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PubMed1992

Molybdate and tungstate act like vanadate on glucose metabolism in isolated hepatocytes.

In rat hepatocytes, molybdate and tungstate inactivate glycogen synthase by a mechanism independent of Ca2+ and activate glycogen phosphorylase by a Ca(2+)-dependent mechanism. On the other hand, both molybdate and tungstate increase fructose 2,6-bisphosphate levels and counteract the decrease in this metabolite induced by glucagon. These effectors do not directly modify 6-phosphofructo-2-kinase activity, even though they partially counteract the inactivation of this enzyme induced by glucagon. These effects are related to an increase on the glycolytic flux, as indicated by the increase in L-lactate and CO2 production and the decrease in glucose 6-phosphate levels in the presence of glucose. All these effects are similar to those previously reported for vanadate, although molybdate and tungstate are less effective than vanadate. These results could indicate that molybdate, tungstate and vanadate act on glucose metabolism in isolated hepatocytes by a similar mechanism of action.

Animals↗

PubMed1996

Possible involvement of a tyrosine kinase-dependent pathway in the regulation of phosphoinositide metabolism by vanadate in normal mouse islets.

The potential roles of protein tyrosine kinases (TKs) and of phosphotyrosine phosphatases (PTPs) in pancreatic islet function are not known. In this study, we investigated whether vanadate, a potent PTP inhibitor, affects phosphoinositide (PI) metabolism by a TK-dependent pathway in isolated mouse islets. To avoid the confounding effects of changes in Ca2+ influx, all experiments were performed in the absence of Ca2+. In the presence of 15mM glucose, vanadate, acetylcholine (ACh) or [Arg]vasopressin (AVP) strongly stimulated InsP production. Vanadate also increased PtdInsP levels in membranes. The TK inhibitor genistein (not its inactive analogues genistin and daidzein) significantly reduced vanadate effects, but was without effect in the absence of stimulation or in the presence of ACh or AVP. Islet proteins resolved by SDS/PAGE were analysed by immunobloting with anti-phosphotyrosine antibody. Under control conditions, several phosphotyrosyl-proteins (PYPs) were present. Vanadate increased phosphotyrosine residues on several PYPs, notably two proteins of 145 and 85 kDa. This effect was prevented by genistein, p145 and p85 could correspond to phospholipate Cgamma(PLCgamma) and the regulatory subunit of PtdIns-3-kinase (PtdIns-3K) respectively. Both proteins are expressed in islets, as revealed by immunoblots with specific antibodies. Tungstate, another PTP inhibitor, reproduced vanadate effects, but inhibition of PtdIns-3K by wortmannin failed to affect vanadate-increased PtdInsP levels. Incubation of the islets in the presence of 10% (v/v) fetal calf serum instead of BSA increased InsP production and this effect was prevented by genistein. These results suggest that inhibition of PTP increases InsP production in mouse islets by a TK-dependent pathway. They also provide evidence for a potential role of TK and PTP in pancreatic B-cell function.

Acetylcholine↗

PubMed1995

Enamel surfaces after orthodontic bracket debonding.

The enamel surfaces of extracted teeth were studied clinically and with a scanning electron microscope following debonding of orthodontic attachments and subsequent polishing. Excess orthodontic resin was removed with tungsten carbide burs and abrasive discs. Several combinations of polishing agents were evaluated. The no. 30 fluted tungsten carbide bur appeared to be the most efficient method of removing highly filled resin, and it produced the least amount of scarring. A polishing sequence was developed which used resin points and cups followed by a water slurry of fine pumice and brown and green cups. This procedure was tested clinically and appeared to return the enamel to an acceptable condition. This procedure is fast, efficient, and comfortable for the patient.

Aluminum Oxide↗

PubMed1999

Optimization of a procedure for rebonding dislodged orthodontic brackets.

