Decavanadate Binding to a High Affinity Site near the Myosin Catalytic Centre Inhibits F-Actin-Stimulated Myosin ATPase Activity

Tiago, Teresa; Aureliano, Manuel; Gutiérrez‐Merino, Carlos

doi:10.1021/bi049910+

Cited by 48 publications

(92 citation statements)

References 56 publications

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“…Vanadium toxicity studies often disregard the formation of different vanadate oligomers known to have different biochemical effects and to interact with high affinity with many proteins such as, for example, myosin [5]. Few animal studies involving vanadium consider the contribution of different oligomeric vanadate species to vanadium toxicity.…”

Section: Resultsmentioning

confidence: 99%

“…As decavanadate is eventually less permeant through the anionic channel than the other vanadate oligomers and likely to be bound with high affinity to proteins, therefore preventing its disintegration to vanadate oligomers and reduction to vanadyl, we suggest that the accumulation of vanadium in liver after decavanadate administration is a consequence of a higher level of exposure of liver to total vanadium. It is known that decavanadate binds with high affinity with proteins [4,5,8]. Moreover, it was demonstrated that, in certain experimental conditions (but at physiological pH), the half-life of 100 lM decameric vanadate species, as ascertained by UV/vis, increases from 5 to 15 h, in the presence of the calcium pump from sarcoplasmic reticulum (Aureliano and Gândara, in press).…”

Section: Resultsmentioning

confidence: 99%

“…Besides monomeric vanadate species, other vanadate oligomers can occur in vanadate solutions, and such oligomers are known to promote different effects in enzymes activities, not only in vitro [4,5] but also in vivo [6,7]. Among vanadate oligomers, decameric vanadate, which may occur upon medium acidification, was considered by Stankiewicz et al [4] as the vanadate oligomer with more biochemical relevance.…”

Section: Introductionmentioning

confidence: 99%

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Vanadate oligomers: In vivo effects in hepatic vanadium accumulation and stress markers

Gândara

Soares

Martins

et al. 2005

Journal of Inorganic Biochemistry

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The formation of vanadate oligomeric species is often disregarded in studies on vanadate effects in biological systems, particularly in vivo, even though they may interact with high affinity with many proteins. We report the effects in fish hepatic tissue of an acute intravenous exposure (12, 24 h and 7 days) to two vanadium(V) solutions, metavanadate and decavanadate, containing different vanadate oligomers administered at sub-lethal concentration (5 mM; 1 mg/kg). Decavanadate solution promotes a 5-fold increase (0.135 ± 0.053 lg V À1 dry tissues) in the vanadium content of the mitochondrial fraction 7 days after exposition, whereas no effects were observed after metavanadate solution administration. Reduced glutathione (GSH) levels did not change and the overall reactive oxygen species (ROS) production was decreased by 30% 24 h after decavanadate administration, while for metavanadate, GSH levels increased 35%, the overall ROS production was depressed by 40% and mitochondrial superoxide anion production decreased 45%. Decavanadate intoxication did not induce changes in the rate of lipid peroxidation till 12 h, but later increased 80%, which is similar to the increase observed for metavanadate after 24 h. Decameric vanadate administration clearly induces different effects than the other vanadate oligomeric species, pointing out the importance of taking into account the different vanadate oligomers in the evaluation of vanadium(V) effects in biological systems.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Vanadate oligomers: In vivo effects in hepatic vanadium accumulation and stress markers

Gândara

Soares

Martins

et al. 2005

Journal of Inorganic Biochemistry

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“…The stimulation of myosin S1 Mg 2+ -ATPase activity by F-actin was measured spectrophotometrically at 340 nm using the coupled enzyme pyruvate kinase/lactate dehydrogenase (0.42 mM phosphoenolpyruvate, 0.375 mM NADH, 18 U of lactate dehydrogenase, and 18 U of pyruvate kinase), as in Tiago et al 9 …”

Section: Measurements Of F-actin Stimulated S1-mg 2+ -Atpase Activitymentioning

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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“…Thereafter, vanadium has a variety of physiological effects acting either as a phosphate analogue in the monomeric form ðH 2 VO À 4 Þ or through oligomeric vanadate species. Thus, vanadium showed to be a powerful biochemical tool to gain a deeper knowledge in several biochemical mechanisms such as the regulation of muscle contraction and the modulation of the F-actin stimulated myosin ATPase activity and its relevance to actin-myosin interactions [6,7].…”

Section: Introductionmentioning

confidence: 99%

Decavanadate interactions with actin: Inhibition of G-actin polymerization and stabilization of decameric vanadate

Ramos

Manuel

Tiago

et al. 2006

Journal of Inorganic Biochemistry

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101

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Decameric vanadate species (V10) inhibit the rate and the extent of G-actin polymerization with an IC50 of 68 ± 22 lM and 17 ± 2 lM, respectively, whilst they induce F-actin depolymerization at a lower extent. On contrary, no effect on actin polymerization and depolymerization was detected for 2 mM concentration of ''metavanadate'' solution that contains ortho and metavanadate species, as observed by combining kinetic with 51 V NMR spectroscopy studies. Although at 25°C, decameric vanadate (10 lM) is unstable in the assay medium, and decomposes following a first-order kinetic, in the presence of G-actin (up to 8 lM), the half-life increases 5-fold (from 5 to 27 h). However, the addition of ATP (0.2 mM) in the medium not only prevents the inhibition of G-actin polymerization by V10 but it also decreases the half-life of decomposition of decameric vanadate species from 27 to 10 h. Decameric vanadate is also stabilized by the sarcoplasmic reticulum vesicles, which raise the half-life time from 5 to 18 h whereas no effects were observed in the presence of phosphatidylcholine liposomes, myosin or G-actin alone. It is proposed that the ''decavanadate'' interaction with G-actin, favored by the G-actin polymerization, stabilizes decameric vanadate species and induces inhibition of G-actin polymerization. Decameric vanadate stabilization by cytoskeletal and transmembrane proteins can account, at least in part, for decavanadate toxicity reported in the evaluation of vanadium (V) effects in biological systems.

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Decavanadate Binding to a High Affinity Site near the Myosin Catalytic Centre Inhibits F-Actin-Stimulated Myosin ATPase Activity

Cited by 48 publications

References 56 publications

Vanadate oligomers: In vivo effects in hepatic vanadium accumulation and stress markers

Vanadate oligomers: In vivo effects in hepatic vanadium accumulation and stress markers

Decavanadate interactions with actin: cysteine oxidation and vanadyl formation

Decavanadate interactions with actin: Inhibition of G-actin polymerization and stabilization of decameric vanadate

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