Biomedical subjects

M Aureliano

Publications and source records attributed to M Aureliano.

11 recordsLinked to original sources

PubMed2006

Vanadium distribution, lipid peroxidation and oxidative stress markers upon decavanadate in vivo administration.

The contribution of decameric vanadate species to vanadate toxic effects in cardiac muscle was studied following an intravenous administration of a decavanadate solution (1mM total vanadium) in Sparus aurata. Although decameric vanadate is unstable in the assay medium, it decomposes with a half-life time of 16 allowing studying its effects not only in vitro but also in vivo. After 1, 6 and 12h upon decavanadate administration the increase of vanadium in blood plasma, red blood cells and in cardiac mitochondria and cytosol is not affected in comparison to the administration of a metavanadate solution containing labile oxovanadates. Cardiac tissue lipid peroxidation increases up to 20%, 1, 6 and 12h after metavanadate administration, whilst for decavanadate no effects were observed except 1h after treatment (+20%). Metavanadate administration clearly differs from decavanadate by enhancing, 12h after exposure, mitochondrial superoxide dismutase (SOD) activity (+115%) and not affecting catalase (CAT) activity whereas decavanadate increases SOD activity by 20% and decreases (-55%) mitochondrial CAT activity. At early times of exposure, 1 and 6h, the only effect observed upon decavanadate administration was the increase by 20% of SOD activity. In conclusion, decavanadate has a different response pattern of lipid peroxidation and oxidative stress markers, in spite of the same vanadium distribution in cardiac cells observed after decavanadate and metavanadate administration. It is suggested that once formed decameric vanadate species has a different reactivity than vanadate, thus, pointing out that the differential contribution of vanadium oligomers should be taken into account to rationalize in vivo vanadate toxicity.

Animals↗

PubMed2005

Vanadium distribution following decavanadate administration.

An acute exposure of two vanadate solutions-metavanadate and decavanadate-containing different vanadate oligomers, induces different patterns of subcellular vanadium distribution in blood plasma, red blood cells (RBC), and cardiac muscle subcellular fractions of the fish Sparus aurata (gilthead seabream). The highest amount of vanadium was found in blood plasma 1 h after (5 mM) intravenous vanadate administration (295 +/- 64 and 383 +/- 104 microg V/g dry tissue, for metavanadate and decavanadate solutions, respectively), being 80-fold higher than in RBC. After 12 h of administration, the amount of vanadium in plasma, as well as in cardiac cytosol, decreased about 50%, for both vanadate solutions. During the period between 1 and 12 h, the ratio of vanadium in plasma/vanadium in RBC increased from 27 to 128 for metavanadate, whereas it remains constant (77) for decavanadate. Both vanadium solutions were primarily accumulated in the mitochondrial fraction (138 +/- 0 and 195 +/- 34 ng V/g dry tissue for metavanadate and decavanadate solutions, respectively, after 12 h exposure), rather than in cytosol. The amount of vanadium in cardiac mitochondria was twofold higher than in cytosol, earlier for metavanadate (6 h) than for decavanadate (12 h). It is concluded that, in fish cardiac muscle, the vanadium distribution is dependent on the administration of decameric vanadate, with vanadium being mainly distributed in plasma, before being accumulated into the mitochondrial fraction.

Animals↗

PubMed2005

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

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 microg V(-1) 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.

Animals↗

PubMed2003

Cadmium and vanadate oligomers effects on methaemoglobin reductase activity from Lusitanian toadfish: in vivo and in vitro studies.

Cadmium and two vanadate solutions as 'metavanadate' (containing ortho and metavanadate species) and 'decavanadate' (containing decameric species) (5 mM) were injected intraperitoneously in Halobatrachus didactylus (Lusitanian toadfish), in order to evaluate the effects of cadmium and oligomeric vanadate species on methaemoglobin reductase activity from fish red blood cells. Following short-term exposure (1 and 7 days), different changes were observed on enzyme activity. After 7 days of exposure, 'metavanadate' increased methaemoglobin reductase activity by 67% (P < 0.05), whereas, minor effects were observed on enzymatic activity upon cadmium and 'decavanadate' administration. However, in vitro studies indicate that decameric vanadate, in concentrations as low as 50 microM, besides strongly inhibiting methaemoglobin reductase activity, promotes haemoglobin oxidation to methaemoglobin. Although decameric vanadate species showed to be unstable in the different media used in this work, the rate of decameric vanadate deoligomerization is in general slow enough, making it possible to study its effects. It is concluded that the increase in H. didactylus methaemoglobin reductase activity is more pronounced upon exposition to 'metavanadate' than to cadmium and decameric species. Moreover, only decameric vanadate species promoted haemoglobin oxidation, suggesting that vanadate speciation is important to evaluate in vivo and in vitro effects on methaemoglobin reductase activity.

