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PubMed1976

Inhibition by triphenyltin chloride of a tightly-bound membrane component involved in photophosphorylation.

At very low concentrations (less than 1 muM) triphenyltin chloride inhibits ATP formation and coupled electron transport in isolated spinach chloroplasts. Basal (-Pi) and uncoupled electron transport are not affected by triphenyltin. The membrane-bount ATP in equilibrium Pi exchange and Mg2+-dependent ATPase activities of chloroplasts are also completely sensitive to triphenyltin, although the Ca2+-dependent and Mg2+-dependent ATPase activities of the isolated coupling factor protein are insensitive to triphenyltin. The light-driven proton pump in chloroplasts is stimulated (up to 60%) by low levels of triphenyltin. Indeed, the amount of triphenyltin necessary to inhibit ATP formation or stimulate proton uptake is dependent upon the amount of chloroplasts present in the reaction mixture, with an apparent stoichiometry of 2-2.5 triphenyltin molecules/100 chlorophyll molecules at 50% inhibition of ATP formation and half-maximal stimulation of proton uptake. Chloroplasts partially stripped of coupling factor by an EDTA was are no longer able to accumulate protons in the light. However, low levels of triphenyltin can effectively restore this ability. The amount of triphenyltin required for the restoration of net proton uptake is also dependent upon the amount of chloroplasts, with a stoichiometry of 4-5 triphenyltin molecules/100 chlorophyll molecules at 50% reconstitution. On the basis of this and other evidence it is concluded that triphenyltin chloride inhibits phosphorylation, ATP + Pi exchange and membrane-bound ATPase activities in chloroplasts by specifically blocking the transport of protons through a membrane-bound carrier or channel located in a hydrophobic region of the membrane at or near the functional binding site for the coupling factor.

Adenosine Triphosphatases↗
PubMed1992

Ring-substituted diaqua(1,2-diphenylethylenediamine)platinum(II) sulfate reacts with DNA through a dissociable complex.

Ring-substituted diaqua(1,2-diphenylethylenediamine)platinum(II) sulfate shows unusual kinetics in its reaction with salmon testis DNA. The mechanism for diaqua[meso-1,2-bis(2,6-dichloro-4- hydroxyphenyl)ethylenediamine]platinum(II) sulfate, [Pt(H2O)2(meso-6)]2+SO4(2-), a representative of this series, has been investigated and compared with that for cis-[Pt(NH3)2(H2O)2]2+. Reactions were followed by atomic absorption, analytical HPLC of Pt-DNA digests, arrest of enzymatic DNA synthesis/degradation, ultraviolet and fluorescence spectrophotometry. Except for the formation of monofunctional DNA adducts, the kinetics of the platinum(II) complexes are comparable. The pseudo-first-order rate constant for the attack of DNA by [Pt(H2O)2(meso-6)]2+ follows the concentration of DNA in a hyperbolic fashion, which is in contrast to the linear dependence for cis-[Pt(NH3)2(H2O)2]2+. The hyperbolic dependence is typical for a dissociable DNA/drug complex preceding the coordination reaction. By studying the binding of free ligand to DNA, and by correlating ligand structures and electrostatic charges with effects on adduct formation, both the phenyl residues and the positive charge of the platinum(II) complex are shown to be crucial for the stability of the dissociable complex. A non-intercalative mode of binding to the DNA backbone is suggested. At the high concentrations of DNA found in cell nuclei, the reaction of the dissociable complex can, principally, become rate-limiting in the attack of DNA and thus reduce the cytotoxic efficiency of a drug.

Animals↗
PubMed1986

Intracellular free Mg2+ in Balanus photoreceptor measured with eriochrome blue.

Intracellular free Mg2+ (Mgf) in darkness and during illumination was measured in the Balanus photoreceptor using the Mg2+ sensitive dye Eriochrome Blue SE (EB). The EB was pressure injected in the cell and Mgf determined from measurements of absorption changes at 570 nm and 600 nm. Mgf is 1.7 mM in the dark-adapted photoreceptor. There was no indication of a change in Mgf when the cell was illuminated with bright light, indicating that Mgf is not elevated during the phototransduction. Changes less than 5 X 10(-5) M could have occurred and remained undetected. The spectrophotometric properties of the indicator were studied at 10(-4) and 10(-3) M, at ionic conditions relevant to the intracellular measurements. Both the differential molar absorption coefficient for the EB-Mg complex at 600 nm (delta epsilon 600EBMg) and the apparent dissociation constant (KD) for the complex formation were different at 10(-4) and 10(-3) M EB.