The purpose of this study was to compare shear bond strength (SBS) of bonded and rebonded orthodontic brackets following a variety of commonly used conditioning treatments and using both light-cured and self-cured composite resin systems. Brackets debonded during the initial determination of SBS were rebonded after the removal of residual resin from enamel surfaces using five different treatments: (1) Remove residual resin using a tungsten carbide bur, re-etch enamel surface, then bond a new bracket; (2) Remove resin from the base mesh with micro-etching then rebond the same bracket, (3) Remove residual resin from the enamel surface using resin-removing pliers, recondition the enamel with an air-powder polisher, then bond a new bracket; (4) Remove residual resin using a rubber cup and pumice, then bond a new bracket; (5) Remove residual resin using pliers alone, then bond a new bracket. The results revealed that the light-cured system produced higher shear bond strength in the initial bond than the self-cured system (p<0.005). Reconditioning the enamel surfaces using a tungsten carbide bur and acid-etching gave the highest SBS (difference 5.8 MPa; p<0.01) and clinically favorable fracture characteristics. The data suggest that the optimal procedure for rebonding dislodged orthodontic brackets is to resurface the enamel using a tungsten carbide bur, acid-etch the enamel, and use a new or re-use an old bracket after microetching.

Acid Etching, Dental↗

PubMed1999

A scanning electron microscopic evaluation of root surfaces and the gutta-percha interface following root-end resection in vitro.

AIM: The aim of this study was to evaluate the effects that various commonly used instruments have on root surface morphology, the obturating material, and the interface between the obturation and the root canal walls following root-end resection in vitro. METHODOLOGY: Sixty human single-rooted teeth with fully formed apices were collected and decoronated. The root canals were instrumented, and then obturated with thermoplasticized gutta-percha using AH-26 as the sealer. The roots were randomly divided into 12 different groups, and apical root-end resections were performed using eight different instrument configurations, and two different directions in which the bur moved across the root face in relation to its direction of rotation. Epoxy resin replicas of the resected root ends were examined using scanning electron microscopy. RESULTS: Each instrument produced a characteristic surface finish on the resected root end that mirrored its cutting profile. Irrespective of the design of the bur used, smearing and shredding of the gutta-percha across the root face occurred only when the handpiece was moved across the root face in reverse direction in relation to the direction of rotation of the bur. CONCLUSIONS: To ensure minimal disruption and distortion of the root filling and to prevent shredding of the gutta-percha interface, care should be taken to ensure that the final pass of the bur across the root canal is in the correct direction in relation to its direction of rotation.

Bismuth↗

PubMed1997

Comparative evaluation of polishing systems on the surface of three aesthetic materials.

This study compared the efficacy of three different polishing methods on a resin composite, a glass ionomer cement (GIC) and a compomer. Thirty samples of each material were prepared. Ten of them were randomly assigned to one of the three polishing methods. The surface roughness (Ra) of the samples were measured before and after the polishing procedure with a profilometer. There was no statistical difference between the composite and the compomer prior to polishing but statistical difference was found between the GIC and the two other materials. After polishing, the smoothest surfaces were obtained using Sof-Lex discs for the three materials, and the roughest surface, with tungsten carbide burs for the composite and the compomer, and with Enhance kit for the GIC. The composite gave the smoothest surface with the three methods.

Compomers↗

PubMed2001

Surface roughness and wettability of enamel and dentine surfaces prepared with different dental burs.

The aim of dental adhesive restorations is to produce a long lasting union between the restoration and the tooth structure. This bond depends on many variables including the geometry of the preparation and the type of bonding agent or luting cement. It is therefore suggested that the topography of the tooth surface may influence the wettability and the bonding quality of adhesive systems. This study measured the surface roughness and wettability of enamel and dentine after preparation with different dental burs. The mesial and distal surfaces of 15 extracted sound human premolar teeth were prepared with a tungsten carbide crown bur, a diamond bur and a tungsten carbide finishing bur and finished in enamel or dentin, respectively. The prepared surfaces were analysed with a surface profilometer and scanning electron microscopy (SEM). The contact angle of distilled water on each of the prepared surfaces was used as the measure of wettability. The differences in average surface roughness (Ra) were significant between the rotary instrument groups, as revealed by a two-way ANOVA test. No differences were detected between enamel and dentine surfaces prepared with the same type of dental bur. The smoothest surfaces were those completed with tungsten carbide finishing burs. The diamond bur preparations were intermediate in the roughness assessment and the tungsten carbide crown burs gave the roughest surfaces. There were no significant differences in the contact angle measurements for the various groups. It was concluded that the surface roughness of enamel and dentine prepared by different rotary instruments had no significant influence on the wettability of distilled water on these surfaces.

