Δgdt2 and Δpmr1 mutants show only mild growth defects. However, the combined deletion of gdt1 or gdt2 with pmr1 results in a strong synthetic growth phenotype, suggesting that Gdt1, Gdt2, and Pmr1 play complementary roles in maintaining divalent cation regulation within the secretory network. Structural comparative analysis reveals that Gdt1 retains a conserved five-transmembrane structure, whereas Gdt2 adopts a six-transmembrane conformation. Both proteins preserve the EIGDKT and EWGDRS motifs characteristic of UPF0016 transporters. These findings establish Gdt1 as a key determinant of Ca²⁺ and Mn²⁺ regulation and support a complementary role for Gdt2 in ion regulation, a process essential for efficient glycosylation and normal cell wall morphogenesis.

Schizosaccharomyces pombe↗
PubMed1993

The COT2 gene is required for glucose-dependent divalent cation transport in Saccharomyces cerevisiae.

Eleven cobalt-tolerant mutants were found to belong to a single complementation group, cot2. In addition to cobalt, the cot2 mutants were found to tolerate increased levels of the divalent cations Zn2+, Mn2+, and Ni2+ as well. All of the cot2 mutants exhibited a wiener-shaped cellular morphology that was exacerbated by the carbon and nitrogen source but was unaffected by metals. The rate of glucose-dependent transport of cobalt into cells was reduced in strains that carry mutations in the COT2 gene. COT2 is not essential for growth. Strains that carry a COT2 allele conferring complete loss of function are viable and exhibit phenotypes similar to those of spontaneous cot2 mutations. The sequence of the COT2 gene shows that it is identical to GRR1, which encodes a protein required for glucose repression. The glucose dependence of the transport defect implies that cot2 mutations affect the link between glucose metabolism and divalent cation active transport.

Amino Acid Sequence↗
PubMed1989

Local anesthetic-divalent cation binding center interaction.

This communication explicitly considers the possibility that local anesthetics interact with divalent cation binding centers, such as chlortetracycline, quin 2, ethyleneglycol bis (B-aminoethyl ether)-N-N,N',N'-tetraacetic acid (EGTA), ethylenediamine tetraacetic acid (EDTA) and ATP. Alterations of local anesthetic fluorescence spectra have been found in the presence of EGTA, EDTA and ATP. On the other hand, the fluorescence of chlortetracycline is enhanced and that of quin 2 is quenched by local anesthetics. The spectrofluorometric evidence presented in this paper clearly indicates that local anesthetics and these divalent cation chelators interact in solution. The fluorescence alterations observed do not derive from parallel changes of their respective absorption spectra, thus, they appear to be due to quantum yield changes. On the basis of the spectral perturbations observed, it is likely that local anesthetics interact with M2+ binding centers via their electron defective aromatic ring. From the association constants obtained in this study, we make an estimation of the free energy of this interaction ranging from -2.8 to -4.0 kcal/mole in the following experimental conditions: pH 7.4 at an ionic strength of 0.1 at 25 degrees. The relevance of these results to define the physical-chemical characteristics of the local anesthetic receptor site is briefly discussed. It is suggested that local anesthetics can bind strongly to Ca2+ and Mg2+ binding centers, provided that a hydrophobic region is located nearby.

Adenosine Triphosphate↗
PubMed1985

Temperature dependence of divalent cation induced fusion of phosphatidylserine liposomes: evaluation of the kinetic rate constants.

The effect of temperature and divalent cation binding (Ca2+, Sr2+, Ba2+) on the kinetic rate constants of aggregation and fusion of large phosphatidylserine liposomes is measured for the first time. Fusion is monitored by the Tb3+/dipicolinate assay. Fusion rate constants increase with temperature (15-35 degrees C) in a roughly linear fashion. These rate constants are not otherwise sensitive to whether the temperature is above or below the phase transition temperature of the Ba2+ or Sr2+ complex of phosphatidylserine, as measured by differential scanning calorimetry. Hence, the isothermal transition of the acyl chains from liquid-crystalline to gel phase induced by the cations is not the driving force of the initial fusion event. The aggregation rate constants increase with temperature, and it is the temperature dependence of the energetics of close approach of the liposomes which underlies this increase. On the other hand, the aggregation becomes more reversible at higher temperatures, which has also been observed with monovalent cation induced liposome aggregation where there is no fusion. Calculations on several cases show that the potential energy minimum holding the liposome dimer aggregates together is approximately 5-6 kT deep. This result implies that the aggregation step is highly reversible; i.e., if fusion were not occurring, no stable aggregates would form.

Barium↗
PubMed1990

Effects of low molecular weight peptides and divalent cations on degradation and binding of angiotensin II.

