@article {1176,
	title = {New insights into the interactions of serum proteins with bis(maltolato)oxovanadium(IV): Transport and biotransformation of insulin-enhancing vanadium pharmaceuticals},
	journal = {Journal of the American Chemical Society},
	volume = {127},
	number = {14},
	year = {2005},
	note = {ISI Document Delivery No.: 914LQTimes Cited: 39Cited Reference Count: 66},
	month = {Apr},
	pages = {5104-5115},
	type = {Article},
	abstract = {Significant new insights into the interactions of the potent insulin-enhancing compound bis(maltolato)oxovanadium(IV) (BMOV) with the serum proteins, apo-transferrin and albumin, are presented. Identical reaction products are observed by electron paramagnetic resonance (EPR) with either BMOV or vanadyl sulfate (VOSO4) in solutions of human serum apo-transferrin. Further detailed study rules out the presence of a ternary ligand-vanadyl-transferrin complex proposed previously. By contrast, differences in reaction products are observed for the interactions of BMOV and VOSO4 with human serum albumin (HSA), wherein adduct formation between albumin and BMOV is detected. In BMOV-albumin solutions, vanadyl ions are bound in a unique manner not observed in comparable solutions Of VOSO4 and albumin. Presentation of chelated vanadyl ions precludes binding at the numerous nonspecific sites and produces a unique EPR spectrum which is assigned to a BMOV-HSA adduct. The adduct species cannot be produced, however, from a solution Of VOSO4 and HSA titrated with maltol. Addition of maltol to a VOSO4-HSA solution instead results in formation of a different end product which has been assigned as a ternary complex, VO(ma)(HSA). Furthermore, analysis of solution equilibria using a model system of BMOV with 1-methylimidazole (formation constant log K = 4.5(1), by difference electronic absorption spectroscopy) lends support to an adduct binding mode (VO(ma)(2)-HSA) proposed herein for BMOV and HSA. This detailed report of an in vitro reactivity difference between VOSO4 and BMOV may have bearing on the form of active vanadium metabolites delivered to target tissues. Albumin binding of vanadium chelates is seen to have a potentially dramatic effect on pharmacokinetics, transport, and efficacy of these antidiabetic chelates.},
	keywords = {BINDING CONSTANTS, COMPLEXES, DEPENDENT DIABETES-MELLITUS, ELECTRON-PARAMAGNETIC RESONANCE, HUMAN SEROTRANSFERRIN, IN-VIVO, IRON REMOVAL, METALLOKINETIC ANALYSIS, MIMETIC AGENT, TRANSFERRIN},
	isbn = {0002-7863},
	url = {<Go to ISI>://000228229600036},
	author = {Liboiron, B. D. and Thompson, K. H. and Hanson, G. R. and Lam, E. and Aebischer, N. and Orvig, Chris}
}
@article {1011,
	title = {Comparison of anti-hyperglycemic effect amongst vanadium, molybdenum and other metal maltol complexes},
	journal = {Journal of Inorganic Biochemistry},
	volume = {98},
	number = {5},
	year = {2004},
	note = {ISI Document Delivery No.: 824HVTimes Cited: 37Cited Reference Count: 7411th International Conference on Biological Inorganic ChemistryJUL 19-23, 2003Cairns, AUSTRALIA},
	month = {May},
	pages = {683-690},
	type = {Proceedings Paper},
	abstract = {A wide variety of vanadium-containing complexes have been tested, both in vivo and in vitro, as possible therapeutic agents for the oral treatment of type 2 diabetes mellitus. None so far has surpassed bis(maltolato)oxovanadium(IV) (BMOV) for glucose- and lipid-lowering in an orally available formulation. Ligand choice is clearly an important factor in pharmacological efficacy of vanadium compounds as insulin enhancing agents. In this study, we kept the ligand and dose the same, varying instead the metal ion bound to the maltolato ligand in a series of binary complexes of neutral charge. A requirement for vanadyl ion as the metal ion of choice was apparent; no other metal ion tested served as a suitable substitute. Amongst [MoO2](2+), Co(II), Cu(II), Cr(III), and Zn(II), only [MoO2](2+) and Co(II) showed any hypoglycemic activity at the ED50 dose for bis(maltolato)oxovanadium(IV), 0.6 mmol kg(-1) by oral gavage in streptozotocin (STZ)-diabetic rats within 72 It of administration of compound. (C) 2004 Elsevier Inc. All rights reserved.},
	keywords = {ABSORPTION, CHROMIUM, cobalt, COORDINATION MODE, copper, DEPENDENT DIABETES-MELLITUS, GLUCOSE-METABOLISM, IN-VIVO, INSULIN, LIPID-METABOLISM, MOLYBDENUM, RATS, VANADIUM, zinc, ZINC SUPPLEMENTATION},
	isbn = {0162-0134},
	url = {<Go to ISI>://000221678300004},
	author = {Thompson, K. H. and Chiles, J. and Yuen, V. G. and Tse, J. and McNeill, J. H. and Orvig, Chris}
}
@article {4957,
	title = {Design of vanadium compounds as insulin enhancing agents},
	journal = {Journal of the Chemical Society-Dalton Transactions},
	number = {17},
	year = {2000},
	note = {ISI Document Delivery No.: 348MDTimes Cited: 77Cited Reference Count: 123},
	pages = {2885-2892},
	type = {Review},
	abstract = {Vanadium compounds, in vitro, stimulate glucose uptake and inhibit lipid breakdown, in a manner remarkably reminiscent of insulin{\textquoteright}s effects. In vivo, vanadium enhances insulin{\textquoteright}s plasma glucose and lipid-lowering properties, leading to normalization of diabetic symptoms in the presence of only minimal endogenous insulin. The coordination chemistry of vanadium has great versatility for adjustment of pharmacological characteristics. Vanadium compounds are generally also very redox active, which is both advantageous and detrimental for optimizing biochemical function. In this perspective, we review and comment on how these properties have been revealed, what questions have arisen along the way, and where future investigations may be headed. While this is not a comprehensive overview of all available compounds touted as {\textquoteright}insulin enhancing agents{\textquoteright}, it will focus on those which are distinctive in some way, or which are representative of the larger library of vanadium compounds, including all currently known relevant oxidation states of vanadium.},
	keywords = {AGENT, BIOLOGICAL-SYSTEMS, DEPENDENT DIABETES-MELLITUS, ECHO ENVELOPE, GLUCOSE-METABOLISM, IN-VIVO, MIMETIC, MODULATION, PEROXOVANADIUM COMPOUNDS, SKELETAL-MUSCLE, STREPTOZOTOCIN-TREATED RATS, TYROSINE PHOSPHORYLATION},
	isbn = {1470-479X},
	url = {<Go to ISI>://000088987800001},
	author = {Thompson, K. H. and Orvig, Chris}
}