Analysis of Variance↗

PubMed1997

A selenium-dependent and a selenium-independent formylmethanofuran dehydrogenase and their transcriptional regulation in the hyperthermophilic Methanopyrus kandleri.

The genome of Methanopyrus kandleri was found to harbour a gene, fwuB, predicted to encode the catalytic subunit of a tungsten formylmethanofuran dehydrogenase with an active site selenocysteine, and a second gene, fwcB, encoding a tungsten formylmethanofuran dehydrogenase with an active site cysteine. Northern blot and primer-extension analysis revealed that both genes were differentially transcribed. During growth of the methanogen on medium supplemented with selenium only fwuB was transcribed, whereas transcription of both fwuB and fwcB was observed on selenium-deprived medium. Growth of M. kandleri was stimulated by tungstate and selenite but not by molybdate. The findings indicate that the hyperthermophilic archaeon contains two tungsten isoenzymes of formylmethanofuran dehydrogenase, one of which is a novel selenium enzyme. They also indicate that the hyperthermophilic methanogen probably does not contain a molybdenum formylmethanofuran dehydrogenase which appears to be present only in thermophilic and mesophilic methanogens.

Aldehyde Oxidoreductases↗

PubMed2003

The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: purification and properties.

NAD-dependent formate dehydrogenase (FDH1) was isolated from the alpha-proteobacterium Methylobacterium extorquens AM1 under oxic conditions. The enzyme was found to be a heterodimer of two subunits (alpha1beta1) of 107 and 61 kDa, respectively. The purified enzyme contained per mol enzyme approximately 5 mol nonheme iron and acid-labile sulfur, 0.6 mol noncovalently bound FMN, and approximately 1.8 mol tungsten. The genes encoding the two subunits of FDH1 were identified on the M. extorquens AM1 chromosome next to each other in the order fdh1B, fdh1A. Sequence comparisons revealed that the alpha-subunit harbours putative binding motifs for the molybdopterin cofactor and at least one iron-sulfur cluster. Sequence identity was highest to the catalytic subunits of the tungsten- and selenocysteine-containing formate dehydrogenases characterized from Eubacterium acidaminophilum and Moorella thermoacetica (Clostridium thermoaceticum). The beta-subunit of FDH1 contains putative motifs for binding FMN and NAD, as well as an iron-sulfur cluster binding motif. The beta-subunit appears to be a fusion protein with its N-terminal domain related to NuoE-like subunits and its C-terminal domain related to NuoF-like subunits of known NADH-ubiquinone oxidoreductases.

Amino Acid Sequence↗

PubMed1998

Effect of molybdate and tungstate on the biosynthesis of CO dehydrogenase and the molybdopterin cytosine-dinucleotide-type of molybdenum cofactor in Hydrogenophaga pseudoflava.

