@article {2637,
	title = {Vanadium treatment of type 2 diabetes: A view to the future},
	journal = {Journal of Inorganic Biochemistry},
	volume = {103},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 429EUTimes Cited: 20Cited Reference Count: 41Thompson, Katherine H. Lichter, Jay LeBel, Carl Scaife, Michael C. McNeill, John H. Orvig, Chris6th International Vanadium SymposiumJUL 17-19, 2008Lisbon, PORTUGALSp. Iss. SI},
	month = {Apr},
	pages = {554-558},
	type = {Proceedings Paper},
	abstract = {3-Hydroxy-2-methyl-4-pryone and 2-ethyl 3-hydroxy-4-pyrone (maltol and ethyl maltol, respectively) have proven especially suitable a ligands for vanadyl tons, fit potential insulin enhancing agents for diabetes mellitus. Both bis(maltolato)oxovanadium(IV) (BMOV), and the ethylmaltol analog, bis(ethylmaltolato)oxovanadium(IV) (BEOV), have the desired intermediate stability for pro-drug use, and have undergone extensive pie-clinical testing for safety and efficacy. Pharmacokinetic evaluation indicates a pattern of biodistribution consistent with fairly rapid dissociation and uptake, binding to serum transferrin for systemic circulation and transport to tissues, with preferential uptake in bone. These bis-ligand oxovanadium(IV) (VOL2) compounds have a clear advantage over inorganic vanadyl sulfate in terms of bioavailability and pharmaceutical efficacy. BEOV has now completed Phase I and has advanced to Phase II clinical trials. In the Phase I trial, a ran-e of doses horn 10 mg, to 90 mg BEOV, given orally to non-diabetic volunteers, resulted in no adverse effects, all biochemical parameters remained within normal limits. In the Phase IIa trial, BEOV (AKP-020). 20 mg, daily for 28 clays, per os, in seven type 2 diabetic Subjects, was associated with reductions in fasting blood and glucose and \%HbA1c; improved responses to oral glucose tolerance testing, versus, the observed worsening of diabetic symptoms in the two placebo controls. (C) 2009 Elsevier Inc. All rights reserved.},
	keywords = {BIODISTRIBUTION, bis(ethylmaltolato)oxovanadium(IV), BIS(MALTOLATO)OXOVANADIUM(IV), CHEMISTRY, Diabetes mellitus, IN-VIVO, INSULIN SENSITIVITY, MALTOL, METAL-COMPLEXES, RATS, SERUM, SKELETAL-MUSCLE, SULFATE, VANADIUM},
	isbn = {0162-0134},
	url = {<Go to ISI>://000264904400011},
	author = {Thompson, K. H. and Lichter, J. and Lebel, C. and Scaife, M. C. and McNeill, J. H. and Orvig, Chris}
}
@article {4489,
	title = {Analysis of gamma-carboxyglutamic acid content of protein, urine, and plasma by capillary electrophoresis and laser-induced fluorescence},
	journal = {Analytical Chemistry},
	volume = {71},
	number = {8},
	year = {1999},
	note = {ISI Document Delivery No.: 186XUTimes Cited: 12Cited Reference Count: 32},
	month = {Apr},
	pages = {1633-1637},
	type = {Article},
	abstract = {When the properties of an analyte are known, the separation system can be designed to make the analyte of interest migrate at either a much faster ora much slower velocity compared to other molecules in the sample matrix. A simple and sensitive method to analyze the gamma-carboxyglutamic acid (Gla) content of protein, urine, and plasma was developed using capillary electrophoresis with laser-induced fluorescence detection (CE-IIF), The separation method is designed according to the specific properties of three amino acids of interest. The number of Gla residues from three vitamin K-dependent proteins were estimated by quantifying the amount of fluorescein thiocarbamyl derivative of Gla after alkaline hydrolysis and fluorescein isothiocyanate labeling. Human prothrombin, blood coagulation factor X, and bovine osteocalcin were calculated to have 10.0 +/- 0.7, 11.0 +/- 0.6, and 2.1 +/- 0.1 Gla residues. per mole of protein, respectively, which agreed well with amino acid sequencing data. The analysis of free Gla content in urine and plasma was also demonstrated by this method. It was demonstrated that submicrograms of protein can be characterized by CE-LIF.},
	keywords = {bone, CLINICAL-SIGNIFICANCE, GLUTAMIC-ACID, MARKERS, PROTHROMBIN, SERUM, VITAMIN-K},
	isbn = {0003-2700},
	url = {<Go to ISI>://000079756900025},
	author = {Britz-McKibbin, P. and Vo, H. C. and MacGillivray, R. T. A. and Chen, D. D. Y.}
