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PubMed2006

Removal of arsenate from aqueous solution by adsorption onto titanium dioxide nanoparticles.

Titanium dioxide (TiO2) was investigated for the removal of pentavalent arsenate from aqueous solution. Kinetic results revealed that arsenate adsorption was almost instantaneous. The extent of arsenate adsorption decreased with increasing pH owing to the decrease of positively charged binding sites on the TiO2 surface. Adsorption isotherms measured at pH 3 and 7 generally followed the Langmuir model. The maximum uptake capacity ranged from 8 mg g-1 at pH 3 to 2.7 mg g-1 at pH 7. Addition of phosphate resulted in a significant reduction in arsenate adsorption, indicating that phosphate-a molecular analogue of arsenate-competes with arsenate for the same surface binding sites. By contrast, bicarbonate had little effect on arsenate adsorption, whereas sulfate exhibited a moderate suppression effect. A considerable reduction in arsenate adsorption was also observed in the presence of relatively high concentrations of background electrolytes (>50 mmol L-1).

Adsorption↗
PubMed2005

Adsorption of arsenate and arsenite by iron-treated activated carbon and zeolites: effects of pH, temperature, and ionic strength.

Naturally occurring arsenic contaminates groundwater in many countries, including the United States, at levels greater than 10 microg l(-1), the current WHO guideline value, increasing the risk of skin, lung, bladder, and kidney cancer in millions of people. Arsenic toxicity is dependent on its chemical form; arsenite is more toxic due to its higher affinity for protein than arsenate. This study supports worldwide research efforts to obtain drinking water with arsenic levels below 10 microg l(-1). Batch adsorption kinetic and isotherm studies were conducted to compare and evaluate iron-treated adsorbents for arsenate and arsenite removal from aqueous media. Two iron treatments were investigated as well as the effects of varied pH, temperature, and ionic strength increases on adsorption effectiveness. Adsorbent materials such as activated carbon and naturally occurring zeolites (clinoptilolite and chabazite) were selected because of their relative low cost and because the zeolites are potential point-of-use materials for mitigating arsenic contaminated groundwater. Molecular sieves, Faujasite (13X) and Linde type A (5A) were selected because they provide a basis for comparison with previous studies and represent well-characterized materials. Iron-treated activated carbon and chabazite showed the most promise as low-cost arsenic adsorbents; activated carbon removed approximately 60% of arsenate and arsenite while chabazite removed approximately 50% of arsenate and 30% of arsenite. Modeling arsenate and arsenite adsorption by these adsorbents using the Langmuir and Freundlich isotherm expressions determined the adsorbents' capacity for arsenic removal from aqueous media. Arsenate removal by iron-treated activated carbon and clinoptilolite best fit the Langmuir model. Arsenate removal by iron-treated chabazite and arsenite removal by activated carbon, chabazite, and clinoptilolite best fit the Freundlich model. Applications of iron-modified activated carbon for effective arsenate removal would require pH values between 7 and 11, chabazite between 4 and 5, and clinoptilolite between 3 and 7. Arsenite removal by iron-modified activated carbon would require pH values between 7 and 11, chabazite between 7 and 10, and clinoptilolite between 4 and 11. Increasing temperature improved adsorption performance for activated carbon and the zeolites. Increasing ionic strength improved performance of iron-treated activated carbon and zeolites.

Adsorption↗
PubMed1994

Arsenate reduction mediated by the plasmid-encoded ArsC protein is coupled to glutathione.

Resistance to arsenate conferred on Escherichia coli by the ars operon of plasmid R773 requires both the product of the arsC gene and reduction of arsenate to arsenite. A genetic analysis was performed to identify the source of reducing potential in vivo. In addition to the ars genes, arsenate resistance required the products of the gor gene for glutathione reductase and the gshA and gshB genes for glutathione synthesis. Mutations in the trx and grx genes for thioredoxin and glutaredoxin, respectively, had no effect on arsenate resistance. Although resistance required the arsC gene, the rate of reduction of arsenate to arsenite was nearly the same in cells lacking the ars operon. In strains deficient in glutathione biosynthesis this endogenous reduction was greatly diminished, and cells exhibited increased sensitivity to arsenate. When glutathione was supplied exogenously to such mutants, resistance was restored only to cells expressing the ars operon, and only such cells had detectable arsenate reduction after addition of glutathione. Since ArsC-catalysed reduction of arsenate provides high level resistance, physical coupling of the ArsC reaction to efflux of the resulting arsenite is hypothesised.