Animals↗

PubMed2003

Acute effects of vanadate oligomers on heart, kidney, and liver histology in the Lusitanian toadfish (Halobatrachus didactylus).

The contribution of vanadate oligomers to the acute histological effects of vanadium was analyzed in the heart, kidney, and liver of Halobatrachus didactylus (Schneider, 1801). A sublethal vanadium dose (5 mM, 1 mL/kg) in the form of metavanadate (containing ortho and metameric species) or in the form of decavanadate (containing only decameric species) was intraperitoneally administered by injection, and specimens of H. didactylus were sacrificed at one and seven days postinjection. Sections of heart ventricle and renal and hepatic tissue were stained with hematoxylin-eosin and examined by light microscopy to identify vanadium-induced tissue injury. In addition, PicroSirius-stained ventricular sections were analyzed by bipolarized light microscopy to determine the fraction of myocardium occupied by the ventricular wall structural elements (collagen I, collagen III, and cardiac muscle). Both vanadate solutions produced similar effects in the renal tissue. Morphological alterations included damaged renal tubules showing disorganized epithelial cells in different states of necrosis. Reabsorbed renal tubules and hyperchromatic interstitial tissue were also observed. The hepatic tissue presented hyperchromatic and hypertrophied nuclei, along with necrotic and hypertrophied hepatocytes, and more severe changes were observed in the liver with exposure to decavanadate. Vanadate oligomers promoted evident tissue lesions in the kidney and liver, but not in the cardiac tissue. However, cardiac tissue structural changes were produced. For example, decavanadate induced a hypertrophy of the ventricle due to a decrease in the percentage of myocardium occupied by collagen fibers. In general, decavanadate was shown to be more toxic than metavanadate.

Animals↗

PubMed2002

Oxidative stress in toadfish (Halobactrachus didactylus) cardiac muscle. Acute exposure to vanadate oligomers.

Vanadate solutions as "metavanadate" (containing ortho and metavanadate species) and "decavanadate" (containing mainly decameric species) (5 mM; 1 mg/kg) were injected intraperitoneously in Halobatrachus didactylus (toadfish), in order to evaluate the contribution of decameric vanadate species to vanadium (V) intoxication on the cardiac tissue. Following short-term exposure (1 and 7 days), different changes on antioxidant enzyme activities-superoxide dismutase (SOD), catalase (CAT), selenium-glutathione peroxidase (Se-GPx), total glutathione peroxidase (GPx), lipid peroxidation and subcellular vanadium distribution were observed in mitochondrial and cytosolic fractions of heart ventricle toadfish. After 1 day of vanadium intoxication, SOD, CAT and Se-GPx activities were decreased up to 25%, by both vanadate solutions, except mitochondrial CAT activity that increased (+23%) upon decavanadate administration. After 7 days of exposure, decavanadate versus metavanadate solutions promoted different effects mainly on cytosolic CAT activity (-56% versus -5%), mitochondrial CAT activity (-10% versus +10%) and total GPx activity (+1% versus -35%), whereas lipid peroxidation products were significantly increased (+82%) upon 500 microM decavanadate intoxication. Accumulation of vanadium in total (0.137+/-0.011 microg/g) and mitochondrial (0.022+/-0.001 microg/g) fractions was observed upon 7 days of metavanadate exposure, whereas for decavanadate, the concentration of vanadium increased in cytosolic (0.020+/-0.005 microg/g) and mitochondrial (0.021+/-0.009 microg/g) fractions. It is concluded that decameric vanadate species are responsible for a strong increase on lipid peroxidation and a decrease in cytosolic catalase activity thus contributing to oxidative stress responses upon vanadate intoxication, in the toadfish heart.

Animals↗

PubMed2000

Vanadate oligomer interactions with myosin.

'Monovanadate' containing a mixture of at least four different vanadate species and 'decavanadate' containing apparently only two vanadate species, mainly decameric species, inhibit myosin and actomyosin ATPase activities. The addition of myosin to 'monovanadate' and 'decavanadate' solutions promotes differential increases on the 51V NMR spectral linewidths of vanadate oligomers. The relative order of line broadening upon myosin addition, reflecting the interaction of the vanadate oligomers with the protein, was V10 > V4 > V1 = 1, whereas no changes were observed for monomeric vanadate species. It is concluded that decameric and tetrameric vanadate species interact quite potently with the protein and affect myosin as well actomyosin ATPase activities.

Animals↗

PubMed2000

Vanadate oligomer inhibition of passive and active Ca2+ translocation by the Ca2+ pump of sarcoplasmic reticulum.

