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At least 613 records · Page 34Linked to original sources
PubMed1976

[Effects of divalent cations on the muscle spindle of frogs].

Afferent discharges were recorded in the nerve from the isolated muscle spindle of the m. extensor longus digiti IV of the bullfrog. Discharges of about 10 Hz generated by a sustained stretch were reduced concentration-dependently when Ca2+, Mg2+ or Mn2+ (1.0 approximately 8.0 mM) was added to normal Ringer's solution containing 2.0 mM Ca2+. In terms of the decrease of discharges following the addition of Ca2+ or Mn2+ (4.0 mM), abortive spikes were observed. With an excess of Mg2+ (4.0 mM), abortive spikes were not apparent. Removal of Ca2+ from the Ringer's solution caused an increase in the rate of discharges, and normal levels were restored by the addition of Ca2+ (2.0 mM), Mg2+ (2.3 mM) or Mn2+ (1.8 mM). Application of much higher concentrations of these ions to the nerve trunk produced no alterations in the conduction of afferent discharges. It appears that Ca2+ in the external medium contributes to the inhibition of the mechanism responsible for generating afferent discharges in the muscle spindle and that Ca2+ action is not specific since Mg2+ and Mn2+ can act as substitutes for Ca2+ to regulate afferent discharges.

Afferent Pathways↗
PubMed1992

Divalent cation substitution reveals CD18- and very late antigen-dependent pathways that mediate human neutrophil adherence to fibronectin.

We investigated the mechanisms by which Mn2+ alters human neutrophil (PMN) adherence to various connective tissue proteins. Substitution of Mn2+ for Ca2+ and Mg2+ significantly increased adhesion of human PMN to plastic well coated with fibronectin, fibrinogen, and laminin but not gelatin. Anti-CD18 mAb almost completely blocked adherence to laminin, partly blocked adherence to fibrinogen, but did not inhibit adhesion to fibronectin at all. In contrast, anti-very late antigen (VLA)-5 mAb antibodies significantly reduced Mn(2+)-mediated PMN adherence to fibronectin, but not to laminin or fibrinogen, demonstrating that VLA-5-mediated PMN adherence to fibronectin, but not to fibrinogen or laminin. This was supported by experiments in which synthetic GRGDSP peptide significantly inhibited Mn(2+)-mediated adherence to fibronectin, but not to laminin or fibrinogen. Activation of PMN with phorbol ester or C5a stimulated VLA-5-mediated adhesion to fibronectin, but the contribution of VLA-5 to the forces mediating adherence could only be detected when CD18 function was either blocked with mAb, or when CD18 was congenitally absent. VLA-5 mediated adhesion was also more transient than CD18-dependent adhesion. These data further confirm the presence of PMN VLA integrins and demonstrate that PMN VLA-5 contributes to stimulated PMN adherence to fibronectin.

Antigens, CD↗
PubMed1992

Modulation of the mitochondrial megachannel by divalent cations and protons.

In patch-clamp experiments on rat liver mitoplasts, the 1.3 nanosiemens (in 150 mM KCl) mitochondrial megachannel was activated by Ca2+ and competitively inhibited by Mg2+, Mn2+, Ba2+, and Sr2+. Cyclosporin A, which inhibits the megachannel, also showed a competitive behavior versus Ca2+. The pore is regulated by pH in the physiological range; lower pH values cause its closure in a Ca(2+)-reversible manner. The modulating sites involved in these effects are located on the matrix side of the membrane. As illustrated in the companion paper (Bernardi, P., Vassanelli, S., Veronese, P., Colonna, R., Szabó, I., and Zoratti, M. (1992) J. Biol. Chem. 267, 2934-2939), the calcium-induced permeability transition of mitochondria is affected by these various agents in a similar manner. The results support the identification of the megachannel with the pore believed to be involved in the permeabilization process. The kinetic characteristics of the single channel events support the idea that the megachannel is composed of cooperating subunits.

Animals↗
PubMed1992

[Repetitive firing in motor nerve endings: modulation by divalent cations, rhythmic activation and cholinergic agents].