Adenosine Triphosphatases↗
PubMed2006

Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2).

Endogenous plant arsenate reductase (ACR) activity converts arsenate to arsenite in roots, immobilizing arsenic below ground. By blocking this activity, we hoped to construct plants that would mobilize more arsenate aboveground. We have identified a single gene in the Arabidopsis thaliana genome, ACR2, with moderate sequence homology to yeast arsenate reductase. Expression of ACR2 cDNA in Escherichia coli complemented the arsenate-resistant and arsenate-sensitive phenotypes of various bacterial ars operon mutants. RNA interference reduced ACR2 protein expression in Arabidopsis to as low as 2% of wild-type levels. The various knockdown plant lines were more sensitive to high concentrations of arsenate, but not arsenite, than wild type. The knockdown lines accumulated 10- to 16-fold more arsenic in shoots (350-500 ppm) and retained less arsenic in roots than wild type, when grown on arsenate medium with <8 ppm arsenic. Reducing expression of ACR2 homologs in tree, shrub, and grass species should play a vital role in the phytoremediation of environmental arsenic contamination.

Amino Acid Sequence↗
PubMed1973

Functioning of the adenine nucleotide transporter in the arsenate uncoupling of corn mitochondria.

Arsenate uncouples mitochondrial respiration in a process stimulated by ADP, inhibited by oligomycin, and competitively inhibited by inorganic phosphate. If mersalyl is added to corn mitochondria to block further transport of accumulated arsenate, the uncoupled respiration continues unabated due to recycling of matrix arsenate. Addition of ADP now inhibits rather than promotes respiration and the mitochondria shrink. It is established by arsenate analyses that arsenate is removed from the matrix. Oligomycin or atractyloside block the removal by inhibiting ADP-arsenate formation or transport, respectively. It is deduced that ADP-arsenate is stable in the membrane and is transported outward for hydrolysis in the external aqueous phase. Hence, ADP-arsenate formed in oxidative phosphorylation is not directly released to the matrix, and a mechanism must exist for its direct transfer to the transporter.

Journal Article↗
PubMed2000

Purification and characterization of ACR2p, the Saccharomyces cerevisiae arsenate reductase.

In Saccharomyces cerevisiae, expression of the ACR2 and ACR3 genes confers arsenical resistance. Acr2p is the first identified eukaryotic arsenate reductase. It reduces arsenate to arsenite, which is then extruded from cells by Acr3p. In this study, we demonstrate that ACR2 complemented the arsenate-sensitive phenotype of an arsC deletion in Escherichia coli. ACR2 was cloned into a bacterial expression vector and expressed in E. coli as a C-terminally histidine-tagged protein that was purified by sequential metal chelate affinity and gel filtration chromatography. Acr2p purified as a homodimer of 34 kDa. The purified protein was shown to catalyze the reduction of arsenate to arsenite. Enzymatic activity as a function of arsenate concentration exhibited an apparent positive cooperativity with an apparent Hill coefficient of 2.7. Activity required GSH and glutaredoxin as the source of reducing equivalents. Thioredoxin was unable to support arsenate reduction. However, glutaredoxins from both S. cerevisiae and E. coli were able to serve as reductants. Analysis of grx mutants lacking one or both cysteine residues in the Cys-Pro-Tyr-Cys active site demonstrated that only the N-terminal cysteine residue is essential for arsenate reductase activity. This suggests that during the catalytic cycle, Acr2p forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase.

Adenosine Triphosphatases↗
PubMed2006

Reduction kinetics of As (V) to As (III) by a dissimilatory arsenate-reducing bacterium, Bacillus sp. SF-1.

This study proposes a kinetic model that accounts for the toxicity of both arsenate and arsenite and characterizes the arsenate reduction ability of a dissimilatory arsenate-reducing bacterium, Bacillus sp. SF-1 as a bioremediation agent. The model results correlated well with a series of batch reduction experiments conducted anaerobically in serum bottles with initial arsenate concentrations of 360, 735, and 1,500 mg-As/L. The reduction rate was expressed by the Haldane equation that describes the inhibitory effect of high concentrations of arsenate. The reduction rate constant k(r), half saturation constant K(S), and inhibition constant K(I) were estimated respectively as 1.2 x 10(9) mg-As/cells/h, 1.5 x 10(2) mg-As/L, and 4.2 x 10(2) mg-As/L. Lethal effects of arsenite that is accumulated as the end-product of arsenate reduction were expressed by the first-order term with a lethal constant of 2.7 x 10(-4) L/mg-As/h. The yield for the bacterial cells by arsenate respiration was estimated at 4.0 x 10(8) cells/mg-As.