The effects of peptide inhibitors (bestatin and amastatin) and divalent cations (Ca2+ and Co2+) on the velocity of Asp1 liberation from angiotensin II (A-II) by human placental membrane fractions and binding of 125I A-II to human placental membranes were tested at 22 degrees C and 4 degrees C. Asp1 liberation was measured by high performance liquid chromatography. As expected, the degradation and binding of A-II were temperature sensitive, with both being at 4 degrees C than at 22 degrees C. While amastatin (10(-4) M) and bestatin 10(-6) M) significantly reduced the velocity of Asp1 liberation from A-II to about 45%, amastatin (10(-4) M) and bestatin (10(-4) M) increased 125I A-II binding to 125% and 130%, respectively. Ca2+ (10 mM) and Co2+ (10 mM) activated the velocity of Asp1 liberation from A-II to 140% and 120%, respectively at 22 degrees C. Ca2+ (10(-1) M) and Co2+ (10 mM) also enhanced 125I A-II binding about 130%. Previously we showed that the A-II degrading activity found in human placental membrane fractions is mainly due to aminopeptidases A and M. Since amastatin and bestatin are the specific inhibitors for aminopeptidases A and M, and since Ca2+ and Co2+ are the activators for aminopeptidase A and aminopeptidase M, respectively, it is conceivable that the enzymes regulate the levels of A-II and, therefore, that they may play an important role in the binding of A-II to human placental membrane fractions.

Adult↗
PubMed1983

Effect of liposomes containing various divalent cations on the release of acetylcholine from synaptosomes.

The effect of increasing the cytoplasmic levels of various divalent cations on the release of [3H]acetylcholine ([3H]ACh) from synaptosomes was investigated. Synaptosomes prepared from rat brain and prelabeled with [3H]choline were incubated with liposomes containing Mg2+, Ca2+, Mn2+, Co2+, Sr2+, or Ba2+. This treatment allows the transfer of the aqueous contents of the liposomes to the cytoplasm of the synaptosomes. The efflux of radioactivity subsequent to this treatment was measured, and the relative proportions of [3H]ACh and [3H]choline were determined. The release of radioactivity from synaptosomes incubated with liposomes containing Mg2+, Mn2+, or Co2+ was not altered when compared with synaptosomes incubated either without liposomes or with liposomes containing isotonic K+/Na+. Synaptosomes incubated with liposomes containing Ca2+, Sr2+, or Ba2+, however, released significantly more radioactivity than did controls. Moreover, the released radioactivity consisted almost entirely of [3H]ACh. Liposomes containing either Ca2+ or Sr2+ were equally effective in promoting the release of [3H]ACh from synaptosomes, whereas liposomes containing Ba2+ were 2.5 times more effective in promoting the release of [3H]ACh than were liposomes containing either Ca2+ or Sr2+. Since liposomes introduce their aqueous contents into cytoplasm via a mechanism not involving plasma membrane channels, the increased release of [3H]ACh caused by liposomes containing Ca2+, Sr2+, or Ba2+ is attributable to an increase in the intrasynaptosomal concentration of these ions, and not to their passage through calcium channels.

Acetylcholine↗
PubMed1978

Superoxide production by digitonin-stimulated guinea pig granulocytes. The effects of N-ethyl maleimide, divalent cations; and glycolytic and mitochondrial inhibitors on the activation of the superoxide generating system.

N-ethylmaleimide, divalent cations, ethylene glycol bis (beta aminoethyl ether) N,N,N',N',-tetraacetate, 2-deoxyglucose, cyanide, and dinitrophenol were examined for their effect on the ability of guinea pig granulocytes to generate superoxide (O(2) (-)) when stimulated by digitonin. N-ethylmaleimide (1 mM) inhibits only when added before complete activation of the O(2) (-) generating system, and at lower concentrations (0.05-0.2 mM) slows the activation process. Ca(++) is required for maximum O(2) (-) generation, and Mg(++) decreases the amount of Ca(++) required. Ethylene glycol bis (beta aminoethyl ether) N,N,N',N',-tetraacetate (10 mM) inhibits only if added before complete activation. Incubation of cells in 2-DOG causes a time- and concentration-dependent inhibition of O(2) (-) generation. It also increases the time required for activation of this system. Cyanide and dinitrophenol increase the rate of O(2) (-) production. However, when these compounds are added to cells whose O(2) (-) production is partially inhibited by incubation in 2-deoxyglucose, complete inhibition results. If cyanide or dinitrophenol is added after activation of 2-deoxyglucose-treated cells, no further inhibition occurs. On the basis of the above results, we conclude that the activation of the O(2) (-) generating system is N-ethylmaleimide sensitive, Ca(++) dependent, and energy requiring, but that the activity of the enzyme system in the cell is not.

