Disease relevance of Chromic ion

• The redox reaction between CrO(4)(2-) and the fully reduced three-heme cytochrome c(7) from Desulfuromonas acetoxidans to give chromium(III) and the fully oxidized protein has been followed by NMR spectroscopy [1].
• Chromium(III) complexes currently being sold as dietary supplements were tested for their ability to cause chromosomal aberrations in Chinese hamster ovary cells [2].
• When chromium(III) was given at weekly intervals mice accumulated 6 times more chromium by 8 weeks than chromium(VI)-treated mice, though only the latter showed symptoms of chronic toxicity [3].
• In this study, we have employed the Salmonella reversion assay to identify mutagenic Cr(III) complexes [4].
• Pseudomonas aeruginosa azurin is stoichiometrically and specifically labeled upon reduction by Cr(II)aq ions, yielding a substitution-inert Cr(III) adduct on the protein surface [5].

Psychiatry related information on Chromic ion

• A yield of Cr(III) equal to that obtained at pH 2.5 and pH 3.1 in about 7 and 25h, respectively, was reached at pH 4.2 only after a much longer reaction time (50h) [6].

High impact information on Chromic ion

• The distance between the copper center and the suggested Cr(III) binding site is approximately 12 A. The intervening region contains an array of highly invariant aromatic residues [7].
• The emission intensity and its pH dependence observed for the tyrosines in this tryptophan-devoid protein differ markedly in the Cr(III) adduct [7].
• This study concludes that both the environmental contaminant Cr(VI) and the nutritional supplement Cr(III) increase DNA deletions in vitro and in vivo, when ingested via drinking water [8].
• We determined the effects of Cr(VI) as potassium dichromate and Cr(III) as chromium(III) chloride on the frequencies of DNA deletions measured with the deletion assay in Saccharomyces cerevisiae and the in vivo p(un) reversion assay in C57BL/6J p(un)/p(un) mice [8].
• The models predict that chromium(III) can accumulate in human tissues to reach the levels at which DNA damage has been observed in animals and in vitro [9].

Chemical compound and disease context of Chromic ion

• The relative stability of the inner sphere complexes of chromium(III) and glutathione or ATP is probably not a significant factor in determining the toxicity of chromium(III) complexes [10].
• The results of this study demonstrate that the mutagenic Cr(III) complexes identified in the Salmonella reversion assay display characteristics of reversibility and positive shifts of the Cr(III)/Cr(II) redox couple consistent with the ability of these Cr(III) complexes to serve as cyclical electron donors in a Fenton-like reaction [4].
• Chromium reduction by Escherichia coli ATCC 33456 quantitatively transferred hexavalent chromium, Cr(VI), to trivalent chromium, Cr(III) [11].
• Significant quantities of Ag(I), Cu(II), and Cr(III) were bound to isolated Bacillus subtilis 168 walls, Escherichia coli K-12 envelopes, kaolinite and smectite clays, and the corresponding organic material-clay aggregates (1:1, wt/wt) [12].
• In this study, the extremely radiation-resistant bacterium Deinococcus radiodurans, which naturally reduces Cr(VI) to the less mobile and less toxic Cr(III), was engineered for complete toluene degradation by cloned expression of tod and xyl genes of Pseudomonas putida [13].

Biological context of Chromic ion

• No DNA damage was detected in either liver or kidney nuclei after chromium(III) treatment, using the technique of alkaline elution [14].
• While the F1-catalyzed ATP hydrolysis activity was lost rapidly upon chemical modification or cold treatment, the ability of the enzyme to produce Pi . adenosine 5'-diphosphate (chromium(III) salt) from phosphate and monodentate adenosine 5'-diphosphate (chromium(III) salt) was unimpaired [15].
• The beta, gamma-bidentate chromium(III) complex of ATP (CrATP) was used as a substrate analog to stabilize a form of the Ca(2+)-ATPase of the sarcoplasmic reticulum containing both of the bound calcium ions in an occluded state without enzyme phosphorylation [16].
• At low Cr(III) concentration (r = 1:40), the number of Cr(III) ions bound to DNA were 6-7 cations/500 base pairs, and this increased to 30-35 cations/500 base pairs at high metal ion content (r = 1:4) [17].
• In this study, we have examined the mechanism of chromium(III) [Cr(III)]-induced cytotoxicity with respect to its relationship to oxidative stress [18].