Arsenates↗
PubMed1989

The impact of temperature on the acute toxicity of arsenate and arsenite to rainbow trout (Salmo gairdneri).

This research investigated the influence of temperature (5 or 15 degrees C) on the acute toxicity of waterborne arsenite and arsenate to rainbow trout. Trout exposed to arsenate at 5 degrees C had a 144-hr LC50 (95% fiducial limits) of 114.1 (106.7 to 121.9) mg liter-1, twice the value of 58 (50.6 to 66.4) mg liter-1 evident in fish exposed at 15 degrees C. Temperature had no effect on the toxicity of arsenite; 144-hr LC50's at 5 and 15 degrees C were 17.7 (16.5 to 18.9) and 20.7 (19.9 to 21.5) mg liter-1, respectively. When fish were exposed to 70 mg liter-1 arsenate for 72 hr, those held at 15 degrees C had mean whole-body arsenic levels that were five times higher than the levels in fish held at 5 degrees C. There were, however, essentially no differences in the patterns of arsenic uptake between 5 and 15 degrees C when the fish were exposed to arsenate at 0.7 or 1.2 of the 144-hr LC50 at each temperature, a strategy which compensates for (eliminates) temperature as a modifier of toxicity. Fish which were held in arsenate-free water after the 72-hr arsenate exposure depurated significantly more arsenic at 15 degrees C than at 5 degrees C. Despite this, it is apparent that enhanced uptake at 15 degrees C was the overriding factor controlling the differences in the expression of arsenate toxicity at the two temperatures.

Animals↗
PubMed1992

Arsenic-75 nuclear magnetic resonance: study of the interaction of arsenate with various molecules of biological interest.

75As NMR (Nuclear Magnetic Resonance) was used as a probe of arsenate interactions in solution. The linewidth at half-height of the 75As NMR signal of arsenate was studied as a function of solution pH and temperature. Below pH 11.5, the 75As signal was too broad to be detected, but at higher pH, up to pH = 13.5, the signal became much narrower. This indicates that the arsenate species AsO4(3-) is quite symmetric, but the asymmetry of HAsO4(2-) is sufficient to cause extensive quadrupolar relaxation of the 75As nucleus. A full pH range 75As and proton NMR study of the interaction of arsenate with ethanol, ethylene glycol, glycerol, ribose, mannose, glucose, gluconic acid and acetate was undertaken in order to follow arsenate ester formation. The 75As line broadening effects and the proton ligand shifts observed indicate that complexation of arsenate by ribose, mannose, glucose, ethanol, ethylene glycol, and glycerol occurs at pH 12.7. However, no significant interaction is detected by NMR with gluconic acid or acetate. The effect of the nucleoside adenosine is quite small and those of phosphate and of the nucleotides AMP and ADP are negligible. The interaction of arsenate with potential cationic centers, such as the basic amino acids lysine and arginine and some macrocyclic triamines, was also studied. Such interaction depends on the pKa for protonation of the amine groups.

Acetates↗
PubMed2005

Toxicity of arsenate and arsenite on germination, seedling growth and amylolytic activity of wheat.

Effects of different concentrations of arsenite and arsenate (0-16 mg/l) on seed germination, relative root length and shoot height, arsenic accumulation in young seedlings, alpha-amylase, beta-amylase and total amylolytic activity in wheat were investigated in order to elucidate the toxicity of arsenic in the early developmental stage. Germination percentages of different wheat varieties had different responses to arsenic species and decreased significantly with increasing arsenic concentrations except Duokang 1. Relative root length (RRL) and relative shoot height (RSH) of wheat seedlings decreased with increasing concentrations of arsenite and arsenate. The relative root lengths were correlated with the relative shoot heights for arsenite (r2 = 0.79) and arsenate (r2 = 0.77). Arsenic uptake by seedlings increased with the increasing concentrations of arsenite or arsenate and followed the Michaelis-Menten kinetics function. The average total amylolytic activity and beta-amylase activity had no significant difference comparable to that of controls at the concentration 2 mg/l arsenite or arsenate, but decreased apparently when the concentration was higher than 2 mg/l. Whereas the alpha-amylase activity decreased with increasing concentrations of arsenite or arsenate over the whole concentration range. Arsenite decreased all the endpoints more remarkably than arsenate. In comparison, shoot height and root length were more sensitive to arsenic than other endpoints and might be used as indicators for arsenic toxicity.