The molybdenum-containing iron-sulfur flavoprotein CO dehydrogenase is expressed in a catalytically fully competent form during heterotrophic growth of the aerobic bacterium Hydrogenophaga pseudoflava with pyruvate plus CO. We have adopted these conditions for studying the effect of molybdate (Mo) and tungstate (W) on the biosynthesis of CO dehydrogenase and its molybdopterin (MPT) cytosine-dinucleotide-(MCD)-type molybdenum cofactor. W was taken up by the Mo transport system and, therefore, interfered with Mo transport in an antagonistic way. Depletion of Mo from the growth medium as well as inclusion of excess W both resulted in the absence of intracellular Mo and led to the biosynthesis of CO dehydrogenase species of proper L2M2S2 subunit structure that carried the two 2Fe:2S type-I and type-II centers and two FAD molecules. EPR, ultraviolet/visible and CD spectroscopies established the full functionality of the cofactors. Due to the absence of the Mo-MCD cofactor, the enzyme species were catalytically inactive. Unexpectedly, the following cytidine nucleotides were present in inactive CO dehydrogenase: CDP, dCDP, CMP, dCMP, CTP or dCTP. The sum of cytidine nucleotides was two/mol enzyme. The binding specificities of inactive CO dehydrogenase for cytidine nucleotides (oxy > deoxy; diphosphate > monophosphate > triphosphate), and the absence of MPT suggest that, in active CO dehydrogenase, the cytidine diphosphate moiety of Mo-MCD provides the strongest interactions with the protein and determines the specificity for the type of nucleotide. In H. pseudoflava, the biosynthesis of MPT (identified as form A) was independent of Mo. Mo was, however, strictly required for the conversion of MPT to MCD (identified as form-A-CMP) as well as the insertion of Mo-MCD into CO dehydrogenase. These data support a model for the involvement of Mo in the biosynthesis of the Mo-MCD cofactor and of fully functional CO dehydrogenase in which the synthesis and insertion of Mo-MCD require Mo, and protein synthesis including integration of the FeS-centers and FAD are independent of Mo.

Aldehyde Oxidoreductases↗

PubMed1999

Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase.

The involvement of the strictly conserved Trp354 residue in the catalysis of the Yersinia protein tyrosine phosphatase (PTPase) has been investigated by site-directed mutagenesis and kinetic studies. Crystallographic structural data have revealed that Trp354 interacts with the active site Arg409 and is located at one of the hinge positions of the flexible surface loop (WpD loop) which also harbors the general acid/base (Asp356) essential for catalysis [Schubert, H. L., Fauman, E. B., Stuckey, J. A., Dixon, J. E. & Saper, M. A. (1995) Protein Sci. 4, 1904-1913]. Two mutants were constructed and expressed that contained the Trp354-->Phe and Trp354-->Ala substitutions. The K(m) of the W354F and W354A mutants were not significantly different from that of the wild-type. However, a major decrease in the affinity for oxyanions was observed for the mutants, which is consistent with Trp354 playing a role in aligning Arg409 for oxyanion binding. In addition replacement of Trp354 with Phe or Ala caused a decrease in kcat of 200-fold and 480-fold, respectively, and impaired the ability of the mutant enzymes to stabilize the negative charge in the leaving group at the transition state. In fact, the W354F and W354A mutants exhibited catalytic efficiency and leaving group dependency similar to those observed for the general acid-deficient PTPase D356N. These results indicate that Trp354 is an important residue that keeps the WpD loop in a catalytically competent conformation and positions the general acid/base Asp356 in the correct orientation for proton transfer.

Arsenates↗

PubMed1999

Selenium-containing xanthine dehydrogenase from Eubacterium barkeri.

A specific dehydrogenase, different from nicotinic acid hydroxylase, was induced during growth of Eubacterium barkeri on xanthine. The protein designated as xanthine dehydrogenase was enriched 39-fold to apparent homogeneity using a three-step purification scheme. It exhibited an NADP-dependent specific activity of 164 micromol xanthine oxidized per min and per mg of protein. In addition it showed an NADPH-dependent oxidase and diaphorase activity. A molecular mass of 530 kDa was determined for the native enzyme and SDS/PAGE revealed three types of subunits with molecular masses of 17.5, 30 and 81 kDa indicating a dodecameric native structure. Molybdopterin was identified as the molybdenum-complexing cofactor using activity reconstitution experiments and fluorescence measurements after KI/I2 oxidation. The molecular mass of the cofactor indicated that it is of the dinucleotide type. The enzyme contained iron, acid-labile sulfur, molybdenum, tungsten, selenium and FAD at molar ratios of 17.5, 18.4, 2.3, 1.1, 0.95 and 2.8 per mol of native enzyme. Xanthine dehydrogenase was inactivated upon incubation with arsenite, cyanide and different purine analogs. Reconstitution experiments of xanthine dehydrogenase activity by addition of selenide and selenite performed with cyanide-inactivated enzyme and with chloramphenicol-treated cells, respectively, indicated that selenium is not attached to the protein in a covalently bound form such as selenocysteine.

