@article {DI2021100753,
	title = {Evaluation of La(XT), a novel lanthanide compound, in an OVX rat model of osteoporosis},
	journal = {Bone Reports},
	volume = {14},
	year = {2021},
	month = {02/2021},
	pages = {100753},
	abstract = {<p>Purpose The purpose of this study was to evaluate the efficacy and toxicity of a novel lanthanum compound, La(XT), in an ovariectomized (OVX) rat model of osteoporosis. Methods Twenty-four ovariectomized female Sprague Dawley rats were divided into 3 groups receiving a research diet with/without treatment compounds (alendronate: 3\&nbsp;mg/kg; La(XT) 100\&nbsp;mg/kg) for three months. At the time of sacrifice, the kidney, liver, brain, lung and spleen were collected for histological examination. The trabecular bone structure of the tibiae was evaluated using micro-CT and a three-point metaphyseal mechanical test was used to evaluate bone failure load and stiffness. Results No significant differences were noted in plasma levels of calcium, phosphorus, creatinine, alanine aminotransferase (ALT), and aspartate aminotransferase (AST) between the La(XT) treatment compared to the non-treated OVX group. Alendronate-treated animals (positive control) showed higher BV/TV, Tb.N and lower Tb.Th and Tb.Sp when compared to the non-treated OVX group. Mechanical analysis indicated that stiffness was higher in the alendronate (32.88\%, p\&nbsp;=\&nbsp;0.04) when compared to the non-treated OVX group. Failure load did not differ among the groups. Conclusions No kidney or liver toxicities of La(XT) treatments were found during the three-month study. The absence of liver and kidney toxicity with drug treatment for 3\&nbsp;months, as well as the increased trabecular bone stiffness are encouraging for the pursuit of further studies with La(XT) for a longer duration of time.</p>},
	keywords = {La(XT), LANTHANUM, osteoporosis, OVX, TOXICITY},
	issn = {2352-1872},
	doi = {https://doi.org/10.1016/j.bonr.2021.100753},
	url = {https://www.sciencedirect.com/science/article/pii/S2352187221000085},
	author = {Yunyun Di and Ellen K. Wasan and Jacqueline Cawthray and Jaweria Syeda and Munawar Ali and David M.L. Cooper and Ahmad Al-Dissi and Nima Ashjaee and Wubin Cheng and James Johnston and David M. Weekes and Thomas I. Kostelnik and Chris Orvig and Kishor M. Wasan}
}
@article {1112,
	title = {Chromatographic separation and identification of products from the reaction of dimethylarsinic acid with hydrogen sulfide},
	journal = {Chemical Research in Toxicology},
	volume = {18},
	number = {12},
	year = {2005},
	note = {ISI Document Delivery No.: 004XYTimes Cited: 24Cited Reference Count: 44},
	month = {Dec},
	pages = {1821-1829},
	type = {Article},
	abstract = {The reaction of dimethylarsinic acid (DMA(V)) with hydrogen sulfide (H2S) is of biological significance and may be implicated in the overall toxicity and carcinogenicity of arsenic. The course of the reaction in aqueous phase was monitored, and an initial product, dimethylthioarsinic acid, was observed by using LC-ICP-MS and LC-ESI-MS. Dimethylarsinous acid was observed as a minor product. A second slower-forming product was identified, and the electrospray mass chromatograms for this species produced ions at m/z 275, 171, and 137 in positive mode. To aid in the identification of this slower-forming product, crystalline standards of sodium dimethyldithioarsinate and dimethylarsino dimethyldithioarsinate were prepared and re-characterized by using improved spectroscopic and structural analysis techniques. An aqueous solution of sodium dimethyldithioarsinate produced a single major chromatographic peak that matched the retention time (7.6 min) of the slower-forming product and contained similar molecular ions at m/z 275, 171, and 137 via LC-ESI-MS. The dimethylarsino dimethyldithioarsinate standard produced four aqueous phase species one of which coeluted with the slower forming product. This coeluting peak also produced the identical ESI-MS ions as the slower-forming product of DMA(V) + H2S. ESI-MS/MS experiments conducted on sodium dimethyldithioarsinate in deuterated water produced molecular