TY  - JOUR
AU  - Petrovic, Voin
AU  - Čolović, Mirjana B.
AU  - Krstić, Danijela Z.
AU  - Vujačić, Ana V.
AU  - Petrović, Sandra
AU  - Joksić, Gordana
AU  - Bugarčić, Živadin D.
AU  - Vasić, Vesna M.
PY  - 2013
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5539
AB  - The in vitro influence of gold(III) complexes, H[AuCl4], [Au(DMSO)(2)Cl-2]Cl and [Au(bipy)Cl-2]Cl (bipy = 2,2-bipyridine), upon commercially available Na+ /K+ ATPase activity, purified from porcine brain cortex, was investigated. Additionally, the complexes were tested on human lymphocytes, and incidence of micronuclei and cell proliferation index was determined. Concentration-dependent inhibition of the enzyme for all three compounds was obtained, but with differing potencies. Calculated IC50 from Hill analysis were (in M): 5.75 x 10(-7), 5.50 x 10(-6) and 3.98 x 10(-5), for H[AuCl4], [Au(DMSO)(2)Cl-2]Cl and [Au(bipy)Cl-2]Cl, respectively, while Hill coefficient values, n, were above 1 in all cases. This inhibition can be prevented using -SH donating ligands such as L-Cys and glutathione, and these ligands can also cause a recovery of the enzyme activity after the induced inhibition. Kinetic analysis demonstrated that each of the studied gold(III) complexes affects Na+ /K+ ATPase reducing maximum enzymatic velocity, V-max, but not significantly changing the affinity for the substrate (K-M value), implying a noncompetitive mode of the interaction. Furthermore, among investigated gold(III) complexes, the [Au(bipy)Cl-2]Cl complex exhibits a strong cytotoxic effect on human lymphocytes, which suggests its potential for use in antitumor therapy. (C(C) 2013 Elsevier Inc. All rights reserved.
T2  - Journal of Inorganic Biochemistry
T1  - In vitro effects of some gold complexes on Na+/K+ ATPase activity and cell proliferation
VL  - 124
SP  - 35
EP  - 41
DO  - 10.1016/j.jinorgbio.2013.03.013
ER  - 

@article{
author = "Petrovic, Voin and Čolović, Mirjana B. and Krstić, Danijela Z. and Vujačić, Ana V. and Petrović, Sandra and Joksić, Gordana and Bugarčić, Živadin D. and Vasić, Vesna M.",
year = "2013",
abstract = "The in vitro influence of gold(III) complexes, H[AuCl4], [Au(DMSO)(2)Cl-2]Cl and [Au(bipy)Cl-2]Cl (bipy = 2,2-bipyridine), upon commercially available Na+ /K+ ATPase activity, purified from porcine brain cortex, was investigated. Additionally, the complexes were tested on human lymphocytes, and incidence of micronuclei and cell proliferation index was determined. Concentration-dependent inhibition of the enzyme for all three compounds was obtained, but with differing potencies. Calculated IC50 from Hill analysis were (in M): 5.75 x 10(-7), 5.50 x 10(-6) and 3.98 x 10(-5), for H[AuCl4], [Au(DMSO)(2)Cl-2]Cl and [Au(bipy)Cl-2]Cl, respectively, while Hill coefficient values, n, were above 1 in all cases. This inhibition can be prevented using -SH donating ligands such as L-Cys and glutathione, and these ligands can also cause a recovery of the enzyme activity after the induced inhibition. Kinetic analysis demonstrated that each of the studied gold(III) complexes affects Na+ /K+ ATPase reducing maximum enzymatic velocity, V-max, but not significantly changing the affinity for the substrate (K-M value), implying a noncompetitive mode of the interaction. Furthermore, among investigated gold(III) complexes, the [Au(bipy)Cl-2]Cl complex exhibits a strong cytotoxic effect on human lymphocytes, which suggests its potential for use in antitumor therapy. (C(C) 2013 Elsevier Inc. All rights reserved.",
journal = "Journal of Inorganic Biochemistry",
title = "In vitro effects of some gold complexes on Na+/K+ ATPase activity and cell proliferation",
volume = "124",
pages = "35-41",
doi = "10.1016/j.jinorgbio.2013.03.013"
}

