Disease relevance of dioxido-dioxo-molybdenum

• The molybdate-dependent transcriptional regulator (ModE) from Escherichia coli functions as a sensor of molybdate concentration and a regulator for transcription of operons involved in the uptake and utilization of the essential element, molybdenum [1].
• Some of the most interesting positive results observed include 4-hydroxyphenyl retinamide plus tamoxifen in breast cancer, piroxicam in colon cancer, dimethylfluoroornithine in breast and bladder cancer, oltipraz in lung cancer, dehydroepiandrosterone in colon cancer, and molybdate in bladder cancer [2].
• Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29413 [3].
• The X-ray structures of the cytoplasmic molybdate-binding protein ModG from Azotobacter vinelandii in two different crystal forms have been determined [4].
• It resembles the molybdate-stabilized complexes in cytosols of other human and rodent, malignant and healthy tissues, and the complex detected in breast tumor cytosol containing leupeptin, a bacterial protease inhibitor [5].

Psychiatry related information on dioxido-dioxo-molybdenum

• In presence of 20 mM molybdate ion and a reaction time of 0.5-2 h at 0-2 degrees C, we are able to detect the appearance of a [6.7-3H]-17,21-dimethyl-19-nor-4,9-pregnadiene-3,20-dione ([3H]-R5020) and [3H]-progesterone binding moiety in human prostatic cytosol [6].

High impact information on dioxido-dioxo-molybdenum

• De-repression of nif transcriptional units is coordinate and molybdate is required for maximal expression of the structural gene operon, which is autogenously regulated [7].
• High doses of molybdate, a potent PTPase inhibitor, block the phosphorylation of p42MAPK and entry into the cell cycle [8].
• Lower doses of molybdate delay both p42MAPK phosphorylation and the release from cell cycle arrest, but once cells have re-entered the cell cycle, they continue with near-normal timing [8].
• A monoclonal antibody BF4 raised against the purified, molybdate-stabilized, 8S progesterone receptor (8S-PR) from chick oviduct, recognizes 8S forms of all steroid hormone receptors [9].
• Effects of molybdate and endogenous inhibitors on steroid-receptor inactivation, transformation, and translocation [10].

Chemical compound and disease context of dioxido-dioxo-molybdenum

• Mol- mutants of Klebsiella pneumoniae requiring high levels of molybdate for nitrogenase and nitrate reductase activity were characterized [11].
• These data suggest that in the absence of the high-affinity molybdate transport system, E. coli utilizes sulfate and selenite transport systems for transporting molybdate, preferring sulfate transport over the selenite transport system [12].
• Organoautotrophic growth of Alcaligenes eutrophus on formate was dependent on the presence of molybdate in the medium [13].
• A Na+:H+ antiporter and a molybdate transporter are essential for arsenite oxidation in Agrobacterium tumefaciens [14].
• Azotobacter vinelandii produces siderophores with different metal-binding properties, depending on the concentration of Fe(III) and molybdate in the growth medium [15].

Biological context of dioxido-dioxo-molybdenum

• Crystal structure of the molybdate binding protein ModA [16].
• Molybdate is admitted to the otherwise inaccessible type 2 binding sites by the movement of the N-terminal residues of each protein chain [17].
• Cnx1E catalyzes the Zn(2+)-/Mg(2+)-dependent hydrolysis of MPT-AMP but only when molybdate is bound as co-substrate [18].
• The modABCD operon, located at 17 min on the Escherichia coli chromosome, encodes the protein components of a high affinity molybdate uptake system [19].
• The molybdate-independent mutant ModE proteins apparently mimic in its conformation the native ModE-molybdate complex, which binds to a DNA sequence motif of TATAT-7bp-TAYAT [20].

Anatomical context of dioxido-dioxo-molybdenum

• Sucrose gradient ultracentrifugation analyses of total cytosol and of affinity gel effluents show a heterogenous pattern of ABS from 10 to 40 S, unchanged by 0.4 M KCl and limited trypsinization (which however provoke transitions of ER from 8S to 4S forms) and by 20 mM molybdate (which stabilizes the 8S form of ER and prevents large aggregates) [21].
• In a cell-free system, hsp90 binding to receptor was stabilized by molybdate but disrupted by high salt [22].
• Degradation without apparent change in size of molybdate-stabilized nonactivated glucocorticoid-receptor complexes in rat thymus cytosol [23].
• However, in liver extracts this effect on lysosomal proteases required high concentrations of vanadate (K1 = 500 microM) and was also observed with molybdate, unlike the inhibition of ATP-dependent proteolysis in reticulocytes [24].
• The effect of molybdate on adenylate cyclase (EC 4.6.1.1) in rat liver plasma membranes has been examined [25].

Associations of dioxido-dioxo-molybdenum with other chemical compounds

• The effect of anaerobic pregrowth on the inhibition of molybdate reduction by added nitrate indicates that in vivo nitrate reduction responds to growth conditions in the same manner as biotin sulfoxide reductase does [26].
• In the presence of 10 mM molybdate ion, we are able to detect the appearance of a [6,7-3H]-17,21-dimethyl-19-nor-4,9-pregnadiene-3,20-dione-([3H]R5020) binding moiety in human prostatic cytosol which sedimented at approximately 8S in a glycerol density gradient [27].
• Ah receptor in human placenta: stabilization by molybdate and characterization of binding of 2,3,7,8-tetrachlorodibenzo-p-dioxin, 3-methylcholanthrene, and benzo(a)pyrene [28].
• These observations support the proposal that molybdate and tungstate are interacting through a reversible association with the glucocorticoid receptor itself [29].
• Vanadate (1 mM) and molybdate (100 microM) increased insulin-dependent phosphorylation of pp160 by 3-fold when tested separately and 7-fold in combination [30].

Gene context of dioxido-dioxo-molybdenum

• However, inclusion of 20 mM molybdate in the homogenizing buffer did significantly protect unliganded Ah receptor from thermal inactivation at 20 degrees C and from KCl-induced loss of ligand-binding ability [31].
• In contrast, treatment of permeabilized cells with orthovanadate, vanadyl sulfate, molybdate, and tungstate at the same range of concentrations does not result in the accumulation of activated Stat1 alpha molecules in the absence of ligand [32].
• Expression of modA and modBC was induced by starvation for molybdate [3].
• In addition, we demonstrate that AhR/ARNT dimerization, but not nuclear translocation of the AhR, is inhibited by molybdate [33].
• Mutant constructs containing deletions of secondary structural elements from the N- and C-termini of Cdk2 were prepared and assayed for their ability to coadsorb Hsp90 and Cdc37 in a salt-stable high-affinity manner with and without the addition of molybdate [34].

Analytical, diagnostic and therapeutic context of dioxido-dioxo-molybdenum

• (i) Molybdate and modulator inhibit receptor activation as measured by DNA-cellulose binding, DEAE-cellulose chromatography, and Sepharose 4B gel filtration [35].
• Molybdate was an essential buffer component for receptor stabilization during cell fractionation and sedimentation analysis [36].
• After gel filtration in the presence and absence of molybdate, the per cent of labeled receptors binding to DNA-cellulose was 57 +/- 10% and 83 +/- 1%, respectively [37].
• After filtration in the presence and absence of molybdate, the S20,w of labeled receptors was 4.2 +/- 0.2 and 4.4 +/- 0.1 S, respectively [37].
• To investigate this process we have characterized cytoplasmic complexes formed in rat thymocytes at 0 and 37 degrees C. Complexes in cytosols stabilized with molybdate were analyzed by sucrose gradient centrifugation and by chromatography on DNA-cellulose, DEAE-cellulose, and agarose gels [38].

References