ions at m/z 276, 173, and 137. Subsequent collisionally activated dissociation (CAD) experiments on m/z 276 did not produce a product ion at m/z 173. These data indicate that two different species are present in solution, while NMR data indicate that only dimethyldithioarsinic acid exists in aqueous solutions. This discrepancy was investigated by conducting NMR studies on the acidic solution of sodium dimethyldithioarsinate after taking this solution to dryness. The resolubilized solution produced a proton NMR signal characteristic of dimethylarsino dimethyldithioarsinate. Therefore, it was concluded that the ESI-MS ion at m/z 275 associated with the slowly forming second reaction product and the sodium dimethyldithioarsinate compound is a product of the ESI desolvation process.},
	keywords = {CRYSTAL-STRUCTURE, DIMETHYLDITHIOARSINATE, GLUTATHIONE, METABOLITE, ORGANIC ARSENIC COMPOUNDS, RATS, REARRANGEMENT, TOXICITY, TRIMETHYLARSINE OXIDE, urine},
	isbn = {0893-228X},
	url = {<Go to ISI>://000234787200005},
	author = {Fricke, M. W. and Zeller, M. and Sun, H. and Lai, V. W. M. and Cullen, W. R. and Shoemaker, J. A. and Witkowski, M. R. and Creed, J. T.}
}
@article {1204,
	title = {Synthesis and characterization of dual function vanadyl, gallium and indium curcumin complexes for medicinal applications},
	journal = {Journal of Inorganic Biochemistry},
	volume = {99},
	number = {11},
	year = {2005},
	note = {ISI Document Delivery No.: 984RUTimes Cited: 22Cited Reference Count: 41},
	month = {Nov},
	pages = {2217-2225},
	type = {Article},
	abstract = {Novel bis[4-hydroxy-3-methoxyphenyl]-1,6-heptadiene-3,5-dione (curcumin) complexes with the formula, ML3, where M is Ga(III) or In(III), or of the formula, ML2 where M is [Vo](2+), have been synthesized and characterized by mass spectrometry, infrared and absorption spectroscopies, and elemental analysis. A new ligand, bis[4-acetyl-3-hydroxyphenyl]-1,6-heptadiene-3,5-dione (diacetylbisdemethoxycurcumin, DABC) was similarly characterized; an X-ray structure analysis was performed. Vanadyl complexes tested in an acute i.p. testing protocol in STZ-diabetic rats showed a lack of insulin enhancing potential. Vanadyl complexes were, however, more cytotoxic than were the ligands alone in standard MTT (3-[4,5-dimethylthiazole-2-yl]ate, -2.5-diphenyl-tetrazolium bromide) cytotoxicity testing, using mouse lymphoma cells. With the exception of DABC, that was not different from VO(DABC)(2), the complexes were not significantly different from one another, with IC50 values in the 5-10 mu M range. Gallium and indium curcumin complexes had IC50 values in the same 5-10 mu M range; whereas Ga(DAC)(3) and In(DAC)(3) (where DAC = diacetylcurcumin) were much less cytotoxiC (IC50 = 20-30 mu M). Antioxidant capacity was decreased in VO(DAC)(2), Ga(DAC)(3), and In(DAC)(3),, compared to vanadyl, gallium and indium curcumin, corroborating the importance of curcumin{\textquoteright}s free phenolic OH groups for scavenging oxidants, and correlated with reduced cytotoxic potential. (c) 2005 Elsevier Inc. All rights reserved.},
	keywords = {ANALOGS, antioxidant capacity, ANTIOXIDANT MECHANISM, ANTITUMOR ACTIVITY, BINDING, COORDINATION CHEMISTRY, curcumin, cytotoxicity, DERIVATIVES, diacetylcurcumin, gallium, GROUP, indium, INSULIN MIMICS, MANGANESE COMPLEXES, RADICAL SCAVENGING ABILITY, TOXICITY, VANADIUM},
	isbn = {0162-0134},
	url = {<Go to ISI>://000233322800012},
	author = {Mohammadi, K. and Thompson, K. H. and Patrick, B. O. and Storr, T. and Martins, C. and Polishchuk, E. and Yuen, V. G. and McNeill, J. H. and Orvig, Chris}
}
@article {929,
	title = {Evidence of hemoglobin binding to arsenic as a basis for the accumulation of arsenic in rat blood},
	journal = {Chemical Research in Toxicology},
	volume = {17},
	number = {12},
	year = {2004},
	note = {ISI Document Delivery No.: 881XKTimes Cited: 45Cited Reference Count: 74},
	month = {Dec},
	pages = {1733-1742},
	type = {Article},