'Monovanadate' containing mainly monomeric, dimeric and tetrameric vanadate species or 'decavanadate', containing mainly decameric vanadate species inhibits the passive and the active efflux of Ca2+ through the sarcoplasmic reticulum calcium pump. When the efflux of Ca2+ by sarcoplasmic reticulum vesicles is not associated with ATP synthesis both vanadate solutions inhibit the passive efflux of Ca2+. However, only 'decavanadate' exerts noticeable effects when the efflux of Ca2+ is associated with ATP synthesis being the active efflux of Ca2+ almost completely inhibited by decameric species concentration as low as 40 microM.

Adenosine Triphosphate↗

PubMed1994

Vanadate oligoanions interact with the proton ejection by the Ca2+ pump of sarcoplasmic reticulum.

Decameric vanadate differs from other oligomeric vanadate species in inhibiting Ca2+ uptake and H+ ejection promoted by sarcoplasmic reticulum ATPase. A decavanadate solution, 2 mM in total vanadium, containing about 200 microM decameric species, inhibits by about 50% the uptake of Ca2+ and by 75% the H+ ejection, whereas 2 mM nominal monovanadate slightly increases the uptake of Ca2+ and inhibits the ejection of H+ by 25%. Moreover, decavanadate linearly increases the Ca2+/H+ ratio, whereas monovanadate mimicks decavanadate behavior only at concentrations up to 1.2 mM. For higher concentrations of monovanadate, this effect is reversed probably due to the formation of metavanadates, namely tetravandate. It is concluded that Ca2+ uptake is tightly coupled to proton ejection through molecular events that are sensitive to the interaction of vanadate species. Apparently, the stoichiometry is variable and modulated by molecular events involved in vanadate interaction suggesting alterations in the energetic coupling associated with Ca2+ translocation.

Animals↗

PubMed1994

The cleavage of phosphoenolpyruvate by vanadate.

Vanadate rapidly promotes the cleavage of phosphoenolpyruvate with phosphate liberation. This was not observed when ATP, glucose-6-phosphate and acetyl phosphate were incubated with vanadate. 51V NMR spectra shows that phosphoenolpyruvate and acetyl phosphate broadened and shifted upfield the monomeric vanadate signal at -561 ppm, indicative of vanadate/phosphate interactions. Comparatively, smaller changes were detected when glucose-6-phosphate was added to the vanadate solution. The shift behavior was not observed in the presence of ATP, ADP or pyruvate.

Adenine Nucleotides↗

PubMed1994

Interactions of vanadate oligomers with sarcoplasmic reticulum Ca(2+)-ATPase.

Upon addition of sarcoplasmic reticulum (SR), the line width of tetrameric vanadate signal of 51V-NMR spectra narrowed in the presence of ATP and Ca2+, whereas monomeric vanadate line widths were broadened. Thus, ATP decreases the affinity of the enzyme for tetravanadate whereas it induces the interaction with monomeric vanadate. In the presence of Ca2+ it was observed that tetrameric and decameric vanadate bind to SR ATPase whereas monomeric vanadate only binds to SR when ATP is present. However, decameric vanadate clearly differs from vanadate oligomers present in monovanadate solutions in preventing the accumulation of Ca2+ by sarcoplasmic reticulum (SR) vesicles coupled to ATP hydrolysis. Mg2+ increased the inhibitory effect promoted by decavanadate whereas a slight enhancement of Ca2+ uptake was observed in the presence of monovanadate. For 5 mM Mg2+, a nominal 2 mM vanadium 'decavanadate' solution containing about 190 to 200 microM decameric and less than 100 microM monomeric species depressed the rate of Ca2+ uptake by 50% whereas a nominal 2 mM monovanadate solution containing about 662 microM monomeric, 143 microM dimeric and 252 microM tetrameric species had no effect on the rate of Ca2+ accumulation. However, 2 mM 'decavanadate' inhibits by 75% the SR Ca(2+)-ATPase activity whereas the presence of 2 mM 'monovanadate' produces an inhibitory effect below 50%. Therefore, the Ca:ATP stoichiometry of Ca2+ transport is enhanced by monovanadate. In the presence of oxalate, inhibition of SR Ca(2+)-ATPase activity by these solutions is enhanced to 97% and 86% whereas in the presence of the ionophore lasalocid, the inhibitory values were 87% and 19% for 2 mM decavanadate and 2 mM monovanadate solutions, respectively. Apparently, the increase of vesicular Ca2+ concentration counteracts monovanadate inhibition of SR Ca(2+)-ATPase activity but it does not significantly affect decavanadate inhibition.

Adenosine Triphosphate↗