Arsenates↗
PubMed2006

Arsenate reduction: thiol cascade chemistry with convergent evolution.

The frequent abundance of arsenic in the environment has guided the evolution of enzymes for the reduction of arsenate. The arsenate reductases (ArsC) from different sources have unrelated sequences and structural folds, and can be divided into different classes on the basis of their structures, reduction mechanisms and the locations of catalytic cysteine residues. The thioredoxin-coupled arsenate reductase class is represented by Staphylococcus aureus pI258 ArsC and Bacillus subtilis ArsC. The ArsC from Escherichia coli plasmid R773 and the eukaryotic ACR2p reductase from Saccharomyces cerevisiae represent two distinct glutaredoxin-linked ArsC classes. All are small cytoplasmic redox enzymes that reduce arsenate to arsenite by the sequential involvement of three different thiolate nucleophiles that function as a redox cascade. In contrast, the ArrAB complex is a bacterial heterodimeric periplasmic or a surface-anchored arsenate reductase that functions as a terminal electron acceptor and transfers electrons from the membrane respiratory chain to arsenate. Finally, the less well documented arsenate reductase activity of the monomeric arsenic(III) methylase, which is an S-adenosylmethionine (AdoMet)-dependent methyltransferase. After each oxidative methylation cycle and before the next methylation step, As(V) is reduced to As(III). Methylation by this enzyme is also considered an arsenic-resistance mechanism for bacteria, fungi and mammals.

Animals↗
PubMed2005

Arsenate removal from water using sand--red mud columns.

This study describes experiments in which sorption filters, filled with chemically modified red mud (Bauxsol) or activated Bauxsol (AB) coated sand, are used to remove As(V) (arsenate) from water. Bauxsol-coated sand (BCS) and AB-coated sand (ABCS) are prepared by mixing Bauxsol or AB with wet sand and drying. Samples of the BCS and ABCS are also used in batch experiments to obtain isotherm data. The observed adsorption data fit the Langmuir model well, with adsorption maxima of 3.32 and 1.64 mgg(-1) at pH values of 4.5 and 7.1, respectively for BCS; and of 2.14 mgg(-1) for ABCS at a pH of 7.1. Test results show that higher arsenate adsorption capacities can be achieved for both BCS and ABCS when using the columns compared to results for batch experiments; the difference is greater for BCS. Additional batch tests, carried out for 21 days using BCS to explain the observed discrepancy, show that the equilibrium time previously used in batch experiments was too short because adsorption continued for at least 21 days and reached 87% after 21 days compared to only 35% obtained after 4h. Fixed bed column tests, used to investigate the effects of flow rate and initial arsenate concentration indicate that the process is sensitive to both parameters, with lower flow rates (longer effective residence times in the columns) and initial arsenate concentrations providing better column performance. An examination of the combined effect of potential competing anions (i.e. silicate, phosphate, sulphate and bicarbonate) on the column performance showed that the presence of these anions in tap water slightly decreases arsenate removal. Each breakthrough curve is compared to the Thomas model, and it is found that the model may be applied to estimate the arsenate sorption capacity in columns filled with BCS and ABCS. The data obtained from both batch and column studies indicate that BCS and ABCS filtration could be effectively used to remove arsenate from water, with the latter being more efficient.

Adsorption↗
PubMed2000

Respiration of arsenate and selenate by hyperthermophilic archaea.

A novel, strictly anaerobic, hyperthermophilic, facultative organotrophic archaeon was isolated from a hot spring at Pisciarelli Solfatara, Naples, Italy. The rod-shaped cells grew chemolithoautotrophically with carbon dioxide as carbon source, hydrogen as electron donor and arsenate, thiosulfate or elemental sulfur as electron acceptor. H2S was formed from sulfur or thiosulfate, arsenite from arsenate. Organotrophically, the new isolate grew optimally in the presence of an inorganic electron acceptor like sulfur, selenate or arsenate. Cultures, grown on arsenate and thiosulfate or arsenate and L-cysteine, precipitated realgar (As2S2). During growth on selenate, elemental selenium was produced. The G+C content of the DNA was 58.3 mol%. Due to 16S rRNA gene sequence analysis combined with physiological and morphological criteria, the new isolate belongs to the Thermoproteales order. It represents a new species within the genus Pyrobaculum, the type species of which we name Pyrobaculum arsenaticum (type strain PZ6*, DSM 13514, ATCC 700994). Comparative studies with different Pyrobaculum-species showed, that Pyrobaculum aerophilum was also able to grow organotrophically under anaerobic culture conditions in the presence of arsenate, selenate and selenite. During growth on selenite, elemental selenium was formed as final product. In contrast to P. arsenaticum, P. aerophilum could use selenate or arsenate for lithoautotrophic growth with carbon dioxide and hydrogen.

