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PubMed1986

The properties of arginine transport in vacuolar membrane vesicles of Neurospora crassa.

We have measured the uptake of arginine into vacuolar membrane vesicles from Neurospora crassa. Arginine transport was found to be dependent on ATP hydrolysis, Mg2+, time, and vesicle protein with transported arginine remaining unmodified after entry into the vesicles. The Mg2+ concentration required for optimal arginine transport varied with the ATP concentration so that maximal transport occurred when the MgATP2- concentration was at a maximum and the concentrations of free ATP and Mg2+ were at a minimum. Arginine transport exhibited Michaelis-Menten kinetics when the arginine concentration was varied (Km = 0.4 mM). In contrast, arginine transport did not follow Michaelis-Menten kinetics when the MgATP2-concentration was varied (S0.5 = 0.12 mM). There was no inhibition of arginine transport when glutamine, ornithine, or lysine were included in the assay mixture. In contrast, arginine transport was inhibited 43% when D-arginine was present at a concentration 16-fold higher than that of L-arginine. Measurements of the internal vesicle volume established that arginine is concentrated 14-fold relative to the external concentration. Arginine transport was inhibited by dicyclohexylcarbodiimide, carbonyl cyanide m-chlorophenyl-hydrazone, and potassium nitrate (an inhibitor of vacuolar ATPase activity). Inhibitors of the plasma membrane or mitochondrial ATPase such as sodium vanadate or sodium azide did not affect arginine transport activity. In addition, arginine transport had a nucleoside triphosphate specificity similar to that of the vacuolar ATPase. These results suggest that arginine transport is dependent on vacuolar ATPase activity and an intact proton channel and proton gradient.

Adenosine Triphosphate↗
PubMed2004

Efficient asymmetric oxidation of sulfides and kinetic resolution of sulfoxides catalyzed by a vanadium-salan system.

The asymmetric oxidation of sulfides to chiral sulfoxides with hydrogen peroxide in good yield and high enantioselectivity has been catalyzed very effectively by chiral vanadium-salan [N,N'-alkyl bis(salicylamine)] complex. The salan ligand shows results superior in terms of reactivity and enantioselectivity to those of salen [N,N'-alkylene bis(salicylideneimine)] analogue, and provides the sulfoxide with opposite configuration. The high enantioselectivity of this reaction is the direct result of the asymmetric oxidation. The efficient kinetic resolution of racemic sulfoxides catalyzed by the vanadium-salan system is also described.

Catalysis↗
PubMed1995

Effect of heavy metal ions on the release of reactive oxygen intermediates by bovine alveolar macrophages.

Short-term incubations of bovine alveolar macrophages (BAM) with metal-containing dusts induce the release of reactive oxygen intermediates (ROI). Incubations of BAM (90 min) with dissolved metal compounds (0.1-100 microM) combined with quartz dusts were performed to investigate the effects of single elements on BAM stimulation. As(III), as well as the calcium antagonists, Ni(II) and Ce(III), inhibited the secretion of superoxide anions (O2-) and hydrogen peroxide (H2O2). O2- concentrations were lowered by Mn(II) and Fe(II). Increased ROI concentrations were observed with V(IV) (O2- and H2O2) and Fe(III) (O2-). The addition of Cd(II), Cr(III) and V(V) showed no effect on the dust-induced respiratory burst. The influence of insoluble heavy metal compounds on ROI secretion by BAM were studied with metal oxide-coated silica particles. In most cases the release of ROI was not affected by the chemical modification of the particle surface. Coating with CuO markedly lowered the concentrations of O2- and H2O2, whereas vanadium(IV) oxide considerably increased both ROIs. Although most of the investigated metal compounds did not alter ROI secretion our present results with V(IV) and Fe(III) confirm our recent statistical evaluation of the effects of heavy metal-containing dusts on ROI secretion (Berg et al., 1993, J. Toxicol. Environ. Health 39, 341).