}
@article {4486,
	title = {Clq binding to liposomes is surface charge dependent and is inhibited by peptides consisting of residues 14-26 of the human ClqA chain in a sequence independent manner},
	journal = {Biochimica Et Biophysica Acta-Biomembranes},
	volume = {1418},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 189EWTimes Cited: 20Cited Reference Count: 36},
	month = {Apr},
	pages = {19-30},
	type = {Article},
	abstract = {Complement activation by anionic liposomes proceeds by antibody-independent, C1q-initiated activation of the classical pathway. Purified C1q bound to anionic liposomes in an acidic lipid concentration-dependent manner. Saturation binding, but not the apparent association constant, was enhanced by increasing the cardiolipin content of the liposomes or decreasing either the pH or ionic strength of the reaction mixture. These observations indicate the involvement of electrostatic factors in the binding. A highly cationic region in the collagen-like domain of C1q comprised of residues 14-26 of the C1qA polypeptide chain was assessed for involvement in liposome binding. This region has previously been shown to mediate C1q binding to other immunoglobulin-independent activators of the classical pathway of complement. Peptides containing residues 14-26 of C1qA, denoted C1qA(14-26), inhibited C1q binding to and complement activation by anionic liposomes. The inhibitory capacity of these cationic peptides had no sequence or conformation specificity. Rather, the amount of positive charge on the peptides was the determining factor. When present in excess, peptides with five cationic residues inhibited C1q binding and complement activation; however, C1q peptides with only two cationic residues did not. In addition to the C1qA(14-26) region, other parts of C1q that contain cationic residues may also be involved in C1q binding to anionic liposomes. (C) 1999 Elsevier Science B.V. All rights reserved.},
	keywords = {1ST, ACTIVATES COMPLEMENT, C1Q A-CHAIN, CLASSICAL COMPLEMENT PATHWAY, CLEARANCE, Clq binding, COLLAGEN, COMPONENT, liposome clearance, liposome-mediated complement activation, PHAGOCYTOSIS, PROTEINS, SERUM, SYSTEM},
	isbn = {0005-2736},
	url = {<Go to ISI>://000079892300002},
	author = {Bradley, A. J. and Brooks, D. E. and Norris-Jones, R. and Devine, D. V.}
}
@article {4584,
	title = {Immunochemical extraction and detection of LSD in whole blood},
	journal = {Journal of Immunological Methods},
	volume = {224},
	number = {1-2},
	year = {1999},
	note = {ISI Document Delivery No.: 195AQTimes Cited: 10Cited Reference Count: 19},
	month = {Apr},
	pages = {11-18},
	type = {Article},
	abstract = {Polyclonal antibodies raised against the hallucinogenic drug, lysergic acid diethylamide (LSD), were used to detect and extract drug from whole blood samples. An indirect ELISA was used to detect as little as 1 pg of total drug in 25 mu l blood. The limit of detection of the immunoassay, calculated from the mean - 3 SD was 39 pg/ml. The analytical recovery of LSD (2.5-0.2 ng/ml) from whole blood was 102-113\%. Within-run CVs for LSD spiked in blood at 1.25, 0.16 and 0.04 ng/ml were 5.6, 3.1, and 8.9\%, respectively (n = 4). There was an overall decrease in precision when whole blood was used in place of urine, due to the increased complexity of the matrix. However, using this technique LSD was calibrated in blood in the sub-ng/ml region of forensic interest. Immunoaffinity extraction was used to isolate LSD from blood and urine samples. The affinity support was prepared by covalently attaching anti-LSD antibodies to Protein A-coated agarose beads. No pre-treatment of the sample was required other than the addition of neutral buffer. Sub-ng/ml concentrations of LSD were routinely extracted from blood and urine samples with greater than 80\% recovery of drug. This technique, which could be used to extract LSD from blood and urine samples prior to confirmatory drug analysis, could be completed in about 10 min. (C) 1999 Elsevier Science B.V. All rights reserved.},
	keywords = {BLOOD, CHROMATOGRAPHY-MASS-SPECTROMETRY, CONFIRMATION, ELISA, HUMAN URINE, immunoaffinity extraction, IMMUNOASSAY, LSD, LYSERGIC-ACID DIETHYLAMIDE, N-DEMETHYL-LSD, RADIOIMMUNOASSAY, SERUM},