	abstract = {Four trivalent arsenic species, inorganic arsenite (iAs(III)), monomethylarsonous acid (MMA(III)), dimethylarsinous acid (DMA(III)), and phenylarsine oxide ((PhAsO)-O-III), have shown increasing binding affinity with the hemoglobin (Hb) of rats and humans. The binding stoichiometry was consistent with the number of reactive cysteine residues in the alpha and beta chains of Hb. Comparing the binding affinity of rat Hb and human Hb for the same trivalent arsenic species, rat Hb was 3-16 times stronger than human Hb as demonstrated by their apparent binding constants. Comparative experiments involving incubation of human and rat red blood cells (RBC) with iAs(III), MMA(III), and DMA(III) showed that 15-30-fold more arsenic species were bound to the Hb of rat RBC than that of human RBC. In vivo experiments using rats fed with an arsenic-supplemented diet showed that arsenic in RBC of the rats was predominantly found in the protein-bound form. Further characterization by nanoelectrospray mass spectrometry of the arsenic species in the RBC of these rats confirmed that most arsenic was bound to the alpha chain of Hb. Taken together, these results suggest that the stronger binding affinity of these arsenic species to rat Hb is responsible for the accumulation of arsenic in rat blood. The results provide a chemical basis to explain the previously observed intriguing difference in the retention of arsenic in the human and the rat. The techniques and approaches described can be applied to the studies of arsenic interactions with other functional proteins.},
	keywords = {ACUTE PROMYELOCYTIC LEUKEMIA, CULTURED HUMAN-CELLS, dimethylarsinous acid, DNA-DAMAGE, HUMAN URINE, METHYLATED METABOLITES, MONOMETHYLARSONOUS ACID MMA(III), TOXICITY, TRIOXIDE, TRIVALENT},
	isbn = {0893-228X},
	url = {<Go to ISI>://000225902600023},
	author = {Lu, M. L. and Wang, H. L. and Li, X. F. and Lu, X. F. and Cullen, W. R. and Arnold, L. L. and Cohen, S. M. and Le, X. C.}
}
@article {647,
	title = {Interaction of trivalent axsenicals with metallothionein},
	journal = {Chemical Research in Toxicology},
	volume = {16},
	number = {7},
	year = {2003},
	note = {ISI Document Delivery No.: 702UQTimes Cited: 53Cited Reference Count: 625th International Conference on Arsenic Exposure and Health EffectsJUL 14-18, 2002SAN DIEGO, CALIFORNIA},
	month = {Jul},
	pages = {873-880},
	type = {Proceedings Paper},
	abstract = {Arsenic is a human carcinogen, causing skin, bladder, and lung cancers. Although arsenic in drinking water affects millions of people worldwide, the mechanism(s) of action by which arsenic causes cancers is not known. Arsenic probably exerts some toxic effects by binding with proteins. However, few experimental data are available on arsenic-containing proteins in biological systems. This study reports on arsenic interaction with metallothionein and established binding stoichiometries between metallothionein and the recently discovered trivalent metabolites of arsenic metabolism. Size exclusion chromatography with inductively coupled plasma mass spectrometry analysis of reaction mixtures between trivalent arsenicals and metallothionein clearly demonstrated the formation of complexes of arsenic with metallothionein. Analysis of the complexes using electrospray quadrupole time-of-flight tandem mass spectrometry revealed the detailed binding stoichiometry between arsenic and the 20 Cys residues in the metallothionein molecule. Inorganic arsenite (As-III) and its two trivalent methylation metabolites, monomethylarsonous acid (MMA(III)) and dimethylarsinous acid (DMA(III)), readily bind with metallothionein. Each metallothionein molecule could bind with up to six As-III, 10 MMA(III), and 20 DMA(III) molecules, consistent with the coordination chemistry of these arsenicals. The findings on arsenic interaction with proteins are useful for a better understanding of arsenic health effects.},
	keywords = {ARSENIC METABOLITES, ENZYMATIC METHYLATION, GLUTATHIONE-REDUCTASE, HUMAN URINE, INORGANIC ARSENICALS, MONOMETHYLARSONOUS ACID MMA(III), PYRUVATE-DEHYDROGENASE, RABBIT LIVER, THIOREDOXIN REDUCTASE, TOXICITY},
	isbn = {0893-228X},
	url = {<Go to ISI>://000184243200009},
	author = {Jiang, G. F. and Gong, Z. L. and Li, X. F. and Cullen, W. R. and Le, X. C.}
