Molecular mechanisms of redox signalling in homeostasis: adaptation and pathology

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info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173014/RS//

Molecular mechanisms of redox signalling in homeostasis: adaptation and pathology (en)
Молекуларни механизми редокс сигналинга у хомеостази, адаптацији и патологији (sr)
Molekularni mehanizmi redoks signalinga u homeostazi, adaptaciji i patologiji (sr_RS)
Authors

Publications

Oxidative stress and the activity of antioxidative defense enzymes in overwintering honey bees

Kojić, Danijela K.; Purać, Jelena S.; Nikolić, Tatjana V.; Orčić, Snežana M.; Vujanović, Dragana; Ilijević, Konstantin; Vukašinović, Elvira L.; Blagojević, Duško P.

(E. Schweizerbart'sche Verlagsbuchhandlung, 2019)

TY  - JOUR
AU  - Kojić, Danijela K.
AU  - Purać, Jelena S.
AU  - Nikolić, Tatjana V.
AU  - Orčić, Snežana M.
AU  - Vujanović, Dragana
AU  - Ilijević, Konstantin
AU  - Vukašinović, Elvira L.
AU  - Blagojević, Duško P.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3734
AB  - Over the past decades, the number of managed honey bee Apis mellifera L. (Hymenoptera: Apidae) colonies have been decreasing. The majority of losses occur during winter, suggesting that overwintering honey bees are more susceptible to adverse factors. We focused on the oxidative status of overwintering honey bees, particularly at the beginning (November) and end (March) of the wintering period. Colonies from three locations with different anthropogenic influences were selected: Belgrade, an urban zone, Zajača, an industrial zone, and Susek, a rural area. We measured levels of malondialdehyde (MDA), as a marker of lipid peroxidation, as well as the expression and activity of select antioxidative enzymes: Superoxide dismutase (SOD), catalase (CAT) and glutathione S-transferase (GST). Our results show that enzyme activity and gene expression of antioxidative enzymes are influenced by both sample location and the time of sampling. The majority of analyzed genes had significantly reduced expression, at the end of the overwintering period when higher activities of antioxidative enzymes were also recorded. Among the analyzed parameters, SOD activity and gene expression of microsomal GST isoforms were more affected by local environmental conditions, suggesting the complex role of these enzymes in antioxidative defense and detoxification. The higher MDA levels observed at the end of overwintering for all three locations likely reflects accumulated oxidative damage which could be associated with the aging process, brood rearing and/or the onset flying activity.
PB  - E. Schweizerbart'sche Verlagsbuchhandlung
T2  - Entomologia Generalis
T1  - Oxidative stress and the activity of antioxidative defense enzymes in overwintering honey bees
VL  - 39
IS  - 1
SP  - 33
EP  - 44
DO  - 10.1127/entomologia/2019/0743
ER  - 
@article{
author = "Kojić, Danijela K. and Purać, Jelena S. and Nikolić, Tatjana V. and Orčić, Snežana M. and Vujanović, Dragana and Ilijević, Konstantin and Vukašinović, Elvira L. and Blagojević, Duško P.",
year = "2019",
abstract = "Over the past decades, the number of managed honey bee Apis mellifera L. (Hymenoptera: Apidae) colonies have been decreasing. The majority of losses occur during winter, suggesting that overwintering honey bees are more susceptible to adverse factors. We focused on the oxidative status of overwintering honey bees, particularly at the beginning (November) and end (March) of the wintering period. Colonies from three locations with different anthropogenic influences were selected: Belgrade, an urban zone, Zajača, an industrial zone, and Susek, a rural area. We measured levels of malondialdehyde (MDA), as a marker of lipid peroxidation, as well as the expression and activity of select antioxidative enzymes: Superoxide dismutase (SOD), catalase (CAT) and glutathione S-transferase (GST). Our results show that enzyme activity and gene expression of antioxidative enzymes are influenced by both sample location and the time of sampling. The majority of analyzed genes had significantly reduced expression, at the end of the overwintering period when higher activities of antioxidative enzymes were also recorded. Among the analyzed parameters, SOD activity and gene expression of microsomal GST isoforms were more affected by local environmental conditions, suggesting the complex role of these enzymes in antioxidative defense and detoxification. The higher MDA levels observed at the end of overwintering for all three locations likely reflects accumulated oxidative damage which could be associated with the aging process, brood rearing and/or the onset flying activity.",
publisher = "E. Schweizerbart'sche Verlagsbuchhandlung",
journal = "Entomologia Generalis",
title = "Oxidative stress and the activity of antioxidative defense enzymes in overwintering honey bees",
volume = "39",
number = "1",
pages = "33-44",
doi = "10.1127/entomologia/2019/0743"
}
Kojić, D. K., Purać, J. S., Nikolić, T. V., Orčić, S. M., Vujanović, D., Ilijević, K., Vukašinović, E. L.,& Blagojević, D. P.. (2019). Oxidative stress and the activity of antioxidative defense enzymes in overwintering honey bees. in Entomologia Generalis
E. Schweizerbart'sche Verlagsbuchhandlung., 39(1), 33-44.
https://doi.org/10.1127/entomologia/2019/0743
Kojić DK, Purać JS, Nikolić TV, Orčić SM, Vujanović D, Ilijević K, Vukašinović EL, Blagojević DP. Oxidative stress and the activity of antioxidative defense enzymes in overwintering honey bees. in Entomologia Generalis. 2019;39(1):33-44.
doi:10.1127/entomologia/2019/0743 .
Kojić, Danijela K., Purać, Jelena S., Nikolić, Tatjana V., Orčić, Snežana M., Vujanović, Dragana, Ilijević, Konstantin, Vukašinović, Elvira L., Blagojević, Duško P., "Oxidative stress and the activity of antioxidative defense enzymes in overwintering honey bees" in Entomologia Generalis, 39, no. 1 (2019):33-44,
https://doi.org/10.1127/entomologia/2019/0743 . .
1
5
4
3

Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(2019)

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3333
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 1
EP  - 7
DO  - 10.1016/j.cbi.2019.108787
ER  - 
@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "1-7",
doi = "10.1016/j.cbi.2019.108787"
}
Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions, 311, 1-7.
https://doi.org/10.1016/j.cbi.2019.108787
Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:1-7.
doi:10.1016/j.cbi.2019.108787 .
Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):1-7,
https://doi.org/10.1016/j.cbi.2019.108787 . .

Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(2019)

TY  - DATA
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3335
T2  - Chemico-Biological Interactions
T1  - Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787
ER  - 
@misc{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
journal = "Chemico-Biological Interactions",
title = "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787"
}
Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions.
Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions. 2019;..
Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787" in Chemico-Biological Interactions (2019).

Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(Elsevier, 2019)

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3865
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
IS  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 
@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
number = "108787",
doi = "10.1016/j.cbi.2019.108787"
}
Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311(108787).
https://doi.org/10.1016/j.cbi.2019.108787
Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311(108787).
doi:10.1016/j.cbi.2019.108787 .
Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311, no. 108787 (2019),
https://doi.org/10.1016/j.cbi.2019.108787 . .

Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity

Božić, Bojana; Korać, Jelena; Stanković, Dalibor; Stanić, Marina; Romanović, Mima; Pristov-Bogdanović, Jelena; Spasić, Snežana; Popović-Bijelić, Ana; Spasojević, Ivan; Bajčetić, Milica

(Elsevier, 2018)

