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
Нема приказа
Аутори
Krinulović, KatarinaBugarčić, Živadin D.
Vrvić, Miroslav M.
Krstić, Danijela Z.
Vasić, Vesna M.
Чланак у часопису
Метаподаци
Приказ свих података о документуАпстракт
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 nega...tive 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.
Кључне речи:
Na/K-ATPase / Pd(II) complex / prevention and recovery of inhibition / glutathione / L-cysteineИзвор:
Toxicology in Vitro, 2006, 20, 8, 1292-1299
DOI: 10.1016/j.tiv.2006.03.002
ISSN: 0887-2333
PubMed: 16697549
WoS: 000242136100004
Scopus: 2-s2.0-33749657607
Колекције
Институција/група
VinčaTY - 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 . .