Animals↗

PubMed2006

Bulk photochromism in a tungstate-phosphate glass: a new optical memory material?

In this work, we present a new photochromic tungstate based glass which have both absorption coefficient and refractive index modified under laser exposure. The photosensitive effect is superficial under ultraviolet (UV) irradiation but occurs in the entire volume of the glass under visible irradiation. The effect can be obtained in any specific point inside the volume using an infrared femtosecond laser. In addition, the photosensitive phenomenon can be erased by specific heat treatment. This glass can be useful to substitute actual data storage supports and is a promising material for 3-dimensional (3D) and holographic optical storage.

Glass↗

PubMed2002

Iatrogenic tooth abrasion comparisons among composite materials and finishing techniques.

STATEMENT OF PROBLEM: Many different rotary instruments are available for shaping composite restorations. Whether use of these instruments causes undesirable iatrogenic abrasion of either the tooth surface or the composite restorative material is unknown. Assuming that damage occurs, which technique is least damaging is unknown. PURPOSE: This in vitro study quantified the loss of surface enamel and dentin surrounding Class V preparations during composite shaping and finishing procedures. The susceptibility of 2 types of composites to tooth abrasion was also examined. MATERIALS AND METHODS: Standardized Class V cavities were prepared at the amelodentinal junction of 36 human molar teeth. The teeth were randomly assigned to 6 groups of 6 teeth each. They were restored with either a low- or high-viscosity composite (Revolution or Prodigy Condensable, respectively) and finished with aluminum oxide disks, tungsten carbide burs, or ultrafine finishing diamond burs. The preparations were profiled before and after restoration. After each finishing procedure, morphological measurements of surface changes in the dentin and enamel were made and reported as volume (in cubic millimeters); maximum depth, mean maximum depth, and mean depth (in micrometers); and surface area (in square millimeters). The results were subjected to a 2-way analysis of variance for restorative material and finishing technique (P<.05). RESULTS: Aluminum oxide disks removed significantly less enamel than tungsten carbide burs or ultrafine finishing diamond burs, as measured by volume, maximum depth, mean maximum depth, mean depth, and surface area (P<.05). Conversely, aluminum oxide disks removed significantly greater dentin than either tungsten carbide burs or ultrafine finishing burs as measured by loss of volume, mean depth, and surface area (P<.05). There was no significant difference in the loss of surrounding tooth substance based on resin type (low or high viscosity). CONCLUSION: Within the limitations of this study, the 3 finishing systems tested resulted in varying degrees of iatrogenic abrasion of enamel and dentin. The composite material used had no significant effect on abrasion of the surrounding enamel or dentin.

Aluminum Oxide↗

PubMed2003

The magnitude of cutting forces at high speed.

STATEMENT OF THE PROBLEM: Previous research has used a range of cutting forces for preparing teeth, but there are no data available on the forces actually imposed while cutting teeth with high-speed handpieces. PURPOSE: The purpose of this study was to measure the forces imposed while cutting teeth with tungsten carbide burs used in high-speed handpieces. MATERIAL AND METHODS: Thirty-one dentists each cut 8 conventional class II MO and DO preparations in intact extracted third molars, by use of 2 different air turbine handpieces with different torque-speed characteristics. Two different flat fissure, plain and cross-cut tungsten carbide burs, cutting wet and dry in each handpiece/bur combination. The teeth were mounted in a custom-made transducer unit that displayed the forces imposed by the bur. Data were analysed with a 1-way ANOVA (alpha =.05) and Spearman correlation test. RESULTS: The results showed that there was no significant difference in the applied force between plain and cross-cut burs, cutting wet or cutting dry, but there was a significant difference between the high and the lower torque handpieces. The higher torque handpiece was used at a mean cutting force of 1.44 N and the lower torque handpiece at 1.20 N (P<.002). The overall general mean force observed was 1.30 N. CONCLUSION: It was concluded that the forces used in cutting teeth with the tungsten carbide burs tested related both to the type of the handpiece and to the forces chosen by clinical operators. There was no difference between the plain and cross-cut burs, there was no difference between the cutting wet or dry, and the higher torque handpiece required a higher mean cutting force.