Animals↗
PubMed1996

Crystal Structure and Spectroscopic Characterization of K(6)(VO)(4)(SO(4))(8) Containing Mixed-Valent Vanadium(IV)-Vanadium(V).

Pleochroistic crystals (dark green to colorless) of a mixed-valence V(IV)-V(V) compound, K(6)(VO)(4)(SO(4))(8), suitable for X-ray determination have been obtained from the catalytically important K(2)S(2)O(7)-V(2)O(5)/SO(2)-O(2)-SO(3)-N(2) molten salt-gas system, at approximately 400 degrees C. The compound crystallizes in the monoclinic space group P2(1) (No. 4) with a = 8.931(2) Å, b = 18.303 (3) Å, c = 9.971(2) Å, beta = 90.11(2) degrees, and Z = 2. It contains two rather similar V(IV)-V(V) pairs of VO(6) octahedra distorted as usual having a short V-O bond of around 1.57 Å, a long bond of around 2.40 Å trans to this, and four equatorial bonds around 2.00 Å. The bond lengths of the V(V)O(6) octahedra are significantly shorter than those found for the V(IV)O(6) octahedra. The eight different SO(4)(2)(-) groups are all bridging bidentate between the V(IV) and V(V) atoms; a third oxygen is coordinated to a vanadium atom of a neighboring chain trans to the short V=O bond, and the fourth oxygen remains uncoordinated. The measured bond distances and angles show a considerable distortion of the SO(4) tetrahedra. This is confirmed by the IR spectra of the compound, where large shift and splitting of the sulfate nu(3) bands up to wave numbers of around 1300 cm(-)(1) is observed. The ESR spectra of the compound exhibit weak anisotropy with g(iso) = 1.972 +/- 0.002 and DeltaB(pp) = 65 +/- 2 G. The compound may cause the deactivation for industrial sulfuric acid catalysts observed around 400 degrees C in highly converted SO(2)-O(2)-N(2) gas mixtures.

Journal Article↗
PubMed2001

Solid-state coordination chemistry: structural influences of copper-phenanthroline subunits on oxovanadium organophosphonate phases. hydrothermal synthesis and structural characterization of the two-dimensional materials [Cu(phen)(VO)(O3PCH2PO3)(H2O)], [[Cu(phen)]2(V2O5)(O3PCH2CH2PO3)], and [[Cu(phen)]2(V3O5)(O3PCH2CH2CH2PO3)2(H2O)] and the three-dimensional phase [[Cu(phen)]2(V3O5)(O3PCH2PO3)2(H2O)].

The hydrothermal reactions of CuCl2*2H2O, Na3VO4, 1,10-phenanthroline, and the appropriate organodiphosphonate ligand yield [Cu(phen)(VO)(O3PCH2PO3)(H2O)] (1), [[Cu(phen)]2(V2O5)(O3PCH2CH2PO3)] (2), [[Cu(phen)]2(V3O5)(O3PCH2CH2CH2PO3)2 (H2O)] (3), and [[Cu(phen)]2(V3O5)(O3PCH2PO3)2(H2O)] (4). Compounds 1-3 exhibit two-dimensional structures. The structures exhibit distinct vanadium building blocks: square pyramidal, mononuclear V(IV) sites in 1, a binuclear unit of corner-sharing V(V) tetrahedra in 2, and a trinuclear unit of corner-sharing V(V) square pyramids and a V(IV) octahedron in 3. The network structures of 1 and 2 are constructed from one-dimensional oxovanadium-diphosphonate chains linked by Cu(II) square pyramids into two-dimensional layers. In contrast, compound 3 exhibits a two-dimensional oxovanadium-organodiphosphonate network, with Cu(II) sites decorating the surfaces. Compound 4 is unique in exhibiting a framework structure, which may be described as a three-dimensional oxovanadium-organodiphosphonate substructure with [Cu(phen)]2+ subunits covalently attached to the surface of channels running parallel to the a-axis. The magnetic properties of 1-4 are also correlated to the structural characteristics. The magnetic behavior of 2 is thus dominated by antiferromagnetic interactions. The magnetic behavior of 1 and 4 is consistent with the presence of two distinct paramagnetic metal ions, Cu(II) and V(IV). In contrast, 3 does not exhibit ferrimagnetic behavior, but rather weak antiferromagnetic coupling. Crystal data: 1, C13H10N2CuP2VO8, monoclinic P2(1)/c, a = 9.0656(5) A, b = 8.6584(5) A, c = 20.934(1) A, beta = 97.306(1) degrees, Z = 4; 2, C26H20N4Cu2P2V2O11, triclinic P1, a = 10.6096(5) A, b = 11.6951(5) A, c = 13.1796(6) A, alpha = 71.369(1) degrees, beta = 70.790(1) degrees, gamma = 80.738(1) degrees, Z = 2; 3, C30H28N4Cu2P4V3O18, triclinic P1, a = 9.4356(6) A, b = 10.6556(6) A, c = 11.0354(7) A, alpha = 118.187(1) degrees, beta = 91.416(1) degrees, gamma = 107.821(1) degrees, Z = 1; 4, C26H20N4Cu2P4V3O18, monoclinic, P2(1)/c a = 8.3947(3) A, b = 16.8401(7) A, c = 11.9144(5) A, beta = 93.903(1) degrees, Z = 2.