Petrovic, V., Čolović, M. B., Krstić, D. Z., Vujačić, A. V., Petrović, S., Joksić, G., Bugarčić, Ž. D.,& Vasić, V. M.. (2013). In vitro effects of some gold complexes on Na+/K+ ATPase activity and cell proliferation. in Journal of Inorganic Biochemistry, 124, 35-41.
https://doi.org/10.1016/j.jinorgbio.2013.03.013

Petrovic V, Čolović MB, Krstić DZ, Vujačić AV, Petrović S, Joksić G, Bugarčić ŽD, Vasić VM. In vitro effects of some gold complexes on Na+/K+ ATPase activity and cell proliferation. in Journal of Inorganic Biochemistry. 2013;124:35-41.
doi:10.1016/j.jinorgbio.2013.03.013 .

Petrovic, Voin, Čolović, Mirjana B., Krstić, Danijela Z., Vujačić, Ana V., Petrović, Sandra, Joksić, Gordana, Bugarčić, Živadin D., Vasić, Vesna M., "In vitro effects of some gold complexes on Na+/K+ ATPase activity and cell proliferation" in Journal of Inorganic Biochemistry, 124 (2013):35-41,
https://doi.org/10.1016/j.jinorgbio.2013.03.013 . .

TY  - JOUR
AU  - Petković, Marijana
AU  - Vujačić, Ana V.
AU  - Schiller, Jürgen
AU  - Bugarčić, Živadin D.
AU  - Savić, Jasmina
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3697
AB  - Attempts are being made to overcome the resistance of tumour cells to platinum (Pt) drugs by the synthesis of new generations of Pt complexes, and it is important to find appropriate and simple methods for the characterization of those novel complexes. The additional applicability of such a method for the analysis of the interactions of metal complexes with biomolecules would be advantageous. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) seems to possess the capability to become this method of choice, since it could be applied to low-mass complexes as well as for the analysis of large biomolecules. In this work the applicability of flavonoids - quercetin and rutin - as matrices for MALDI-TOFMS analysis of dichlorido(ethylendiamine)platinum(II) ([PtCl(2)(en)]), dichlorido(diaminocyclohexane)platinum(II) ([PtCl(2)(dach)]) and chloride (diethylenetriamine) palladium(II) chloride ([PdCl(dien)]Cl) complexes is demonstrated. Spectra of Pt(II) and Pd(II) complexes recorded in the presence of quercetin and rutin are rather simple: Pt(II) complexes generate [M+Na](+) or [M+K](+)ions, whereas the investigated Pd(II) complex gives ions generated by the loss of one Cl(-) or HCl. Flavonoids give a relatively small number of well-defined ions in the low-mass region (at m/z 303.3 for quercetin and m/z 633.5 for rutin). Quercetin and rutin can be applied in much lower concentrations than other common MALDI matrices and require rather low laser intensity. We speculate that flavonoids stabilize the structures of the metal complexes and that they may be useful for the analysis of other biologically active metal complexes, thus implying their broader applicability. Copyright (C) 2009 John Wiley and Sons, Ltd.
T2  - Rapid Communications in Mass Spectrometry
T1  - Application of flavonoids - quercetin and rutin - as new matrices for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of Pt(II) and Pd(II) complexes
VL  - 23
IS  - 10
SP  - 1467
EP  - 1475
DO  - 10.1002/rcm.4024
ER  - 