Anaerobiosis↗
PubMed2003

A potential mechanism for the impairment of nitric oxide formation caused by prolonged oral exposure to arsenate in rabbits.

We have recently found evidence for impairment of nitric oxide (NO) formation and induction of oxidative stress in residents of an endemic area of chronic arsenic poisoning in Inner Mongolia, China. To investigate the underlying mechanisms responsible for these phenomena, a subchronic animal experiment was conducted using male New Zealand White rabbits. After 18 weeks of continuous exposure of rabbits to 5 mg/l of arsenate in drinking water, a significant decrease in systemic NO production occurred, as shown by significantly reduced plasma NO metabolites levels (76% of control) and a tendency towards decreased serum cGMP levels (81.4% of control). On the other hand, increased oxidative stress, as shown by significantly increased urinary hydrogen peroxide (H(2)O(2)) (120% of control), was observed in arsenate-exposed rabbits. In additional experiments measuring aortic tension, the addition of either the calcium ionophore A23187 or acethylcholine (ACh) induced a transient vasoconstriction of aortic rings prepared from arsenate-exposed rabbits, but not in those prepared from control animals. This calcium-dependent contractility action observed in aorta rings from arsenate-exposed rabbits was markedly attenuated by the superoxide (O2(.-)) scavenging enzyme Cu, Zn-SOD, as well as diphenyleneiodonium (DPI) or N(G)-nitro-L-arginine methyl ester (L-NAME), which are inhibitors for nitric oxide synthase (NOS). However, the cyclooxygenase inhibitor indomethacin or the xanthine oxidase blocker allopurinol had no effect on this vasoconstriction. These results suggest that arsenate-mediated reduction of systemic NO may be associated with the enzymatic uncoupling reaction of NOS with a subsequent enhancement of reactive oxygen species such as O2(.-), an endothelium-derived vasoconstricting factor. Furthermore, hepatic levels of (6R)-5,6,7,8-tetrahydro-L-biopterin (BH(4)), a cofactor for NOS, were markedly reduced in arsenate-exposed rabbits to 62% of control, while no significant change occurred in cardiac L-arginine levels. These results suggest that prolonged exposure of rabbits to oral arsenate may impair the bioavailability of BH(4) in endothelial cells and, as a consequence, disrupt the balance between NO and O2(.-) produced from endothelial NOS, such that enhanced free radicals are produced at the expense of NO.

Acetylcholine↗
PubMed2001

Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme.

BACKGROUND: In Escherichia coli bearing the plasmid R773, resistance to arsenite, arsenate, antimonite, and tellurite is conferred by the arsRDABC plasmid operon that codes for an ATP-dependent anion pump. The product of the arsC gene, arsenate reductase (ArsC), is required to efficiently catalyze the reduction of arsenate to arsenite prior to extrusion. RESULTS: Here, we report the first X-ray crystal structures of ArsC at 1.65 A and of ArsC complexed with arsenate and arsenite at 1.26 A resolution. The overall fold is unique. The native structure shows sulfate and sulfite ions binding in the active site as analogs of arsenate and arsenite. The covalent adduct of arsenate with Cys-12 in the active site of ArsC, which was analyzed in a difference map, shows tetrahedral geometry with a sulfur-arsenic distance of 2.18 A. However, the corresponding adduct with arsenite binds as a hitherto unseen thiarsahydroxy adduct. Finally, the number of bound waters (385) in this highly ordered crystal structure approaches twice the number expected at this resolution for a structure of 138 ordered residues. CONCLUSIONS: Structural information from the adduct of ArsC with its substrate (arsenate) and with its product (arsenite) together with functional information from mutational and biochemical studies on ArsC suggest a plausible mechanism for the reaction. The exceptionally well-defined water structure indicates that this crystal system has precise long-range order within the crystal and that the upper limit for the number of bound waters in crystal structures is underestimated by the structures in the Protein Data Bank.

Arsenates↗
PubMed1995

Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773.