Animals↗
PubMed1995

Phosphoarginine stimulation of Na(+)-Ca2+ exchange in squid axons--a new pathway for metabolic regulation?

1. [Na+]o-dependent Ca2+ efflux (forward Na(+)-Ca2+ exchange), [32P]ATP wash-out curves and [ATP] were measured in internally dialysed squid giant axons at 17-18 degrees C. 2. We found that dialysing squid axons without ATP and with [Ca2+]i around 1 microM the basal levels of the [Na+]o-dependent Ca2+ efflux were significantly higher in the presence of N omega-phosphoarginine (PA). Phosphocreatine, a related phosphagen, is without effect. 3. PA stimulation of the Na(+)-Ca2+ exchange occurs in the complete absence of ATP (< 1 microM), being independent of, and additive to, the ATP-stimulated [Na+]o-dependent Ca2+ efflux. PA stimulation of [Na+]o-dependent Ca2+ efflux is fully and rapidly reversible with a Km around 7.7 mM. Activation by saturating [PA] is equivalent in magnitude to that of ATP. 4. PA stimulation of Na(+)-Ca2+ exchange is markedly dependent on intracellular Ca2+ and Mg2+ ions. Below 0.5 microM Ca2+i PA effect is negligible, becoming noticeable between 0.8 and 2 microM. In addition, Ca2+i considerably increases the rate at which PA activates the Na(+)-Ca2+ exchange. Although there is no absolute requirement of the PA effect for Mg2+ ions, this divalent cation largely stimulates the PA effect. 5. This work demonstrates, for the first time, the presence in squid axons of a new form of metabolic regulation of the Na(+)-Ca2+ exchange directly and solely related to PA and different from that of MgATP. This novel mechanism is likely to play a physiological role in Ca2+ extrusion through the Na(+)-Ca2+ exchanger, particularly at micromolar [Ca2+]i.

Animals↗
PubMed2004

The CorA Mg2+ transporter does not transport Fe2+.

corA encodes the constitutively expressed primary Mg2+ uptake system of most eubacteria and many archaea. Recently, a mutation in corA was reported to make Salmonella enterica serovar Typhimurium markedly resistant to Fe2+-mediated toxicity. Mechanistically, this was hypothesized to be from an ability of CorA to mediate the influx of Fe2+. Consequently, we directly examined Fe2+ transport and toxicity in wild-type versus corA cells. As determined by direct transport assay, CorA cannot transport Fe2+ and Fe2+ does not potently inhibit CorA transport of 63Ni2+. Mg2+ can, relatively weakly, inhibit Fe2+ uptake, but inhibition is not dependent on the presence of a functional corA allele. Although excess Fe2+ was slightly toxic to S. enterica serovar Typhimurium, we were unable to elicit a significant differential sensitivity in a wild-type versus a corA strain. We conclude that CorA does not transport Fe2+ and that the relationship, if any, between iron toxicity and corA is indirect.

Bacterial Proteins↗
PubMed1968

Activation of fatty acid synthesis in cell-free extracts of Saccharomyces cerevisiae.

Fatty acid synthesis from acetate in extracts of Saccharomyces cerevisiae strain LK2G12 was shown to be stimulated by alpha-glycerophosphate and citrate, and by a number of compounds related to them. Magnesium was shown to stimulate fatty acid synthesis from acetyl-coenzyme A but not from malonyl-coenzyme A, thus indicating the site of stimulation of fatty acid synthesis to be the acetyl-coenzyme A step.

Carbon Isotopes↗
PubMed2006

Response surface methodology for the optimization of keratinase production in culture medium containing feathers produced by Kocuria rosea.

A 43-fold increase in keratinase production by Kocuria rosea was achieved in batch fermentation using response surface methodology. Factorial designs were used to select the components of a culture medium that showed a significant effect on keratinase production. An orthogonal-central composite experimental design was performed, with only two (feathers and magnesium) from nine initial compounds being further analyzed by response surface methodology. An optimum keratinase production of 14 886.9 U/mg was obtained with the following medium composition (per litre): NH4Cl, 0.3 g; NaCl, 0.3 g; K2HPO4, 3.2 g; KH2PO4, 4.0 g; MgSO4.6H2O, 0.5 g; yeast extract, 0.1 g; and finely milled feathers, 30 g. The medium was shaken at 400 r/min with an incubation period of 14 h at 40 degrees C.