The phenomenon of repetitive firing (RG) in motor nerve endings induced by 4-aminopyridine (4-AP) was studied in cut sartorius frog muscle under the voltage clamp conditions. In the presence of 4-AP (1.10(-4) mol/l) one stimulus applied to the nerve induced two end plate currents (EPC) in half of cells studied (n = 35). The elevation of calcium ion concentration up to 5.4 mmol/l or magnesium to 5-9 mmol/l or rhythmic activity (0.05 Hz and above) abolished RF. Substitution of calcium by strontium or barium enhanced RF (the number of EPC during the burst of RF). EPC with very slow time course were observed in some cells in the presence of barium, that disrupted to the burst of RF by repetitive nerve stimulation. Neostigmine, an anticholinesterase agent, increased the number of EPC in the burst of RF, but alpha-bungarotoxin exerted no effect on the RF. The role of calcium and calcium-activated potassium currents in generation and termination of RF in motor nerve endings is discussed.

4-Aminopyridine↗
PubMed2005

[The effects of divalent cations on the fibrin clot formation and its lysis].

Hemocoagulation is a Ca(2+)-dependent process, and we suppose that other bivalent cations (BC) can also influence this system. The effects of some BC (Ca2+, Fe2+, Zn2+, Cd2+, Co2+ and Ni2+) on thrombin-induced plasma clotting and clot lysis caused by streptokinase have been studied. All BC studied, except Fe2+, maintained the formation of fibrin clot followed by its lysis. In the presence of BC the coagulation part of the turbidimetry curve changed in a dose-dependen manner and was characterized by: (1) the decrease of the induction period which seems to be due to thrombin activation or accelerating fibrin self-association; (2) the elevation of the maximal optical density of the fibrin clot and the velocity of its achievement. The fibrinolytic part of the curve was characterized by the optical density downfall acceleration at low Co2+, Cd2+, Zn2+ and Ni2+ concentrations but marked delay of the process at BC higher concentrations. So, ions of Co2+, Cd2+, Zn2+ and Ni2+ but not Fe2+ significantly influence the dynamics of thrombin-induced clot formation and optical clot characteristics. At different ion concentrations BC may activate or inhibit fibrinolysis.

Cations, Divalent↗
PubMed1991

Regulation of reverse uniport activity in mitochondria by extramitochondrial divalent cations. Dependence on a soluble intermembrane space component.

We previously reported that uncoupling Ca2(+)-loaded mitochondria in the presence of [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) produces a partial expression of the permeability transition. From this and related observations, it was proposed that the absence of external free Ca2+ is inhibitory to reverse activity of the Ca2+ uniporter (Igbavboa, U., and Pfeiffer, D.R. (1988) J. Biol. Chem. 263, 1405-1412). By using Sr2(+)-instead of Ca2(+)-loaded mitochondria, the transition is avoided upon treatment with EGTA plus uncoupler, and inhibition of reverse uniport activity can be observed directly. In the presence of physiological Mg2+ concentrations, reverse uniport of Sr2+ is eliminated by external EGTA following a brief period of rapid activity. It is proposed that binding of Mg2+ rather than Sr2+ (Ca2+) at an external site is responsible for the inhibition. Regulation at the external site is modified by the size of the Sr2+ load. EGTA, in the presence of Mg2+, does not inhibit the reverse uniport-dependent release of Sr2+ from mitoplasts. The inhibitory effect can be recovered by adding back the soluble components obtained as the intermembrane space fraction following removal of the outer membrane. The soluble factor could be a regulatory subunit which contains the external cation binding site. Adjustments to uniporter activity due to regulation by the binding site and/or the soluble factor may be slow and may be significant in determining how mitochondria respond to rapid Ca2+ transients in vivo.

Animals↗
PubMed1990

[Latrotoxin channels. Permeability for divalent cations].

The dependence of Ca2+ transport in synaptosomes along the channels formed by alpha-latrotoxin on [Ca2+]in and the feasibility of transport along these channels of other bivalent cations were studied. It was found that the concentration dependence of Ca2+ influx is nonlinear and is described by the Michaelis-Menten kinetics (Km = 1.07 +/- 0.19 mM). Mg2+, Ba2+, Sr2+, Mn2+ and Co2+ competitively inhibited the Ca2+ influx via latrotoxin channels. Studies with the use of the fluorescent Ca2+ probes, Quin-2 and Fura-2, revealed that these cations can also penetrate inside synaptosomes via latrotoxin channels. The bivalent cation influx via latrotoxin channels caused a decrease of the membrane potential of synaptosomes. The similarity of properties of latrotoxin and endogenous Ca2+ channels is discussed.

Aminoquinolines↗