Animals↗
PubMed1991

The association between blood pressure, calcium and other divalent cations: a population study.

This report investigated the associations between blood pressure and the levels of various divalent cations in blood and urine in the population at large. The 1,982 participants (963 men and 1019 women; mean age 48 years) constituted a stratified random sample of the population of 4 Belgian districts. Systolic/diastolic pressure averaged 133/78 mmHg in men, and 128/76 mmHg in women. Serum total calcium (2.37 mmol/l), serum magnesium (1.00 mmol/l) and blood cadmium (10.0 nmol/l) were on average similar in the two sexes. By contrast, serum zinc (13.1 and 12.6 mumol/l, respectively), blood lead (0.56 and 0.36 mumol/l) and the urinary excretions of calcium (4.86 and 3.95 mmol/24h), copper (0.16 and 0.13 mumol/24h), and cadmium (9.4 and 7.2 nmol/24h) were significantly higher in men than in women. After adjustment for significant blood pressure covariates (age, body mass index, pulse rate, log gamma-glutamyltranspeptidase, smoking habits, and in women the contraceptive pill), serum total calcium was independently and positively correlated with systolic pressure in both sexes, and with diastolic pressure in women. After similar adjustments systolic pressure was positively correlated with urinary copper in men and women. In addition, systolic pressure and blood lead, and diastolic pressure and urinary cadmium were negatively correlated in men. In conclusion, this population study demonstrated a positive relationship between systolic blood pressure and both serum total calcium and urinary copper.

Adult↗
PubMed1990

Multiple roles of divalent cation in the terminal deoxynucleotidyltransferase reaction.

Terminal deoxynucleotidyltransferase activity is absolutely dependent on the presence of a divalent cation in the reaction mixture. This requirement can be satisfied by either Mg2+, Co2+, or Mn2+. When Mg2+ is used, the reaction rate is inhibited by metal ligands, and this inhibition can be reversed by Zn2+. Reaction rates in Mg2+ are also stimulated by the addition of micromolar amounts of Zn2+. To examine the role of Zn2+ in terminal transferase catalysis we analyzed for Zn2+ in homogeneous recombinant human terminal transferase preparations and found that Zn2+ is not an intrinsic part of enzyme molecule. Analysis of Zn2+ binding to terminal transferase under equilibrium conditions shows about 0.3 g of atom of Zn2+/mol of enzyme, suggesting that Zn2+ forms an easily dissociable complex with the enzyme molecule. Kinetic analyses showed that the stimulatory effect of Zn2+ is observed in several buffer systems. Zn2+ increases the affinity of the enzyme for the initiator about 2-fold and decreases affinity for dATP more than 10-fold, resulting in an increase in the apparent Vmax of the reaction. Using a 3'-ended 2',3'-dideoxyoligonucleotide as an inhibitor demonstrates that the inhibitor has no effect on the reaction rate in the absence of Zn2+ but is competitive with respect to the initiator in the presence of Zn2+. These results suggest that Zn2+ is a positive effector for terminal transferase, interacting with oligonucleotide and enzyme near the initiator binding site. Binding of Zn2+ to the enzyme appears to induce conformational changes that greatly increase the Vmax of the reaction with a concomitant decrease in the affinity of the enzyme for dNTP.

Adenosine Triphosphate↗
PubMed1980

Different divalent cation requirements for binding IgM complexes to lymphocytes and macrophages.

We have found that Mg++ supports IgM complex binding to mouse lymphocytes but not to macrophages. In contrast, Ca++ supports IgM complex binding to macrophages but not lymphocytes. IgG complex binding to both lymphocytes and macrophages is divalent cation independent. These findings allow one to distinguish IgG from IgM binding and macrophage from lymphocyte IgM complex binding by their differential divalent cation requirements.

Animals↗
PubMed1999

Sodium influx via a non-selective pathway activated by the removal of extracellular divalent cations: possible role in the calcium paradox.

OBJECTIVE: Cation non-selective conductances which are induced upon removal of extracellular divalent cations have been identified in cardiac and other cells. We have examined whether the conductance identified in cardiac myocytes mediates an increase in intracellular Na+ (Nai+) and have tested the ability of drugs to prevent this influx. METHODS: Rat single ventricular myocytes at 22 degrees C were voltage-clamped in whole-cell mode to measure membrane currents or were loaded with SBFI to measure Nai+. RESULTS: Removal of extracellular Ca2+ (Cao2+) and Mg2+ (Mgo2+), which induced a current with reversal potential of -10 mV, also caused an increase in SBFI fluorescence ratio (340/380 nm). These changes were reversible on repletion of Cao2+ and/or Mgo2+. They could not be prevented by nifedipine, indicating that they were not mediated by L-type Ca2+ channels. Both increases in non-selective conductance and in Nai+ were prevented by trivalent cations (Dyo3+, Gdo3+ or Lao3+; 100 microM) or reduced by the aminoglycoside gentamicin. CONCLUSION: A cation non-selective conductance, different from L-type Ca2+ channels, contributes to the Nai+ accumulation obtained during perfusion with Ca2+/Mg(2+)-free media, hence also to the Cai2+ overload and cellular damage upon Cao2+ repletion (the Ca2+ paradox).