Animals↗
PubMed2005

Characterization of the Na+-dependent Mg2+ transport in sheep ruminal epithelial cells.

This study examines the routes by which Mg2+ leaves cultured ovine ruminal epithelial cells (REC). Mg2+-loaded (6 mM) REC were incubated in completely Mg2+-free solutions with varying Na+ concentrations, and the Mg2+ extrusion rate was calculated from the increase of the Mg2+ concentration in the incubation medium determined with the aid of the fluorescent probe mag-fura 2 (Na+ salt). In other experiments, REC were also studied for the intracellular free Mg2+ concentration ([Mg2+]i; using mag-fura 2), the intracellular Na+ concentration (using Na+-binding benzofuran isophthalate), the intracellular cAMP concentration ([cAMP]i; using an enzyme-linked immunoassay), and Na+/Mg2+ exchanger existence [using a monoclonal antibody (mAb) raised against the porcine red blood cell Na+/Mg2+ exchanger]. Mg2+-loaded REC show a Mg2+ efflux that was strictly dependent on extracellular Na+. The Mg2+ extrusion rate increased from 0.018+/-0.009 in a Na+-free medium to 0.73+/-0.3 mM.l cells-1.min-1 in a 145 mM Na+ medium and relates to extracellular Na+ concentration ([Na+]e) according to a typical saturation kinetic (Km value for [Na+]e=24 mM; maximal velocity=11 mM.l cells-1.min-1). Mg2+ efflux was reduced by imipramine (48%) and increased after application of dibutyryl-cAMP (55%) or PGE2 (17%). These effects are completely abolished in Na+-free media. Furthermore, an elevation of [cAMP]i led to an [Mg2+]i decrease that amounted to 375+/-105 microM. The anti-Na+/Mg2+ exchanger mAb inhibits Mg2+ extrusion; moreover, it detects a specific 70-kDa immunoreactive band in protein lysates of ovine REC. The data clearly demonstrate that a Na+/Mg2+ exchanger is existent in the cell membrane of REC. The transport protein is the main pathway (97%) for Mg2+ extrusion and can be assumed to play a considerable role in the process of Mg2+ absorption as well as the maintenance of the cellular Mg2+ homeodynamics.

Animals↗
PubMed1990

Electrical behavior of myenteric neurons induced by mesenteric nerve stimulation in the guinea pig ileum.

Effects of mesenteric nerve (MN) stimulation on the electrophysiological behavior of myenteric neurons in the guinea pig ileum were investigated with intracellular recording techniques in the myenteric flaps innervated with mesenteric nerves. MN stimulation at 0.11-6 Hz evoked fast excitatory postsynaptic potentials (EPSPs) in 6 myenteric neurons (2 Type 2/AH, 3 NS and 1 Type 1/S cells) and rarely evoked antidromic soma spike potentials in 3 myenteric neurons. Fast EPSPs were abolished by hexamethonium. Slow EPSPs evoked by MN stimulation (Takaki and Nakayama (1988) Brain Res., 442, 351-353) were also obtained in 5 Type 2/AH neurons and were irreversibly abolished by superfusion with capsaicin 10 microM. It is, therefore, likely that fast EPSPs mediated by nicotinic cholinergic receptors are due to stimulation of the vagus nerve and slow EPSPs are mediated by a release of substance P at axosomatic synapses due to antidromic activation of the capsaicin-sensitive sensory nerves.

Animals↗
PubMed2005

Hypermagnesemia induced by massive cathartic ingestion in an elderly woman without pre-existing renal dysfunction.

A 76-year-old woman was referred to our hospital for unresponsiveness and hypotension. She had developed constipation that had led to ileus and had received 34 g of magnesium citrate (Magcolol P) orally the day before. She was lethargic, her blood pressure was less than 50 mmHg, and electrocardiogram (ECG) revealed sinus arrest with junctional escape rhythm. Her serum concentration of magnesium (Mg) was markedly elevated (16.6 mg/dl =13.7 mEq/l). Emergency colonoscopy revealed ischemic colitis. As her condition ameliorated, her renal function returned to normal. Hence, the present case suggests that severe hypermagnesemia can occur in the absence of pre-existing renal dysfunction in elderly patients with gastrointestinal diseases.

Administration, Oral↗