Journal Article↗
PubMed2006

Follow-up studies on glycosylated flavonoids and their complexes with vanadium: their anti-hyperglycemic potential role in diabetes.

The present study sought to evaluate the hypoglycemic activities of free glycosylated flavonoids and flavonoid complexes with vanadium(IV), (VO(IV)), on glycemia in experimental diabetic rats. Besides free kaempferol-3,7-O-(alpha)-dirhamnoside and kaempferol-3-neohesperidoside, complexes of these flavonoids with VO(IV) were administered by different routes in order to compare the potency of the compounds as well as the efficacy of insulin or VO(IV) in lowering serum glucose. Wistar rats were made diabetic by alloxan. The glycemia was assessed at different times after the administering of compounds. The equilibrium constants were determined by potentiometric study and two species with VO(IV) are proposed at physiological pH, VOH(2)L(2) for kaempferitrin and VOHL for kaempferol-3-neohesperidoside. The latter exhibited hypoglycemic activity at all times examined with 50 and 100 mg/kg and the former reduced the glycemia from 0 to 6h by i.p. route. The administering of the complexes or 0.0146 mmol/kg VO(IV) resulted in a serum glucose-lowering effect over time in the case of i.p. treatment. A marked hypoglycemic effect was observed for 0.5IU of insulin (67.5%); 0.0146 mmol VO(IV) (16.8%); 0.0294 mmol kaempferitrin-VO(IV) (17.8%) and 0.0286 mmol kaempferol-3-neohesperidoside-VO(IV) (56.0%) at 3h after i.p. treatment when compared with respective zero time in diabetic groups. Kaempferol-3-neohesperidoside-VO(IV) was 2.5 times more effective than VO(IV), twice as effective as the free compound and three times more effective than kaempferitrin-VO(IV). This is of particular interest since kaempferol-3-neohesperidoside appears to represent a suitable ligand for VO(IV) to mimic the efficacy of insulin in lowering serum glucose levels.

Animals↗
PubMed1982

The transport and accumulation of oxyvanadium compounds in human erythrocytes in vitro.