}
@article {5045,
	title = {Determination of trivalent methylated arsenicals in biological matrices},
	journal = {Toxicology and Applied Pharmacology},
	volume = {174},
	number = {3},
	year = {2001},
	note = {ISI Document Delivery No.: 464KTTimes Cited: 129Cited Reference Count: 67},
	month = {Aug},
	pages = {282-293},
	type = {Article},
	abstract = {The enzymatically catalyzed oxidative methylation of As yields methylated arsenicals that contain pentavalent As (As-V). Because trivalent As (As-III) is the favored substrate for this methyltransferase, methylated arsenicals containing As-V are reduced to trivalency in cells. Methylated arsenicals that contain As-III are extremely potent inhibitors of NADPH-dependent flavoprotein oxidoreductases and potent cytotoxins in many cell types. Therefore, the formation of methylated arsenicals that contain As-III may be properly regarded as an activation step, rather than a means of detoxification. Recognition of the role of methylated arsenicals that contain As-III in the toxicity and metabolism of As emphasizes the need for analytical methods to detect and quantify these species in biological samples. Hence, a method was developed to exploit pH-dependent differences in the generation of arsines from inorganic and methylated arsenicals that contain either As-V or As-III. Reduction with borohydride at pH 6 generated arsines from inorganic As-III, methyl As-III, and dimethyl As-III, but not from inorganic As-V, methyl As-V, and dimethyl As-V. Reduction with borohydride at pH 2 or lower generated arsines from arsenicals that contained either As-V or As-III. Arsines are trapped in a liquid nitrogen-cooled gas chromatographic trap, which is subsequently warmed to allow separation of the hydrides by their boiling points. Atomic absorption spectrophotometry is used to detect and quantify the arsines. The detection limits (ng As ml(-1)) for inorganic As-III, methyl As-III, and dimethyl As-III are 1.1, 1.2, and 6.5, respectively. This method has been applied to the analysis of arsenicals in water, human urine, and cultured cells. Both methyl As-III. and dimethyl As-III are detected in urine samples from individuals who chronically consumed inorganic As-contaminated water and in human cells exposed in vitro to inorganic As-III. The reliable quantitation of inorganic and methylated arsenicals that contain As-III. in biological samples will aid the study of the toxicity of these species and may provide a new biomarker of the effects of chronic exposure to As. (C) 2001 Academic Press.},
	keywords = {analysis, arsenic, atomic absorption spectrophotometry, biological matrices, CANCER MORTALITY, DIABETES-MELLITUS, DIMETHYLARSINIC ACID, DOSE-RESPONSE RELATIONSHIP, DRINKING-WATER, ENZYMATIC, HUMAN URINE, HYDRIDE GENERATION, MAMMALIAN SYSTEMS, MASS-SPECTROMETRY, METABOLISM, methylated arsenic, METHYLATION, MONOMETHYLARSONOUS ACID MMA(III), pentavalent arsenic, STABILITY, TOXICITY, trivalent arsenic},
	isbn = {0041-008X},
	url = {<Go to ISI>://000170532300010},
	author = {Del Razo, L. M. and Styblo, M. and Cullen, W. R. and Thomas, D. J.}
}
@article {4921,
	title = {Characterization of dissolved tannins and their metal-ion complexes by electrospray ionization mass spectrometry},
	journal = {Analytica Chimica Acta},
	volume = {411},
	number = {1-2},
	year = {2000},
	note = {ISI Document Delivery No.: 305EYTimes Cited: 25Cited Reference Count: 51},
	month = {May},
	pages = {91-102},
	type = {Article},