	isbn = {0022-1759},
	url = {<Go to ISI>://000080227300002},
	author = {Kerrigan, S. and Brooks, D. E.}
}
@article {4306,
	title = {Indirect enzyme-linked immunosorbent assay for the quantitative estimation of lysergic acid diethylamide in urine},
	journal = {Clinical Chemistry},
	volume = {44},
	number = {5},
	year = {1998},
	note = {ISI Document Delivery No.: ZL795Times Cited: 5Cited Reference Count: 27},
	month = {May},
	pages = {985-990},
	type = {Article},
	abstract = {A new antibody to lysergic acid diethylamide (LSD) was used to develop a novel indirect ELISA for the quantification of drug in urine. Evaluation of the new assay with the commercially available LSD ELISA (STC Diagnostics) shows improved performance. The test requires 50 mu L of urine, which is used to measure concentrations of drug in the mu g/L to ng/L range. The Limit of detection was 8 ng/L compared with 85 ng/L in the commercial assay, and analytical recoveries were 98-106\%. Our test detected 0.1 mu g/L of LSD in urine with an intraassay CV of 2.4\% (n = 8) compared with 6.0\% for a 0.5 mu g/L sample in the commercial assay (n = 20). The upper and lower limits of quantification were estimated to be 7 mu g/L and 50 ng/L, respectively. Specificity was evaluated by measuring the extent of cross-reactivity with 24 related substances. Drug determination using the new assay offers both improved sensitivity and precision compared with existing methods, thus facilitating the preliminary quantitative estimation of LSD in urine at lower concentrations with a greater degree of certainty.},
	keywords = {AFFINITY, BODY-FLUIDS, ELISA, GAS-CHROMATOGRAPHY, METABOLITES, MONOCLONAL-ANTIBODIES, N-DEMETHYL-LSD, RADIOIMMUNOASSAY, SERUM, TANDEM MASS-SPECTROMETRY},
	isbn = {0009-9147},
	url = {<Go to ISI>://000073472300014},
	author = {Kerrigan, S. and Brooks, D. E.}
}
@article {4210,
	title = {Inhibition of liposome-induced complement activation by incorporated poly(ethylene glycol) lipids},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {357},
	number = {2},
	year = {1998},
	note = {ISI Document Delivery No.: 119UCTimes Cited: 65Cited Reference Count: 50},
	month = {Sep},
	pages = {185-194},
	type = {Article},
	abstract = {Complement activation causes opsonization of foreign particles leading to particle elimination from the blood. Complement-mediated opsonization of charged and large liposomes presents a fundamental problem in their use to deliver therapeutic agents in vivo. To prolong the circulation half-lives of such liposomes, complement activation must be curtailed. The aim of this study was to assess the ability of poly(ethylene glycol)-lipids (PEG-lipids) to inhibit the in vitro activation of the classical pathway of complement in human serum by anionic liposomes. Incorporation of cholesterol-PEG(600) (CH-PEG(600)), cholesterol-PEG(1000) (CH-PEG(1000)), or phosphatidylethanolamine-PEG(2000) (PE-PEG(2000)) resulted in dose-dependent inhibition of Clq binding and complement activation. The dose of PEG-lipid at which complement activation was blocked was inversely related to the PEG chain length. Complement activation was strongly inhibited when 15 mole\% of CH-PEG(600), 10 mole\% CH-PEG(1000), or 5 mole\% PE-PEG(2000), was incorporated into 100-nm anionic liposomes. PEG-lipid incorporation into larger liposomes (240 nm) was also successful in blocking C1q binding and complement activation. Radiolabeled cholesterol-PEG(similar to 1400) was prepared and used to determine both the percentage of CH-PEG incorporated into the liposomes and the percentage maintained in the liposomes in the presence of 50\% human serum at 37 degrees C for up to 24 h. (C) 1998 Academic Press.},
	keywords = {C1q, CHOLESTEROL, CLEARANCE, complement activation, HEPATIC-UPTAKE, INVIVO, LARGE UNILAMELLAR VESICLES, LIPOSOMES, POLY(ETHYLENE GLYCOL), POLYETHYLENE-GLYCOL, PROLONGED CIRCULATION TIME, SERUM, SIZE, SURFACE-CHARGE},
	isbn = {0003-9861},
	url = {<Go to ISI>://000075915200002},
	author = {Bradley, A. J. and Devine, D. V. and Ansell, S. M. and Janzen, J. and Brooks, D. E.}
}
@article {2953,