Metavanadate, at physiologic pH the oxyanion form of pentavalent vanadium, is a potent reversible inhibitor of the sodium pump. Vanadium must enter cells to inhibit the sodium pump, and metavanadate may be converted to an inactive form inside of cells. Because of these factors and the complex inorganic chemistry of vanadium, we examined the kinetics of vanadium uptake and accumulation in normal erythrocytes in vitro at 37 degrees C. The kinetics of vanadium influx, efflux, and accumulation in erythrocytes in Tris-buffered, isotonic salt medium were fit closely by a model with vanadium in two possible oxidation states and with the vanadium permeating between two compartments. The equation for this model is: (formula: see text) in which subscripts i and o signify "inside" and "outside" the cells, respectively, and k1, k-1, and k2 are rate constants. 48V or EPR of vanadium(IV) gave similar estimates of the concentrations of the components. The k1 was 0.37 +/- 0.06 (S.E.M.) min-1 and k2 was 0.04 +/- 0.01 min-1. In control Tris-medium, k1 exceeded k-1 by a factor of 1.8. After 120 min of incubation in media with initial concentrations of 1, 10, or 100 microM vanadium(V), the total intracellular vanadium concentration exceeded that in the bath 4.5 to 18-fold. Vanadium influx was not appreciably changed by variations of external sodium or glucose levels. The k1 and k-1 were inversely related to external pH over the range 6.5 to 8.2. High O2 tension (95% to 100% O2) caused a decrease in k2, and the lipophilic oxidant, cumene hydroperoxide, accelerated the loss of accumulated vanadium from the cells, indicating that the k2 step represents reduction of vanadium(V) to vanadium(V) within the cells. On the basis of these studies we suggest that the intracellular concentration of vanadium(V), the inhibitor of the sodium pump, is determined by the combined effects of the rate of vanadium influx (dependent on the extracellular concentration of free metavanadate), the rate of vanadium efflux, and the rate of conversion of vanadium(V) to vanadium(IV).

Biological Transport↗
PubMed2004

Activation of aPKC is required for vanadate-induced phosphorylation of protein kinase B (Akt), but not p70S6k in mouse epidermal JB6 cells.

Vanadium is a metal widely distributed in the environment. Although vanadate-containing compounds exert potent toxic effects on a wide variety of biological systems, the mechanisms by which vanadate mediates adverse effects are not well understood. The present study investigated the vanadate-induced phosphorylation of Akt and p70S6K, two kinases known to be vital for cell survival, growth, transformation, and transition of the cell cycle in mammals. Exposure of mouse epidermal JB6 cells to vanadium led to phosphorylation of Akt and p70S6K in a time- and dose-dependent manner. Vanadium exposure also caused translocation of atypical isoforms of PKC (lambda, zeta) from the cytosol to the membrane, but had no effect on PKCalpha translocation, suggesting that the atypical PKCs (aPKC) were specifically involved in vanadium-induced cellular response. Importantly, overexpression of a dominant negative mutant PKClambda blocked Akt phosphorylation at Ser473 and Thr308, whereas it did not inhibit p70S6k phosphorylation at Thr389 and Thr421/Ser424, suggesting that aPKC activation is specifically involved in vanadium-induced activation of Akt, but not in activation of p70S6k. Furthermore, vanadium-induced p70S6k phosphorylation at Thr389 and Thr421/Ser424 and Akt phosphorylation at Thr308 occurred through a PI-3K-dependent pathway because a PI-3K dominant negative mutant inhibited induction as compared with vector control cells. These results indicate that there was a differential role of aPKC in vanadate-induced phosphorylation of Akt and p70S6k, suggesting that signal transduction pathways leading to the activation of Akt and p70S6k were different.

Animals↗
PubMed2003

A vanadium(IV) phosphite with a pillared layered structure: hydrothermal synthesis and characterization of (VO)4(4,4'-bpy)2(HPO3)4.

A novel vanadium(IV) phosphite, (VO)(4)(4,4'-bpy)(2)(HPO(3))(4), was hydrothermally synthesized and characterized by single-crystal X-ray diffraction. This compound crystallizes in the monoclinic system with the space group C2/c and cell parameters a = 35.970(3) A, b = 15.9400(13) A, c = 10.7681(7) A, beta = 101.073(4) degrees, and Z = 8 with R(1) = 0.0482. The structure of the compound consists of trigonal bipyramidal [VO(4)N] and pseudopyramidal [HPO(3)] blocks, which are connected by corner-sharing, to form vanadium phosphite layers in the bc plane. These layers are further linked through 4,4'-bpy pillars, generating a 3D framework. Thermogravimetric analysis and magnetic susceptibility data for this compound are given.