	abstract = {Electrospray mass spectrometry was used to characterize metal-complexing ligands derived from tannic acid, a component of natural dissolved organic matter. Complexes formed by tannin ligands with copper and other biogeochemically important metals were identified from the mass-to-charge ratios of the corresponding deprotonated molecular ions, allowing stoichiometry and metal oxidation state to be determined. Ligand ion intensities were proportional to tannic acid concentration, with detection limits on the order of 5 nM for individual compounds in 50:50 water/acetonitrile. The relative abundance of free ligand and complex ions indicated the degree of complexation under different solution conditions (metal concentration, pH, ionic strength). Using tandem mass spectrometry, the structure and principal copper binding site for one of the tannins were also determined, providing unique information with regard to metal complexation by these polyfunctional ligands. The technique can be combined with high performance liquid chromatography for on-line separation of dissolved organic compounds. Results demonstrate the potential of this approach for characterizing the different classes of metal-complexing ligands found in natural waters. (C) 2000 Elsevier Science B.V. All rights reserved.},
	keywords = {AFFINITY-CHROMATOGRAPHY, CHROMATOGRAPHY, COMPLEXATION, copper, electrospray ionization, high performance liquid, iron, LIGANDS, MASS SPECTROMETRY, metal-ion complexes, NATURAL ORGANIC-LIGANDS, ORGANIC, PERFORMANCE, PROTEINS, REGIOSELECTIVE MONO-OXIDATION, SPECIATION, STOICHIOMETRY, tannins, TOXICITY, trace metals},
	isbn = {0003-2670},
	url = {<Go to ISI>://000086527500011},
	author = {Ross, A. R. S. and Ikonomou, M. G. and Orians, K. J.}
}
@article {4942,
	title = {Comparative toxicity of trivalent and pentavalent inorganic and methylated arsenicals in rat and human cells},
	journal = {Archives of Toxicology},
	volume = {74},
	number = {6},
	year = {2000},
	note = {ISI Document Delivery No.: 349ZATimes Cited: 358Cited Reference Count: 37},
	month = {Aug},
	pages = {289-299},
	type = {Article},
	abstract = {Biomethylation is considered a major detoxification pathway for inorganic arsenicals (iAs). According to the postulated metabolic scheme, the methylation of iAs yields methylated metabolites in which arsenic is present in both pentavalent and trivalent forms. Pentavalent mono- and dimethylated arsenicals are less acutely toxic than iAs. However, little is known about the toxicity of trivalent methylated species. In the work reported here the toxicities of iAs and trivalent and pentavalent methylated arsenicals were examined in cultured human cells derived from tissues that are considered a major site for iAs methylation (liver) or targets for carcinogenic effects associated with exposure to iAs (skin, urinary bladder, and lung). To characterize the role of methylation in the protection against toxicity of arsenicals, the capacities of cells to produce methylated metabolites were also examined. In addition to human cells, primary rat hepatocytes were used as methylating controls. Among the arsenicals examined, trivalent monomethylated species were the most cytotoxic in all cell types. Trivalent dimethylated arsenicals were at least as cytotoxic as trivalent iAs (arsenite) for most cell types. Pentavalent arsenicals were significantly less cytotoxic than their trivalent analogs. Among the cell types examined, primary rat hepatocytes exhibited the greatest methylation capacity for iAs followed by primary human hepatocytes, epidermal keratinocytes, and bronchial epithelial cells. Cells derived from human bladder did not methylate iAs. There was no apparent correlation between susceptibility of cells to arsenic toxicity and their capacity to methylate iAs. These results suggest that (1) trivalent methylated arsenicals, intermediary products of arsenic methylation, may significantly contribute to the adverse effects associated with exposure to iAs, and (2) high methylation capacity does not protect cells from the acute toxicity of trivalent arsenicals.},
	keywords = {ARSENATE, arsenic, ARSENITE, BINDING, bladder, cell culture, CELLULAR UPTAKE, DIMETHYLARSINIC ACID, dimethylarsinous acid, DRINKING-WATER, ENZYMATIC METHYLATION, GLUTATHIONE, HEPATOCYTES, HUMAN, IN-VITRO METHYLATION, LIVER, lung, METABOLISM, methylarsonic acid, methylarsonous acid, METHYLATION, RABBIT LIVER, SKIN, TOXICITY},
	isbn = {0340-5761},
	url = {<Go to ISI>://000089074500001},
	author = {Styblo, M. and Del Razo, L. M. and Vega, L. and Germolec, D. R. and LeCluyse, E. L. and Hamilton, G. A. and Reed, W. and Wang, C. and Cullen, W. R. and Thomas, D. J.}
}
@article {4711,