@article{
author = "Petković, Marijana and Vujačić, Ana V. and Schiller, Jürgen and Bugarčić, Živadin D. and Savić, Jasmina and Vasić, Vesna M.",
year = "2009",
abstract = "Attempts are being made to overcome the resistance of tumour cells to platinum (Pt) drugs by the synthesis of new generations of Pt complexes, and it is important to find appropriate and simple methods for the characterization of those novel complexes. The additional applicability of such a method for the analysis of the interactions of metal complexes with biomolecules would be advantageous. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) seems to possess the capability to become this method of choice, since it could be applied to low-mass complexes as well as for the analysis of large biomolecules. In this work the applicability of flavonoids - quercetin and rutin - as matrices for MALDI-TOFMS analysis of dichlorido(ethylendiamine)platinum(II) ([PtCl(2)(en)]), dichlorido(diaminocyclohexane)platinum(II) ([PtCl(2)(dach)]) and chloride (diethylenetriamine) palladium(II) chloride ([PdCl(dien)]Cl) complexes is demonstrated. Spectra of Pt(II) and Pd(II) complexes recorded in the presence of quercetin and rutin are rather simple: Pt(II) complexes generate [M+Na](+) or [M+K](+)ions, whereas the investigated Pd(II) complex gives ions generated by the loss of one Cl(-) or HCl. Flavonoids give a relatively small number of well-defined ions in the low-mass region (at m/z 303.3 for quercetin and m/z 633.5 for rutin). Quercetin and rutin can be applied in much lower concentrations than other common MALDI matrices and require rather low laser intensity. We speculate that flavonoids stabilize the structures of the metal complexes and that they may be useful for the analysis of other biologically active metal complexes, thus implying their broader applicability. Copyright (C) 2009 John Wiley and Sons, Ltd.",
journal = "Rapid Communications in Mass Spectrometry",
title = "Application of flavonoids - quercetin and rutin - as new matrices for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of Pt(II) and Pd(II) complexes",
volume = "23",
number = "10",
pages = "1467-1475",
doi = "10.1002/rcm.4024"
}

Petković, M., Vujačić, A. V., Schiller, J., Bugarčić, Ž. D., Savić, J.,& Vasić, V. M.. (2009). Application of flavonoids - quercetin and rutin - as new matrices for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of Pt(II) and Pd(II) complexes. in Rapid Communications in Mass Spectrometry, 23(10), 1467-1475.
https://doi.org/10.1002/rcm.4024

Petković M, Vujačić AV, Schiller J, Bugarčić ŽD, Savić J, Vasić VM. Application of flavonoids - quercetin and rutin - as new matrices for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of Pt(II) and Pd(II) complexes. in Rapid Communications in Mass Spectrometry. 2009;23(10):1467-1475.
doi:10.1002/rcm.4024 .

Petković, Marijana, Vujačić, Ana V., Schiller, Jürgen, Bugarčić, Živadin D., Savić, Jasmina, Vasić, Vesna M., "Application of flavonoids - quercetin and rutin - as new matrices for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of Pt(II) and Pd(II) complexes" in Rapid Communications in Mass Spectrometry, 23, no. 10 (2009):1467-1475,
https://doi.org/10.1002/rcm.4024 . .

TY  - JOUR
AU  - Krinulović, Katarina
AU  - Bugarčić, Živadin D.
AU  - Vrvić, Miroslav M.
AU  - Krstić, Danijela Z.
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3120
AB  - The effect of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride ([PdCl(dien)]Cl) on the activity of Na/K-ATPase from porcine cerebral cortex was studied in vitro, in the absence and presence of -SH containing ligandS L-cysteine and glutathione (GSH). The aim of the study was to elucidate the mechanism of [PdCl(dien)](+) induced inhibition of the enzyme activity and to examine the ability of thiols to prevent and recover the inhibition. The coordinative interaction between [PdCl(dien)](+) and enzyme was verified by UV and H-1 NMR spectra. The semblance in the changes in absorption spectra of [PdCl(dien)](+) in the presence of Na/K-ATPase and thiols (L-Cysteine and GSH) suggested that the complex ion interacts with enzymatic sulfhydryl groups. [PdCl(dien)](+) inhibited the enzyme activity in a dose-dependent manner. The Hill analysis of the inhibition curve yielded the half-maximum inhibitory activity value, IC50 = 1.21 x 10(-4) M, and Hill coefficient, n = 0.7, suggesting the negative cooperation for binding of [PdCl(dien)](+) to the enzyme. Dependence of the initial reaction rate on the concentration of MgATp(2-) exhibited typical Michelis-Menten kinetics in the absence and presence of the inhibitor. Kinetic analysis showed that [PdCl(dien)](+) inhibited Na/K-ATPase by reducing the maximum reaction rate (V-max), rather than changing the affinity to the substrate (Km). Kinetic parameters derived using Lineweaver-Burk transformation of experimental data indicated the non-competitive nature of Na/K-ATPase inhibition. The inhibitory constant, K-i = 1.05 x 10(-4) M, was determined from secondary replot of Lineweaver-Burk graph, and correlated with stability constants of [Pd(dien)(thiol)] complexes. 1 x 10(-3) M L-Cysteine or GSH prevented the enzyme inhibition induced by Pd(II) complex cation when present below 1 x 10(-4) M. The both thiols completely reversed the inhibited activity in the concentration dependent manner, due to the complex formation with [PdCl(dien)](+). (c) 2006 Elsevier Ltd. All rights reserved.
T2  - Toxicology in Vitro
T1  - Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione
VL  - 20
IS  - 8
SP  - 1292
EP  - 1299
DO  - 10.1016/j.tiv.2006.03.002
ER  - 