Journal Article↗
PubMed2004

Vanadium(III) complexes with L-cysteine--stability, speciation and the effect on actin in hepatoma Morris 5123 cells.

The complexation processes of vanadium(III) with L-cysteinate and s-methyl-L-cysteinate ligands have been studied in aqueous solutions in the pH range 2-7 by the pH-potentiometric, UV-Vis absorption and CD spectroscopy methods. The equilibria model of complex formation, evaluated by SUPERQUAD program, so as careful inspection of spectroscopic data have allowed to determine the speciation and the coordination mode of vanadium(III) ion in the major species present in aqueous solutions. Relatively stable ML2 species of vanadium(III)-L-cysteinate system exists in aqueous solutions above pH 5. It was deduced from spectral data that the coordination sphere of vanadium(III) ion in V(Cys)2 is completed by oxygen, nitrogen and sulfur atoms of two L-cysteinate ligands. Solution of vanadium(III) with L-cysteine (pH approximately 7, L/M=20) was administrated to the culture medium of hepatoma Morris 5123 growing cells. Cytotoxic effect of this solution towards tumor cells was observed. The viability of these cells depended on the complex concentration. It was reduced by 70% at 100 microM of the vanadium species concentration in the culture medium. The death of cancer cells seems to be induced on apoptotic route. The statistically significant increase of total actin level and filamentous to monomeric actin ratios (F/G) were found in the cytoplasm of cells exposed to the vanadium(III)-L-cysteine complex. It was accompanied by the rearrangement of actin cytoskeleton architecture. These factors are important for migration and metastasis formation of the cancer cells.

Actins↗
PubMed2006

Two new hybrid organic/inorganic copper(II)-oxovanadate(V) diphosphonates: [Cu2(phen)2(O3PCH2PO3)(V2O5)(H2O)] x H2O and [Cu2(phen)2(O3P(CH2)3PO3)(V2O5)] x C3H8. Synthesis, structure, and magnetic properties.

Two new hybrid organic/inorganic copper oxovanadium diphosphonates [Cu2(phen)2(O3PCH2PO3)(V2O5)(H2O)] x H2O (1) and [(Cu2(phen)2(O3P(CH2)3PO3)(V2O5)] x C3H8 (2) have been obtained by hydrothermal synthesis. The compounds are monoclinic, and they crystallize in the space group P2(1)/n with cell parameters of a = 11.788(2) A, b = 17.887(3) A, c = 14.158(2) A, and beta = 93.99(0) degrees and in the space group C2/c with cell parameters of a = 11.025(1) A, b = 18.664(2) A, c = 15.054(2) A, and beta = 90.06(0) degrees, respectively. Both compounds present two-dimensional frameworks built up from infinite chains of corner-sharing vanadium tetrahedra and diphosphonate groups connected by copper tetramers for (1) and copper dimers for (2). The remarkable feature of (2) is the encapsulation of propane molecules, stabilized by strong hydrogen bonding between the layers. The magnetic properties of the compounds have been investigated showing antiferromagnetic coupling with Tmax = 64 K for (1) and Curie-like paramagnetic behavior for (2).

Journal Article↗
PubMed2002

Intracellular signal transduction of cells in response to carcinogenic metals.

Epidemiological and animal studies suggest that several metals and metal-containing compounds are potent mutagens and carcinogens. These metals include chromium, arsenic, vanadium, nickel, and others. During the last two decades, chemical and cellular studies have contributed enormously to our understanding of the mechanisms of metal-induced pathophysiological processes. Although each of these metals is unique in its mechanism of action, some common signaling molecules, such as reactive oxygen species (ROS), may be shared by many of the carcinogenic metals. New techniques are now available to reveal the mechanisms of carcinogenesis in precise molecular terms. In this review, we focused our attentions on carcinogenic metal-induced signal transduction pathways leading to the activation of NF-kappaB, cell apoptosis and cell cycle progression, three crucial steps or events involved in the transformation and carcinogenesis. This review summarizes current knowledge and our recent studies concerning intracellular signal transduction pathways initiated by carcinogenic metals and the cross-talk that occurs among these pathways in cells in response to metals.