	title = {Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMA(III)) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes},
	journal = {Toxicology and Applied Pharmacology},
	volume = {158},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 216QCTimes Cited: 80Cited Reference Count: 33},
	month = {Jul},
	pages = {9-15},
	type = {Article},
	abstract = {Inorganic arsenite is methylated by some, but not all, animal species to dimethylarsinic acid (DMA), The monomethyl compound containing arsenic in an oxidation state of +3 has been proposed as an intermediate. Using highly purified arsenic methyltransferase from rabbit liver and the partially purified enzyme from Chang human liver hepatocytes, the activity of methylarsonic acid (MMA(V)) and methylarsonous acid (MMA(III)) as a substrate has been characterized by Michaelis-Menten kinetics. The rabbit liver enzyme has a greater affinity for MMA(III) (K-m = 0.92 x 10(-5) M) than MMA(V) (K-m = 7.0 x 10(-5) M) since the smaller the K, the greater the affinity. In addition, a dithiol, reduced lipoic acid or dithiothreitol, appears to be more active than GSH in satisfying the thiol requirement of the enzyme. Although investigators have been unable to detect the arsenic methyltransferase in surgically removed human liver, its presence in Chang human hepatocytes now has been established. The K-m for MMA(III), 3.04 x 10(-6), using MMAIII methyltransferase from Chang human hepatocytes was not greatly different from that of the rabbit liver enzyme, (C) 1999 Academic Press.},
	keywords = {BINDING, CYTOSOL, IN-VITRO, INVITRO, METABOLISM, TOXICITY, WATER, WEST-BENGAL},
	isbn = {0041-008X},
	url = {<Go to ISI>://000081452500002},
	author = {Zakharyan, R. A. and Ayala-Fierro, F. and Cullen, W. R. and Carter, D. M. and Aposhian, H. V.}
}
@article {4673,
	title = {Metabolism of arsenic in primary cultures of human and rat hepatocytes},
	journal = {Chemical Research in Toxicology},
	volume = {12},
	number = {7},
	year = {1999},
	note = {ISI Document Delivery No.: 219JCTimes Cited: 81Cited Reference Count: 26},
	month = {Jul},
	pages = {560-565},
	type = {Article},
	abstract = {The liver is considered a major site for methylation of inorganic arsenic (iAs). However, there is Little data on the capacity of human liver to methylate iAs. This work examined the metabolism of arsenite (iAs(III)), arsenate (iAs(v)), methylarsine oxide ((MAsO)-O-III), methylarsonic acid (MAsv), dimethylarsinous acid (DMAsIII), and dimethylarsinic acid (DMAsV) in primary cultures of normal human hepatocytes. Primary rat hepatocytes were used as methylating controls, iAs(III) and (MAsO)-O-III were metabolized more extensively than iAs(v) and MAsv by either cell type. Neither human nor rat hepatocytes metabolized DMAsIII or DMAsV. Methylation of iAs(III) by human hepatocytes yielded methylarsenic (MAs) and dimethylarsenic (DMAs) species; (MAsO)-O-III was converted to DMAs. The total methylation yield (MAs and DMAs) increased over the range of 0.1 to 4 mu M iAs(III). However, DMAs production was inhibited by iAs(III) in a concentration-dependent manner, and the DMAs/MAs ratio decreased. iAs(III) (10 and 20 mu M) inhibited both methylation reactions. Inhibition of DMAs synthesis resulted in accumulation of iAs and MAs in human hepatocytes, suggesting that dimethylation is required for iAs clearance from cells. Methylation capacities of human hepatocytes obtained from four donors ranged from 3.1 to 35.7 pmol of iAs(III) per 10(6) cells per hour and were substantially lower than the methylation capacity of rat hepatocytes (387 pmol of iAs(III) per 10(6) cells per hour). The maximal methylation rates for either rat or human hepatocytes were attained between 0.4 and 4 mu M iAs(III). In summary, (i) human hepatocytes methylate iAs, (ii) the capacities for iAs methylation vary among individuals and are saturable, and (iii) moderate concentrations of iAs inhibit DMAs synthesis, resulting in an accumulation of iAs and MAs in cells.},
	keywords = {ASSAY, ENZYMATIC METHYLATION, IN-VITRO, INGESTION, LIVER, PURIFICATION, TOXICITY, URINARY-EXCRETION},