	title = {PHARMACOKINETICS AND DISTRIBUTION OF TRIS(MALTOLATO)ALUMINUM(III) INTO THE CENTRAL-NERVOUS-SYSTEM},
	journal = {Neurotoxicology},
	volume = {15},
	number = {2},
	year = {1994},
	note = {ISI Document Delivery No.: PB305Times Cited: 4Cited Reference Count: 37},
	month = {Sum},
	pages = {371-378},
	type = {Article},
	abstract = {The maltolate compound of aluminum (Al), tris(maltolato)aluminum(III), has been demonstrated to be quite toxic after central administration and in cell cultures. However, reports of peripheral Al-maltolate administration in vivo demonstrated un impressive neurological effects. We found no reports of Al-maltolate pharmacokinetics or its distribution into the central nervous system (CNS) after systemic administration. In the present study, we evaluated Al pharmacokinetics in serum and Al distribution into brain extracellular fluid (ECF) in rats following Al-maltolate administration. The pharmacokinetic studies revealed that systemic clearance, elimination half-life and mean residence time were 42 (+/- 5) ml/hr/kg, 2.2 (+/- 0.5) hr and 3.1 (+/- 0.7) hr [mean+/-SD), respectively. The steady state volume of distribution (V-ss) for Al-maltolate was 130 ml/kg. This V-ss suggests that Al-maltolate may exhibit limited distribution outside the vascular compartment, which is estimated to be approximate to 80 ml/kg in these rats. Previously, we used microdialysis (MD) probes to assess Al-citrate distribution into the CNS. MD was utilized in the present study to evaluate the CNS distribution of Al as a result of Al-maltolate administration. MD probes were implanted into the frontal cortex (FC) and jugular vein to sample Al from brain and blood ECF, respectively. Al was not measurable in FC MD probe dialysates after a 0.5 mmol/kg Al (as maltolate) bolus, but could be measured after steady state blood and brain ECF Al concentrations had been achieved. The Al brain/blood ra tio calculated from Al-maltolate steady state brain and blood MD samples was 0.04, significantly less than those calculated for other Al salts at equimolar Al doses. The present study suggests that unless it is administered centrally, Al-maltolate might render minimal neurological insult because of its minimal permeation into brain extracellular space. (C) 1994 Intox Press, Inc.},
	keywords = {ALUMINUM MALTOL, ALUMINUM NEUROTOXICITY, ALUMINUM PHARMACOKINETICS, ALUMINUM-MALTOLATE, BLOOD-BRAIN-BARRIER, COMPLEXES, DIALYSIS, ENCEPHALOPATHY, EQUILIBRIUM, gallium, INVIVO MICRODIALYSIS, MICRODIALYSIS, permeability, RABBITS, SERUM},
	isbn = {0161-813X},
	url = {<Go to ISI>://A1994PB30500014},
	author = {Allen, D. D. and Orvig, Chris and Yokel, R. A.}
}
@article {7352,
	title = {STABILIZATION OF THE STRUCTURE OF HORSE PLASMA VITAMIN-D BINDING-PROTEIN BY DISULFIDE BONDS},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: HG742Times Cited: 1Cited Reference Count: 27},
	month = {Jan},
	pages = {10-15},
	type = {Article},
	abstract = {Vitamin D binding protein (DBP) was isolated from horse plasma in a four-step procedure that involved Affi-Gel Blue affinity chromatography, gel filtration, hydroxylapatite chromatography, and anion exchange high-pressure liquid chromatography. The yield of DBP from 80 mL of plasma was 6-7 mg. Horse plasma DBP closely resembles other plasma DBPs, being a tryptophan-free protein of M(r) 53 000. It is able to bind to and block the polymerization of monomeric actin. The secondary structure of DBP was calculated from circular dichroism measurements to be 39\% alpha-helix, 42\% beta-sheet, and 19\% random coil. Circular dichroism and fluorescence studies revealed that the disulfide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation. The thermal stability of DBP can be used to advantage. Incorporation of a brief treatment at 70-degrees-C into the preparative scheme enables omission of one chromatographic step, without detectable alteration of the purified product.},
	keywords = {actin, circular dichroism, CIRCULAR-DICHROISM, COMPLEX, denaturation, DISULFIDE BONDS, FLUORESCENCE, GC-GLOBULIN, POLYMERIZATION, RAT, SERUM, thermal, TROPOMYOSIN, VITAMIN-D BINDING PROTEIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992HG74200002},
	author = {Robinson, R. C. and Burtnick, L. D.}
}