@article{
author = "Krinulović, Katarina and Bugarčić, Živadin D. and Vrvić, Miroslav M. and Krstić, Danijela Z. and Vasić, Vesna M.",
year = "2006",
abstract = "The effect of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride ([PdCl(dien)]Cl) on the activity of Na/K-ATPase from porcine cerebral cortex was studied in vitro, in the absence and presence of -SH containing ligandS L-cysteine and glutathione (GSH). The aim of the study was to elucidate the mechanism of [PdCl(dien)](+) induced inhibition of the enzyme activity and to examine the ability of thiols to prevent and recover the inhibition. The coordinative interaction between [PdCl(dien)](+) and enzyme was verified by UV and H-1 NMR spectra. The semblance in the changes in absorption spectra of [PdCl(dien)](+) in the presence of Na/K-ATPase and thiols (L-Cysteine and GSH) suggested that the complex ion interacts with enzymatic sulfhydryl groups. [PdCl(dien)](+) inhibited the enzyme activity in a dose-dependent manner. The Hill analysis of the inhibition curve yielded the half-maximum inhibitory activity value, IC50 = 1.21 x 10(-4) M, and Hill coefficient, n = 0.7, suggesting the negative cooperation for binding of [PdCl(dien)](+) to the enzyme. Dependence of the initial reaction rate on the concentration of MgATp(2-) exhibited typical Michelis-Menten kinetics in the absence and presence of the inhibitor. Kinetic analysis showed that [PdCl(dien)](+) inhibited Na/K-ATPase by reducing the maximum reaction rate (V-max), rather than changing the affinity to the substrate (Km). Kinetic parameters derived using Lineweaver-Burk transformation of experimental data indicated the non-competitive nature of Na/K-ATPase inhibition. The inhibitory constant, K-i = 1.05 x 10(-4) M, was determined from secondary replot of Lineweaver-Burk graph, and correlated with stability constants of [Pd(dien)(thiol)] complexes. 1 x 10(-3) M L-Cysteine or GSH prevented the enzyme inhibition induced by Pd(II) complex cation when present below 1 x 10(-4) M. The both thiols completely reversed the inhibited activity in the concentration dependent manner, due to the complex formation with [PdCl(dien)](+). (c) 2006 Elsevier Ltd. All rights reserved.",
journal = "Toxicology in Vitro",
title = "Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione",
volume = "20",
number = "8",
pages = "1292-1299",
doi = "10.1016/j.tiv.2006.03.002"
}

Krinulović, K., Bugarčić, Ž. D., Vrvić, M. M., Krstić, D. Z.,& Vasić, V. M.. (2006). Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione. in Toxicology in Vitro, 20(8), 1292-1299.
https://doi.org/10.1016/j.tiv.2006.03.002

Krinulović K, Bugarčić ŽD, Vrvić MM, Krstić DZ, Vasić VM. Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione. in Toxicology in Vitro. 2006;20(8):1292-1299.
doi:10.1016/j.tiv.2006.03.002 .

Krinulović, Katarina, Bugarčić, Živadin D., Vrvić, Miroslav M., Krstić, Danijela Z., Vasić, Vesna M., "Prevention and recovery of (mu(3)-diethylentriamino)-chloro-palladium(II)-chloride induced inhibition of Na/K-ATPase by SH containing ligands - L-cysteine and glutathione" in Toxicology in Vitro, 20, no. 8 (2006):1292-1299,
https://doi.org/10.1016/j.tiv.2006.03.002 . .