Animals↗
PubMed2006

Catalytic reduction of hydrazine to ammonia by a vanadium thiolate complex.

Vanadium(III) thiolate complexes, [V(PS3'')(Cl)]- [1a; PS3'' = P(C6H3-3-Me3Si-2-S)3(3-)] and [V(PS3')(Cl)]- [1b; PS3' = P(C6H3-5-Me-2-S)3(3-)], were synthesized and characterized. Complex 1a serves as a precursor for the catalytic reduction of hydrazine to ammonia. The spectroscopic and electrochemical studies indicate that hydrazine is bound and activated in a V(II) state.

Ammonia↗
PubMed2005

Modeling of crystallization process in confined melt of sulfuric acid catalyst.

Metropolis Monte Carlo technique has been applied to simulate the crystallization process in the melt of vanadium sulfuric acid supported catalysts. The melt is a lattice binary compound consisting of (V4+)(2) and (V5+)(2) binuclear complexes (dimers) confined by pore walls of cylindrical or slitlike shape. It has been shown that the crystallization process retards significantly as the pore size decreases. This result is in good agreement with the experimental data obtained earlier. The effect of the energy properties of pore walls (attractive, repulsive, or inert) on the crystallization features has been studied as well.

Journal Article↗
PubMed2001

Carcinogenic metals and NF-kappaB activation.

Epidemiological and animal studies suggest that several metals and metal-containing compounds are potent mutagens and carcinogens. These metals include chromium, arsenic, vanadium, and nickel. During the last two decades, chemical and cellular studies have contributed enormously to our understanding of the mechanisms of metal-induced pathophysiological processes. Although each of these metals is unique in its mechanism of action, some common signaling molecules, such as reactive oxygen species (ROS), may be shared by many of these carcinogenic metals. New techniques are now available to reveal the mechanisms of carcinogenesis in precise molecular terms. In this review, we focused our attentions on metal-induced signal transduction pathways leading to the activation of NF-kappaB, a transcription factor governing the expression of most early response genes involved in a number of human diseases.

Animals↗
PubMed2004

The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products.

Halogenated natural products are frequently reported metabolites in marine seaweeds. These compounds span a range from halogenated indoles, terpenes, acetogenins, phenols, etc., to volatile halogenated hydrocarbons that are produced on a very large scale. In many cases these halogenated marine metabolites possess biological activities of pharmacological interest. Given the abundance of halogenated marine natural products found in marine organisms and their potentially important biological activities, the biogenesis of these compounds has intrigued marine natural product chemists for decades. Over a quarter of a century ago, a possible role for haloperoxidase enzymes was first suggested in the biogenesis of certain halogenated marine natural products, although this was long before haloperoxidases were discovered in marine organisms. Since that time, FeHeme- and Vanadium-haloperoxidases (V-HPO) have been discovered in many marine organisms. The structure and catalytic activity of vanadium haloperoxidases is reviewed herein, including the importance of V-HPO-catalyzed bromination and cyclization of terpene substrates.

Biological Products↗
PubMed2002

Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the recombinant enzyme.

The vanadium-dependent bromoperoxidase from the marine macro-alga Corallina pilulifera was heterologously expressed in Saccharomyces cerevisiae. The enzyme was purified and crystals in "tear drop" form were obtained. The catalytic properties of the recombinant enzyme were studied and compared with those of the native enzyme purified from C. pilulifera. Differences in thermal stability and chloroperoxidase activity were observed. The recombinant enzyme retained full activity after preincubation at 65 degrees C for 20 min, but the native enzyme was completely inactivated under the same conditions. The chlorinating activity of the native enzyme was more than ten times higher than that of the recombinant enzyme. Other properties, such as K(m) values for KBr and H(2)O(2), and optimal temperature and pH, were similar for each source of C. pilulifera bromoperoxidase.

Bromides↗