Anatomical context of Chromic ion

• This study was designed to investigate the interaction of calf thymus DNA with Cr(VI) and Cr(III) in aqueous solution at pH 6.5-7.5, using Cr(VI)/DNA(P) molar ratios (r) of 1:20 to 2:1 and Cr(III)/DNA(P) molar ratios (r) of 1:80 to 1:2 [17].
• F1I, the specific ATPase inhibitor protein, and the chromium(III) analogs of ATP and ADP, CrATP and CrADP, were used to study the inhibition of Pi goes to and comes from ATP exchange reaction catalyzed by beef heart submitochondrial particles [19].
• The first systematic study of XANES spectra of Cr(III) complexes formed in Cr(VI)-treated mammalian cells (A549, HepG2, V79, and C2C12 cell lines), and in subcellular fractions of A549 cells, has been performed using a library of XANES spectra of model Cr(III) complexes [20].
• Cytotoxicity studies of chromium(III) complexes on human dermal fibroblasts [21].
• We show that chromium(VI), but not chromium(III), can oxidize ascorbate both in cells and in a cell-free system [22].

Associations of Chromic ion with other chemical compounds

• The in vitro HAH1/WDp interaction is metalospecific; HAH1 preincubated with Cu(2+) or Hg(+) but not with Zn(2+), Cd(2+), Co(2+), Ni(3+), Fe(3+), or Cr(3+) interacted with WDp [23].
• Exploring the capabilities of X-ray absorption spectroscopy for determining the structure of electrolyte solutions: computed spectra for Cr(3+) or Rh(3+) in water based on molecular dynamics [24].
• The results of multiple linear regression analyses of XANES spectra, in combination with multiple-scattering fits of XAFS spectra, indicate that Cr(III) formed in Cr(VI)-treated cells is most likely to bind to carboxylato, amine, and imidazole residues of amino acids, and to a lesser extent to hydroxo or aqua ligands [20].
• This chloride ligand is formed in a redox process from the solvent and is responsible for the oxidation of surface Cr(II) to Cr(III) [25].
• Isolated calf thymus nuclei bound a chromium(III) glutathione complex in a time-dependent manner [26].

Gene context of Chromic ion

• Co(2+) decreased catalase expression while Cr(3+) increased it in a dose- and time-dependent manner [27].
• Here, we show that Cr(3+) increased the T(4)-binding capacity of wild-type (WT) and amyloidogenic V30M-TTR [28].
• In this report we describe the results of a kinetic analysis of the effects of the addition of Cr(III) pyrophosphate (Cr-PPi) to the OPRTase and HGPRTase assay solutions, which delineates further the differences between these enzyme activations by metal ions [29].
• Only one of the two sites in lactoferrin allows displacement of Cr(III) by Fe(III) [30].
• Genes encoding proteins associated with general (e.g., groL and dnaJ) and membrane (e.g., pspBC) stress were also upregulated, particularly under U(VI)-reducing conditions, pointing to membrane damage by the solid-phase reduced U(IV) and Cr(III) and/or the direct effect of the oxidized forms of the metals [31].

Analytical, diagnostic and therapeutic context of Chromic ion

• Titration with increasing amounts of tris(1,10-phenanthroline) chromium(III) shows changes in the NMR spectrum that are inconsistent with a single binding site [32].
• Using high performance liquid chromatography (HPLC), the formation of 8-hydroxy-2-deoxyguanosine (8-OH-dG) in purified calf thymus DNA treated with the Fenton reagents, chromium(III) (as CrCl3) plus hydrogen peroxide (H2O2) (Cr(III)/H2O2), was measured in the presence or absence of the antioxidants alone or in combination with melatonin [33].
• Speciation of chromium(III) and cobalt(III) (amino)carboxylate complexes using capillary electrophoresis [34].
• Chromium adsorption and precipitation, as observed by transmission electron microscopy coupled with energy dispersive X-ray spectroscopy (TEM/EDS), revealed that the surfaces of the cells were uniformly stained with bound Cr(III) and amorphous precipitates (as determined by selected area electron diffraction; SAED) [35].
• Following exposure of approximately 10(6) cells to 0.4 mM Cr(III) for 4 h, the Cr uptake by single cells was less than 10(-)(14) g/cell (as determined by GFAAS analysis and as confirmed by PIXE analysis where the Cr concentration was below the limit of detection) [36].

References