Biological effects of a complex of vanadium(V) with salicylaldehyde semicarbazone in osteoblasts in culture: Mechanism of action

Rivadeneira, Josefina; Barrio, Daniel Alejandro; Arrambide, Gabriel; Gambino, Dinorah; Bruzzone, Liliana; Etcheverry, Susana B.

doi:10.1016/j.jinorgbio.2008.11.009

Cited by 56 publications

(44 citation statements)

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“…UMR-106 cells have been widely used for the evaluation of cytotoxicity of different compounds of clinical interest during the last two decades. [29][30][31] On the basis of previous observations on the key role of early biofilm formation in implant-related infections, the present study was designed to find a CHX drug delivery system with suitable antiadherent properties and drug release rate, effective as antimicrobial agent during the initial bacterial adhesion, and free of cytotoxic effects. Thus, CHX-containing titanium/polybenzyl acrylate coatings (Ti/PBA-CHX) with different drug loads were used.…”

Section: Introductionmentioning

confidence: 99%

Chlorhexidine delivery system from titanium/polybenzyl acrylate coating: Evaluation of cytotoxicity and early bacterial adhesion

Cortizo

Oberti

Cortizo

et al. 2012

Journal of Dentistry

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Section: Introductionmentioning

confidence: 99%

Chlorhexidine delivery system from titanium/polybenzyl acrylate coating: Evaluation of cytotoxicity and early bacterial adhesion

Cortizo

Oberti

Cortizo

et al. 2012

Journal of Dentistry

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“…Cellular studies have shown that vanadium compounds induce changes in actin cytoskeleton, which are responsible for morphological and cell proliferation alterations. 8,9 These effects are probably induced through the inhibition of protein tyrosine phosphatases, as referred above, or eventually through reactive oxygen species generation, hence it is well known that transition elements, such as vanadium, promote Fenton-like reactions. These actions could explain, at least in part, the increasing interest in vanadium for antitumor effects, 10 as well as antidiabetic agents, this latter process being induced through an insulin dependent or insulin independent pathway, 6,11,12 although the mechanisms of action are still to be clarified.…”

Section: Introductionmentioning

confidence: 99%

Recent advances into vanadyl, vanadate and decavanadate interactions with actin

2012

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Although the number of papers about ''vanadium'' has doubled in the last decade, the studies about ''vanadium and actin'' are scarce. In the present review, the effects of vanadyl, vanadate and decavanadate on actin structure and function are compared. Decavanadate 51 V NMR signals, at À516 ppm, broadened and decreased in intensity upon actin titration, whereas no effects were observed for vanadate monomers, at À560 ppm. Decavanadate is the only species inducing actin cysteine oxidation and vanadyl formation, both processes being prevented by the natural ligand of the protein, ATP. Vanadyl titration with monomeric actin (G-actin), analysed by EPR spectroscopy, reveals a 1 : 1 binding stoichiometry and a K d of 7.5 mM À1 . Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC 50 of 68 and 300 mM, respectively, as analysed by light scattering assays, whereas no effects were detected for vanadate up to 2 mM. However, only vanadyl (up to 200 mM) induces 100% of G-actin intrinsic fluorescence quenching, whereas decavanadate shows an opposite effect, which suggests the presence of vanadyl high affinity actin binding sites. Decavanadate increases (2.6-fold) the actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Both vanadium species increased the e-ATP exchange rate (k = 6.5 Â 10 À3 s À1 and 4.47 Â 10 À3 s À1 for decavanadate and vanadyl, respectively). Finally, 1 H NMR spectra of G-actin treated with 0.1 mM decavanadate clearly indicate that major alterations occur in protein structure, which are much less visible in the presence of ATP, confirming the preventive effect of the nucleotide on the decavanadate interaction with the protein. Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl. By affecting actin structure and function, vanadium can regulate many cellular processes of great physiological significance.

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“…Vanadium changes in cells morphology are associated with reorganization of specific cytoskeleton proteins such as actin [49]. Although the mode of action of oxidovanadium(IV) and complexes has not been completely revealed yet, it was described that in osteoblasts exposed to a vanadium(V) complex, actin filaments were disrupted, whereas the complex also enhanced the level reactive oxygen species (ROS) [50]. On the other hand, one of the earliest events induced by ROS is thought to be the actin cytoskeleton disruption, a frequent feature in both apoptotic and necrotic cell death [51].…”

Section: Discussionmentioning

confidence: 99%