	isbn = {0893-228X},
	url = {<Go to ISI>://000081603300003},
	author = {Styblo, M. and Del Razo, L. M. and LeCluyse, E. L. and Hamilton, G. A. and Wang, C. Q. and Cullen, W. R. and Thomas, D. J.}
}
@article {3552,
	title = {TISSUE DISTRIBUTION AND CLEARANCE OF TRITIUM-LABELED DIHYDROMICROCYSTIN-LR EPIMERS ADMINISTERED TO ATLANTIC SALMON VIA INTRAPERITONEAL INJECTION},
	journal = {Toxicon},
	volume = {33},
	number = {2},
	year = {1995},
	note = {ISI Document Delivery No.: QQ042Times Cited: 33Cited Reference Count: 20},
	month = {Feb},
	pages = {125-131},
	type = {Article},
	abstract = {The two epimers of [H-3]dihydromicrocystin-LR (spec. act. 32.6 mu Ci/mu mole) were synthesized by reduction of microcystin-LR, a cyclic heptapeptide hepatotoxin, with sodium boro[H-3]hydride. In Atlantic salmon, following an i.p. injection of the epimers (0.1 mg of toxin/100 g), the toxins were; after 2 hr, concentrated in the liver and pyloric caeca and intestine; after 5 and 22 hr, concentrated in the liver; and after 46 hr concentrated in the liver and kidney. The maximum concentration in the liver, 4.9 +/- 0.5\% of the injected dose, was observed at 5 hr. At 46 hr the incorporation of tritium in the liver was 2.4\%. The total whole body incorporation of tritium label at 2, 5, 22 and 46 hr was 67.9 +/- 7.3\%, 78.4 +/- 3.1\%, 54.5 +/- 6.6\% and 12.2\%, respectively. The per cent levels of incorporation are significantly lower and the clearance rates are significantly higher than those observed in mice. The ratio of relative concentrations of radiolabel observed in the livers and flesh indicates that extremely low levels of microcystin-LR would be present in the flesh of fish afflicted with {\textquoteright}netpen liver disease{\textquoteright}. Coupled with further evidence, it is suggested that the consumption of Atlantic salmon suffering from {\textquoteright}netpen liver disease{\textquoteright} does not represent a potential human health hazard.},
	keywords = {AERUGINOSA, DIARRHETIC SHELLFISH TOXINS, HEPATOTOXINS, IDENTIFICATION, MICROCYSTIN-LR, NETPEN LIVER-DISEASE, TOXICITY},
	isbn = {0041-0101},
	url = {<Go to ISI>://A1995QQ04200002},
	author = {Williams, D. E. and Kent, M. L. and Andersen, R. J. and Klix, H. and Holmes, C. F. B.}
}
@article {7102,
	title = {PHOTOSENSITIZING POTENCY OF STRUCTURAL ANALOGS OF BENZOPORPHYRIN DERIVATIVE (BPD) IN A MOUSE-TUMOR MODEL},
	journal = {British Journal of Cancer},
	volume = {63},
	number = {1},
	year = {1991},
	note = {ISI Document Delivery No.: ER853Times Cited: 85Cited Reference Count: 19},
	month = {Jan},
	pages = {87-93},
	type = {Article},
	abstract = {The in vivo characteristics of four analogues of benzoporphyrin derivative (BPD) have been investigated. Biodistribution data obtained in DBA/2J mice with BPD-MA (monoacid ring A analogue) which had been tritiated or internally labelled with C-14 showed that both labelled materials acted in an essentially identical manner during the period of study. Biodistribution and clearance studies showed that relative distribution in a variety of mouse tissues was similar for all BPD analogues. M1 tumour cells (rhabdomyosarcoma in DBA/2J mice) taken from tumours excised from animals treated 3 h earlier with BPD, and tested in vitro for photosensitivity provided evidence that significant levels of photosensitiser detected in tumour was both active and associated with tumour cells. The monoacid forms of BPD were found to be much more photodynamically active in this test that were the diacid analogues. The ability of the analogues to ablate tumours in mice by photodynamic therapy was also tested. Again, BPD-MA and BPD-MB proved to be measurably better than the diacid analogues. These findings are discussed in reference to structural and physical differences between the analogues.},
	keywords = {HEMATOPORPHYRIN, PHOTOFRIN-II, PHTHALOCYANINES, PLASMA-LIPOPROTEINS, porphyrins, TOXICITY},
	isbn = {0007-0920},
	url = {<Go to ISI>://A1991ER85300018},
	author = {Richter, A. M. and Waterfield, E. and Jain, A. K. and Allison, B. and Sternberg, E. D. and Dolphin, D. and Levy, J. G.}
}
