Decavanadate (V10O286-) and oxovanadates: Oxometalates with many biological activities

Aureliano, Manuel; Crans, Debbie C.

doi:10.1016/j.jinorgbio.2008.11.010

Cited by 232 publications

(262 citation statements)

References 132 publications

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“…15 Milestones in the history of vanadium biochemistry are the studies on the redox profile of vanadium, the role of vanadium in bromoperoxidases, the vanadium binding proteins in ascidians and, more recently, decavanadate interactions with lipidic structures, muscle proteins and the in vivo effects induced by the decameric vanadate species. 15, 17 Currently, decavanadate, a vanadate oligomer, is well known to exhibit many biological functions. A review of biological activities of decavanadate is given in a recent paper.…”

Section: Introductionmentioning

confidence: 99%

“…A review of biological activities of decavanadate is given in a recent paper. 17 One of these studies points to mitochondria as a potential target for decameric toxicity, and also associates the effects of decavanadate with bioenergetics processes. 15,17 Therefore, otherwise neglected, decavanadate has travelled a journey in a search of a role, but along the way it has been found to be a very useful tool in the understanding of protein structure and function, biochemical mechanisms and a…”

Section: Introductionmentioning

confidence: 99%

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Decavanadate: a journey in a search of a role

Aureliano

2009

Dalton Trans.

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Currently, efforts have been directed towards using decavanadate as a tool for the understanding of several biochemical processes such as muscle contraction, calcium homeostasis, in vivo changes of oxidative stress markers, mitochondrial oxygen consumption, mitochondrial membrane depolarization, actin polymerization and glucose uptake, among others. In addition, studies have been conducted in order to make vanadium available and safe for clinical use, for instance with decavanadate compounds that present interesting pharmacological properties, eventually useful for the treatment of diabetes. Here, recent contributions of decavanadate to the effects of vanadium in biological systems, not only in vitro, but also in vivo, are analysed

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Decavanadate: a journey in a search of a role

Aureliano

2009

Dalton Trans.

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“…1 This oxovanadate species, also referred to as decavanadate (V 10 ), is known to affect lipidic structures, protein function and also several biochemical processes. 2 One of these processes is the formation of F-actin, the major component of muscle thin filaments, is shown to be inhibited by decavanadate with an IC 50 of 17 mM, whereas no effects were detected for monomeric vanadate species.…”

Section: Introductionmentioning

confidence: 99%

“…1,4, 8 However, in the last 10 years the number of studies involving decavanadate has increased gradually. 1 In fact, V 10 has proved itself to be a very useful tool in the comprehension of protein structure and function, biochemical mechanisms and biological processes, 18-22 being now considered the major protein-bound vanadate species. 1, 22 Moreover, it is known that decavanadate interacts with enzymes at the polyphosphate, nucleotide and inositol-3-phosphate binding sites in the substrate domain or in an allosteric site, in a complex manner.…”

Section: Introductionmentioning

confidence: 99%

Decavanadate interactions with actin: cysteine oxidation and vanadyl formation

et al. 2009

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Incubation of actin with decavanadate induces cysteine oxidation and oxidovanadium(IV) formation. The studies were performed combining kinetic with spectroscopic (NMR and EPR) methodologies. Although decavanadate is converted to labile oxovanadates, the rate of deoligomerization can be very slow (half-life time of 5.4 h, at 25 • C, with a first order kinetics), which effectively allows decavanadate to exist for some time under experimental conditions. It was observed that decavanadate inhibits F-actin-stimulated myosin ATPase activity with an IC 50 of 0.8 mM V 10 species, whereas 50 mM of vanadate or oxidovanadium(IV) only inhibits enzyme activity up to 25%. Moreover, from these three vanadium forms, only decavanadate induces the oxidation of the so called "fast" cysteines (or exposed cysteine, Cys-374) when the enzyme is in the polymerized and active form, F-actin, with an IC 50 of 1 mM V 10 species. Decavanadate exposition to F-and G-actin (monomeric form) promotes vanadate reduction since a typical EPR oxidovanadium(IV) spectrum was observed. Upon observation that V 10 reduces to oxidovanadium(IV), it is proposed that this cation interacts with G-actin (K d of 7.48 ± 1.11 mM), and with F-actin (K d = 43.05 ± 5.34 mM) with 1:1 and 4:1 stoichiometries, respectively, as observed by EPR upon protein titration with oxidovanadium(IV). The interaction of oxidovanadium(IV) with the protein may occur close to the ATP binding site of actin, eventually with lysine-336 and 3 water molecules.

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“…49 Furthermore, decavanadate, 50 and compounds containing decavanadate 51 have been reported to lower glycemic levels, 50,51 and to normalize plasma lipid profiles. 51 Due to the ability of V 10 to interfere with several biological processes, such as calcium homeostasis, muscle contraction and oxidative stress, 8,54,55 not only in vitro but also in vivo, 52,53 decavanadate has recently been associated with the treatment of Leishmaniosis. 56 In this and probably in many other cases the mechanism of action of decavanadate progresses via the inhibition of the E1-E2 Ca 2+ -ATPases.…”

Section: Ca 2+ -Atpase Inhibitorsmentioning

confidence: 99%

Ion pumps as biological targets for decavanadate

2013

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The putative applications of poly-, oligo-and mono-oxometalates in biochemistry, biology, pharmacology and medicine are rapidly attracting interest. In particular, these compounds may act as potent ion pump inhibitors and have the potential to play a role in the treatment of e.g. ulcers, cancer and ischemic heart disease. However, the mechanism of action is not completely understood in most cases, and even remains largely unknown in other cases. In the present review we discuss the most recent insights into the interaction between mono-and polyoxometalate ions with ion pumps, with particular focus on the interaction of decavanadate with Ca 2+ -ATPase. We also compare the proposed mode of action with those of established ion pump inhibitors which are currently in therapeutic use. Of the 18 classes of compounds which are known to act as ion pump inhibitors, the complete mechanism of inhibition is only known for a handful. It has, however, been established that most ion pump inhibitors bind mainly to the E2 ion pump conformation within the membrane domain from the extracellular side and block the cation release. Polyoxometalates such as decavanadate, in contrast, interact with Ca 2+ -ATPase near the nucleotide binding site domain or at a pocket involving several cytoplasmic domains, and therefore need to cross through the membrane bilayer.In contrast to monomeric vanadate, which only binds to the E2 conformation, decavanadate binds to all protein conformations, i.e. E1, E1P, E2 and E2P. Moreover, the specific interaction of decavanadate with sarcoplasmic reticulum Ca 2+ -ATPase has been shown to be non-competitive with respect to ATP and induces protein cysteine oxidation with concomitant vanadium reduction which might explain the high inhibitory capacity of V 10 (IC 50 = 15 μM) which is quite similar to the majority of the established therapeutic drugs.

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Decavanadate (V10O286-) and oxovanadates: Oxometalates with many biological activities

Cited by 232 publications

References 132 publications

Decavanadate: a journey in a search of a role

Decavanadate: a journey in a search of a role

Decavanadate interactions with actin: cysteine oxidation and vanadyl formation

Ion pumps as biological targets for decavanadate

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