Fifteen years of dancing with vanadium

Crans, Debbie C.

doi:10.1351/pac200577091497

Cited by 89 publications

(82 citation statements)

References 118 publications

(199 reference statements)

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“…In particular, their potential insulin mimetic capacity has been extensively investigated [10][11][12][13][14][15][16]. It has been shown that VCs can be used to mitigate insufficient insulin response in DM thus presenting insulin-mimetic properties in vitro and [17][18][19][20] in vivo [21][22][23][24], and two of them were tested in clinical trials [25].…”

Section: Introductionmentioning

confidence: 99%

Therapeutic properties of VO(dmpp)2 as assessed by in vitro and in vivo studies in type 2 diabetic GK rats

Domingues

Pelletier

Östenson

et al. 2014

Journal of Inorganic Biochemistry

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The bis(1,2-dimethyl-3-hydroxy-4-pyridinonato)oxidovanadium(IV), VO(dmpp) 2 , has shown anti-diabetic effects by in vitro studies in Wistar (W) rat adipocytes and in vivo in obese Zucker rats. The aim of this work is to confirm the therapeutic properties of VO(dmpp) 2 in non-obese type 2 diabetic Goto-Kakizaki (GK) rats. An in vivo study was carried out, treating W and GK rats during 21 days with a daily dose of VO(dmpp) 2 (44 μmol/kg). It was shown that VO(dmpp) 2 doesn't affect the normal increase of body weight of both W and GK rats, after 8 days of treatment ameliorates glycemia in GK rats (8.4 ± 0.3 vs 10.1 ± 0.2 mM in GK control, P b 0.001) but doesn't interfere with glucose levels in W rats and, after 21 days of treatment, improves the glucose intolerant profile of GK rats (13.1 ± 0.5 vs 20.6 ± 0.7 mM/min in GK control, P b 0.001), despite no increase of plasma insulin levels during glucose tolerance test. Additionally, it was demonstrated that VO(dmpp) 2 significantly enhances [3-3 H]-glucose uptake by W and GK rat adipocytes (non-toxic concentration of 100 μM: respectively 193 ± 20 and 254 ± 21%, P b 0.001, relative to the basal value) showing an efficacy similar to insulin 1.72 nM and better than the same concentration of BMOV (P b 0.01). Western blotting revealed that in W and GK rats VO(dmpp) 2 significantly promotes IRS2 (P b 0.05) and p-AKT expression (P b 0.001 and P b 0.05, respectively, relative to the respective controls) and in GK animals reduces the increase of PTP1β expression (P b 0.001, relative to GK control).

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Section: Introductionmentioning

confidence: 99%

Therapeutic properties of VO(dmpp)2 as assessed by in vitro and in vivo studies in type 2 diabetic GK rats

Domingues

Pelletier

Östenson

et al. 2014

Journal of Inorganic Biochemistry

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“…5,6 However, despite a number of studies pointing towards the biological importance of vanadate and its polyoxo forms, the molecular basis of this activity remains largely unexplored, as these studies are often hindered by the complex solution chemistry of vanadate and the existence of equilibria with different polyoxoanions at physiological pH. 7,8 While it has been mainly assumed that the mode of action of oxovanadates mostly depends on their structural features such as the charge and the size of the species, 9 their reactivity towards biologically relevant substrates has been very scarcely explored. Recent studies on the biological relevance of polyoxometalates revealed the unprecedented hydrolytic activity of oxovanadates towards several important classes of compounds such as phosphodiesters, monophosphoesters 10,11 and carboxylic esters.…”

Section: Introductionmentioning

confidence: 99%

Unraveling the Mechanisms of Carboxyl Ester Bond Hydrolysis Catalyzed by a Vanadate Anion

2012

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The mechanism of the p-nitrophenyl acetate (pNPA) hydrolysis promoted by vanadate ions was investigated utilizing both density functional and ab initio methods. In accordance with experiments, suggesting pure hydrolytic ester bond cleavage involving a nucleophilic addition in the rate-limiting transition state, four possible B AC 2 (acyl-oxygen bond cleavage) mode reaction pathways were modeled. Moreover, two alternative reaction modes were also considered. Geometry optimizations were carried out using B3LYP, BP86 and MPWB1K functionals, conjugated with 6-31++G(d,p) basis set and Stuttgart ECP for vanadium atom.

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“…6,15,16 However, various approaches to address this problem have provided some further insight as to the biological activity of these compounds. [5][6][7]16,20 Information on how effectively specific compounds inhibit isolated enzymes is important for consideration of their mode of actions in cells and animals. 6 A range of studies of a few vanadium compounds on isolated enzyme systems have been reported where the species exerting the effects can be more rigorously tracked.…”

Section: Introductionmentioning

confidence: 99%

Sarcoplasmic Reticulum Calcium ATPase Is Inhibited by Organic Vanadium Coordination Compounds: Pyridine-2,6-dicarboxylatodioxovanadium(V), BMOV, and an Amavadine Analogue

et al. 2008

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The general affinity of the sarcoplasmic reticulum (SR) Ca 2+ -ATPase was examined for three different classes of vanadium coordination complexes including a vanadium(V) compound, pyridine-2,6-dicarboxylatodioxovanadium(V) (PDC-V(V)), and two vanadium(IV) compounds, bis(maltolato)oxovanadium(IV) (BMOV), and an analogue of amavadine, bis(N-hydroxylamidoiminodiacetato)vanadium(IV) (HAIDA-V(IV)). The ability of vanadate to act either as a phosphate analogue or as a transition-state analogue with enzymes' catalysis phosphoryl group transfer suggests that vanadium coordination compounds may reveal mechanistic preferences in these classes of enzymes. Two of these compounds investigated, PDC-V(V) and BMOV, were hydrolytically and oxidatively reactive at neutral pH, and one, HAIDA-V(IV), does not hydrolyze, oxidize, or otherwise decompose to a measurable extent during the enzyme assay. The SR Ca 2+ -ATPase was inhibited by all three of these complexes. The relative order of inhibition was PDC-V(V) > BMOV > vanadate > HAIDA-V(IV), and the IC 50 values were 25, 40, 80, and 325 µM, respectively. Because the observed inhibition is more potent for PDC-V(V) and BMOV than that of oxovanadates, the inhibition cannot be explained by oxovanadate formation during enzyme assays. Furthermore, the hydrolytically and redox stable amavadine analogue HAIDA-V(IV) inhibited the Ca 2+ -ATPase less than oxovanadates. To gauge the importance of the lipid environment, studies of oxidized BMOV in microemulsions were performed and showed that this system remained in the aqueous pool even though PDC-V(V) is able to penetrate lipid interfaces. These findings suggest that the hydrolytic properties of these complexes may be important in the inhibition of the calcium pump. Our results show that two simple coordination complexes with known insulin enhancing effects can invoke a response in calcium homeostasis and the regulation of muscle contraction through the SR Ca 2+ -ATPase.

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Fifteen years of dancing with vanadium

Cited by 89 publications

References 118 publications

Therapeutic properties of VO(dmpp)2 as assessed by in vitro and in vivo studies in type 2 diabetic GK rats

Therapeutic properties of VO(dmpp)2 as assessed by in vitro and in vivo studies in type 2 diabetic GK rats

Unraveling the Mechanisms of Carboxyl Ester Bond Hydrolysis Catalyzed by a Vanadate Anion

Sarcoplasmic Reticulum Calcium ATPase Is Inhibited by Organic Vanadium Coordination Compounds: Pyridine-2,6-dicarboxylatodioxovanadium(V), BMOV, and an Amavadine Analogue

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