Analysis of Variance↗

PubMed1986

In vitro synthesis of the iron-molybdenum cofactor of nitrogenase.

Molybdate- and ATP-dependent in vitro synthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase requires the protein products of at least the nifB, nifN, and nifE genes. Extracts of FeMo-co-negative mutants of Klebsiella pneumoniae and Azotobacter vinelandii with lesions in different genes can be complemented for FeMo-co synthesis. Both K. pneumoniae and A. vinelandii dinitrogenase (component I) deficient in FeMo-co can be activated by FeMo-co synthesized in vitro. Properties of the partially purified dinitrogenase activated by FeMo-co synthesized in vitro were comparable to those of dinitrogenase from the wild-type organism; e.g., ratios of acetylene- to nitrogen-reduction activities, as well as those of acetylene reduction activities to EPR spectrum peak height at g = 3.65, were very similar. A. vinelandii mutants UW45 and CA30 have mutations in a gene functionally equivalent to nifB of K. pneumoniae.

Acetylene↗

PubMed1996

The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications.

X-ray crystal structures of the Yersinia tyrosine phosphatase (PTPase) in complex with tungstate and nitrate have been solved to 2. 4-A resolution. Tetrahedral tungstate, WO42-, is a competitive inhibitor of the enzyme and is isosteric with the substrate and product of the catalyzed reaction. Planar nitrate, NO3-, is isosteric with the PO3 moiety of a phosphotransfer transition state. The crystal structures of the Yersinia PTPase with and without ligands, together with biochemical data, permit modeling of key steps along the reaction pathway. These energy-minimized models are consistent with a general acid-catalyzed, in-line displacement of the phosphate moiety to Cys403 on the enzyme, followed by attack by a nucleophilic water molecule to release orthophosphate. This nucleophilic water molecule is identified in the crystal structure of the nitrate complex. The active site structure of the PTPase is compared to alkaline phosphatase, which employs a similar phosphomonoester hydrolysis mechanism. Both enzymes must stabilize charges at the nucleophile, the PO3 moiety of the transition state, and the leaving group. Both an associative (bond formation preceding bond cleavage) and a dissociative (bond cleavage preceding bond formation) mechanism were modeled, but a dissociative-like mechanism is favored for steric and chemical reasons. Since nearly all of the 47 invariant or highly conserved residues of the PTPase domain are clustered at the active site, we suggest that the mechanism postulated for the Yersinia enzyme is applicable to all the PTPases.

Amino Acid Sequence↗

PubMed1998

Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1.

The crystal structures of the protein-tyrosine phosphatase SHP-1 catalytic domain and the complex it forms with the substrate analogue tungstate have been determined and refined to crystallographic R values of 0.209 at 2.5 A resolution and 0.207 at 2.8 A resolution, respectively. Despite low sequence similarity, the catalytic domain of SHP-1 shows high similarity in secondary and tertiary structures with other protein-tyrosine phosphatases (PTPs). In contrast to the conformational changes observed in the crystal structures of PTP1B and Yersinia PTP, the WPD loop (Trp419-Pro428) in the catalytic domain of SHP-1 moves away from the substrate binding pocket after binding the tungstate ion. Sequence alignment and structural analysis suggest that the residues in the WPD loop, especially the amino acid following Asp421, are critical for the movement of WPD loop on binding substrates and the specific activity of protein-tyrosine phosphatases. Our mutagenesis and kinetic measurements have supported this hypothesis.

Amino Acid Sequence↗