The ArsC protein encoded by the arsenical resistance operon of plasmid R773 catalyzes the reduction of arsenate to arsenite in Escherichia coli. The reductase has been shown to require glutathione and glutaredoxin, suggesting that thiol chemistry might be involved in the reaction mechanism. The ArsC arsenate reductase has two cysteinyl residues, Cys12 and Cys106. By a combination of random and site-specific mutagenesis, Cys12 was altered to four other amino acid residues. Cells expressing any of those arsC genes were sensitive to arsenate. The ArsCC12S protein was purified and found to be catalytically inactive. Cys106 was altered separately to seryl, glycyl, and valyl residues. Cells expressing arsCC106S, arsCC106G, and arsCC106V genes retained arsenate resistance, and the purified C106S and C106G proteins had reductase activity. Both wild-type ArsC and C106S proteins were inactivated by iodoacetate. In the native enzyme only Cys12 was alkylate by iodoacetate; Cys106 was alkylated only if the enzyme was first denatured. In the presence of the substrate, arsenate, or competitive inhibitors, phosphate or sulfate, the rate of alkylation was reduced. Reductase activity was inhibited by N-ethylmaleimide and could be protected by arsenate. These results suggest Cys12 is an active-site residue essential for catalysis by the arsenate reductase.

Adenosine Triphosphatases↗
PubMed2002

Rates of hydrous ferric oxide crystallization and the influence on coprecipitated arsenate.

Arsenate coprecipitated with hydrous ferric oxide (HFO) was stabilized against dissolution during transformation of HFO to more crystalline iron (hydr)oxides. The rate of arsenate stabilization approximately coincided with the rate of HFO transformation at pH 6 and 40 degrees C. Comparison of extraction data and X-ray diffraction results confirmed that hematite and goethite were the primary transformation products. HFO transformation was significantly retarded at or above an arsenate solid loading of 29 455 mg As/kg HFO. However, HFO transformation proceeded at a significant rate for arsenate solid loadings of 4208 and 8416 mg As/kg HFO. At a solid loading of 8416 mg As/kg HFO, XRD results suggested arsenate primarily partitioned to hematite. Comparison of HFO transformation rates observed in this research to rates obtained from the literature at pH 6 and temperatures ranging from 24 to 70 degrees C suggests that arsenate stabilization could be realized in oxic environments with a significantfraction of iron (hydr)oxides. While this process has not been documented in natural systems, the predicted half-life for transformation of an arsenic-bearing HFO is approximately 300 days at 25 degrees C at solid loading < 8415 mg As/kg HFO. The projected time frame for arsenate stabilization indicates this process should be considered during development of conceptual and analytical models describing arsenic fate and transport in oxic systems containing reactive iron (hydr)oxides. The likelihood of this process would depend on the chemical dynamics of the soil or sediment system relative to iron (hydr)oxide precipitation-dissolution reactions and the potential retarding/competing influence of ions such as silicate and organic matter.

Arsenates↗
PubMed2006

Thyrotoxicity of sodium arsenate, sodium perchlorate, and their mixture in zebrafish Danio rerio.

Both perchlorate and arsenate are environmental contaminants. Perchlorate is a definitive thyroid disruptor, and arsenic may disrupt thyroid homeostasis via multiple pathways. To evaluate the effects of sodium perchlorate and sodium arsenate on thyroid function and possible interactions between them, zebrafish (Danio rerio) were exposed to sodium perchlorate (10 and 100 mg/L), sodium arsenate (1 and 10 mg/L), and the mixture sodium perchlorate + sodium arsenate (10 + 1 and 100 + 10 mg/ L) for up to 90 days. At day 10, 30, 60, and 90, fish were sampled and analyzed forthyroid histopathological end points including follicular cell height, follicle size, colloid size, colloid depletion, hyperplasia, and angiogenesis. Effects on epithelial cell height (hypertrophy) were seen as early as 10 days after exposure. Perchlorate induced changes in all parameters staring at 30 days of exposure. Prolonged perchlorate exposure induced angiogenesis, a relatively new marker of thyroid disruption. Sodium arsenate was less effective than sodium perchlorate in causing thyroid histopathologies, but transient responses were seen for hypertrophy, hyperplasia, and colloid depletion (% colloid). This is the first report of arsenate-induced effects on thyroid histopathology. However, because statistically significant effects were not consistently seen in all end points, evidence for arsenate as a thyroid disruptor remains equivocal. In general, the sensitivity of the following histopathological indicators for indicating thyroid perturbations is, in descending order: follicular cell height > percent of colloid area/follicle area > colloid area/follicular cell height > hyperplasia > angiogenesis > colloid area >follicle area = fish growth.

Angiogenesis Inducing Agents↗