Action Potentials↗
PubMed1998

Extracellular proton alters the divalent cation binding affinity in a cyclic nucleotide-gated channel pore.

Extracellular protons in the range of 10(-9) to 10(-5) M effectively suppressed Na+ current (K(1/2) = 10(-6.1)) through the bovine retinal guanosine 3',5'-cyclic mononucleotide-gated ion channel expressed in Xenopus oocytes. The reduction of channel current was mediated by a single glutamate residue (Glu363) within the pore-forming region of the channel, also involved in extracellular divalent cation binding. Increasing the concentration of extracellular proton decreased the binding affinity of the extracellular divalent cation (e.g. Sr2+) and the large difference of binding affinity previously observed between the wild-type and E363D mutant channel disappeared. These results indicate that the permeation characteristics of cyclic nucleotide-gated ion channel can be altered by extracellular pH through a single acidic residue in the channel conduction pathway.

Amino Acid Substitution↗
PubMed2000

Genetic susceptibility to intracellular infections: Nramp1, macrophage function and divalent cations transport.

Nramp1 is one of the few host resistance genes that have been characterized at the molecular level. Nramp1 is an integral membrane protein expressed in the lysosomal compartment of macrophages and is recruited to the membrane of bacterial phagosomes where it affects intracellular microbial replication. Nramp1 is part of a very large gene family conserved from bacteria and man that codes for transporters of divalent cations transporters. We propose that Nramp1 affects the intraphagosomal microbial replication by modulating divalent cations content in this organelle. Both mammalian and bacterial transporters may compete for the same substrate in the phagosomal space.

Animals↗
PubMed1981

Platelet adherence to collagen: role of plasma, ADP, and divalent cations.

The effect of varying methods of platelet preparation and the role of ADP and divalent cations in supporting platelet adherence to collagen and the release of 14C-serotonin were assessed by affinity chromatography on collagen/Sepharose to define physiological conditions for this interaction. Platelets were separated by centrifugation or gel filtration from blood anticoagulated with EDTA or citrate and suspended in native plasma or buffer. After labelling with 51Cr or 14C-serotonin, they were passed though columns of collagen covalently linked to cyanogen bromide-activated Sepharose. Adherence to collagen was less in plasma as compared to buffer, was increased by centrifuging the platelets before testing, and was unaltered by addition of ADP. Removal of ADP with CP/CPK decreased the adherence of gel-filtered citrated and EDTA platelets and washed EDTA platelets (P less than 0.001) but not EDTA platelets in plasma. Adherence and release of citrated platelets in plasma or buffer containing CP/CPK were greater than that of EDTA platelets (P less than 0.01); no difference existed with gel-filtered platelets. The addition of 1 mM Mg++ to citrate or EDTA-anticoagulated washed platelets increased adherence and release (P less than 0.01). The results indicate that the choice of experimental conditions affect the assessment of factors which influence or promote platelet interaction with collagen. Platelet-collagen adherence is enhanced by laboratory manipulations and partially inhibited by normal plasma. Maximal adherence and release occur when divalent cations, particularly Mg++, and ADP are available. Their absence reduces but does not inhibit these reactions.

Adenosine Diphosphate↗
PubMed1982

Ionophore-mediated transmembrane movement of divalent cations in small unilamellar liposomes: an evaluation of the chlortetracycline fluorescence technique and correlations with black lipid membrane studies.

Conceptual advances in the field of membrane transport have, in the main, utilized artificial membranes, both planar and vesicular. Systems of biological interest, viz., cells and organelles, resemble vesicles in size and geometry. Methods are, therefore, required to extend the results obtained with planar membranes to liposome systems. In this report we present an analysis of a fluorescence technique, using the divalent cation probe chlortetracycline, in small, unilamellar vesicles, for the study of divalent cation fluxes. An ion carrier (X537 A) and a pore former (alamethicin) have been studied. The rate of rise of fluorescence signal and the transmembrane ion gradient have been related to transmembrane current and potential, respectively. A second power dependence of ion conduction - including the electrically silent portion thereof - on X537 A concentration, has been observed. An exponential dependence of "current" on "transmembrane potential" in the case of alamethicin is also confirmed. Possible errors in the technique are discussed.

Alamethicin↗