TY  - JOUR
AU  - Božić, Bojana
AU  - Korać, Jelena
AU  - Stanković, Dalibor
AU  - Stanić, Marina
AU  - Romanović, Mima
AU  - Pristov-Bogdanović, Jelena
AU  - Spasić, Snežana
AU  - Popović-Bijelić, Ana
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/349
AB  - An increase in the copper pool in body fluids has been related to a number of pathological conditions, including infections. Copper ions may affect antibiotics via the formation of coordination bonds and/or redox reactions. Herein, we analyzed the interactions of Cu2+ with eight β-lactam antibiotics using UV–Vis spectrophotometry, EPR spectroscopy, and electrochemical methods. Penicillin G did not show any detectable interactions with Cu2+. Ampicillin, amoxicillin and cephalexin formed stable colored complexes with octahedral coordination environment of Cu2+ with tetragonal distortion, and primary amine group as the site of coordinate bond formation. These β-lactams increased the solubility of Cu2+ in the phosphate buffer. Ceftazidime and Cu2+ formed a complex with a similar geometry and gave rise to an organic radical. Ceftriaxone-Cu2+ complex appears to exhibit different geometry. All complexes showed 1:1 stoichiometry. Cefaclor reduced Cu2+ to Cu1+ that further reacted with molecular oxygen to produce hydrogen peroxide. Finally, meropenem underwent degradation in the presence of copper. The analysis of activity against Escherichia coli and Staphylococcus aureus showed that the effects of meropenem, amoxicillin, ampicillin, and ceftriaxone were significantly hindered in the presence of copper ions. The interactions with copper ions should be taken into account regarding the problem of antibiotic resistance and in the selection of the most efficient antimicrobial therapy for patients with altered copper homeostasis. © 2018 Elsevier Inc.
PB  - Elsevier
T2  - Free Radical Biology and Medicine
T1  - Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity
VL  - 129
SP  - 279
EP  - 285
DO  - 10.1016/j.freeradbiomed.2018.09.038
UR  - Kon_1320
ER  - 
@article{
author = "Božić, Bojana and Korać, Jelena and Stanković, Dalibor and Stanić, Marina and Romanović, Mima and Pristov-Bogdanović, Jelena and Spasić, Snežana and Popović-Bijelić, Ana and Spasojević, Ivan and Bajčetić, Milica",
year = "2018",
abstract = "An increase in the copper pool in body fluids has been related to a number of pathological conditions, including infections. Copper ions may affect antibiotics via the formation of coordination bonds and/or redox reactions. Herein, we analyzed the interactions of Cu2+ with eight β-lactam antibiotics using UV–Vis spectrophotometry, EPR spectroscopy, and electrochemical methods. Penicillin G did not show any detectable interactions with Cu2+. Ampicillin, amoxicillin and cephalexin formed stable colored complexes with octahedral coordination environment of Cu2+ with tetragonal distortion, and primary amine group as the site of coordinate bond formation. These β-lactams increased the solubility of Cu2+ in the phosphate buffer. Ceftazidime and Cu2+ formed a complex with a similar geometry and gave rise to an organic radical. Ceftriaxone-Cu2+ complex appears to exhibit different geometry. All complexes showed 1:1 stoichiometry. Cefaclor reduced Cu2+ to Cu1+ that further reacted with molecular oxygen to produce hydrogen peroxide. Finally, meropenem underwent degradation in the presence of copper. The analysis of activity against Escherichia coli and Staphylococcus aureus showed that the effects of meropenem, amoxicillin, ampicillin, and ceftriaxone were significantly hindered in the presence of copper ions. The interactions with copper ions should be taken into account regarding the problem of antibiotic resistance and in the selection of the most efficient antimicrobial therapy for patients with altered copper homeostasis. © 2018 Elsevier Inc.",
publisher = "Elsevier",
journal = "Free Radical Biology and Medicine",
title = "Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity",
volume = "129",
pages = "279-285",
doi = "10.1016/j.freeradbiomed.2018.09.038",
url = "Kon_1320"
}
Božić, B., Korać, J., Stanković, D., Stanić, M., Romanović, M., Pristov-Bogdanović, J., Spasić, S., Popović-Bijelić, A., Spasojević, I.,& Bajčetić, M.. (2018). Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity. in Free Radical Biology and Medicine
Elsevier., 129, 279-285.
https://doi.org/10.1016/j.freeradbiomed.2018.09.038
Kon_1320
Božić B, Korać J, Stanković D, Stanić M, Romanović M, Pristov-Bogdanović J, Spasić S, Popović-Bijelić A, Spasojević I, Bajčetić M. Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity. in Free Radical Biology and Medicine. 2018;129:279-285.
doi:10.1016/j.freeradbiomed.2018.09.038
Kon_1320 .
Božić, Bojana, Korać, Jelena, Stanković, Dalibor, Stanić, Marina, Romanović, Mima, Pristov-Bogdanović, Jelena, Spasić, Snežana, Popović-Bijelić, Ana, Spasojević, Ivan, Bajčetić, Milica, "Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity" in Free Radical Biology and Medicine, 129 (2018):279-285,
https://doi.org/10.1016/j.freeradbiomed.2018.09.038 .,
Kon_1320 .
1
3
1
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Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity

Božić, Bojana; Korać, Jelena; Stanković, Dalibor; Stanić, Marina; Romanović, Mima; Pristov-Bogdanović, Jelena; Spasić, Snežana; Popović-Bijelić, Ana; Spasojević, Ivan; Bajčetić, Milica

(Elsevier, 2018)

TY  - JOUR
AU  - Božić, Bojana
AU  - Korać, Jelena
AU  - Stanković, Dalibor
AU  - Stanić, Marina
AU  - Romanović, Mima
AU  - Pristov-Bogdanović, Jelena
AU  - Spasić, Snežana
AU  - Popović-Bijelić, Ana
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2940
AB  - An increase in the copper pool in body fluids has been related to a number of pathological conditions, including infections. Copper ions may affect antibiotics via the formation of coordination bonds and/or redox reactions. Herein, we analyzed the interactions of Cu2+ with eight β-lactam antibiotics using UV–Vis spectrophotometry, EPR spectroscopy, and electrochemical methods. Penicillin G did not show any detectable interactions with Cu2+. Ampicillin, amoxicillin and cephalexin formed stable colored complexes with octahedral coordination environment of Cu2+ with tetragonal distortion, and primary amine group as the site of coordinate bond formation. These β-lactams increased the solubility of Cu2+ in the phosphate buffer. Ceftazidime and Cu2+ formed a complex with a similar geometry and gave rise to an organic radical. Ceftriaxone-Cu2+ complex appears to exhibit different geometry. All complexes showed 1:1 stoichiometry. Cefaclor reduced Cu2+ to Cu1+ that further reacted with molecular oxygen to produce hydrogen peroxide. Finally, meropenem underwent degradation in the presence of copper. The analysis of activity against Escherichia coli and Staphylococcus aureus showed that the effects of meropenem, amoxicillin, ampicillin, and ceftriaxone were significantly hindered in the presence of copper ions. The interactions with copper ions should be taken into account regarding the problem of antibiotic resistance and in the selection of the most efficient antimicrobial therapy for patients with altered copper homeostasis. © 2018 Elsevier Inc.
PB  - Elsevier
T2  - Free Radical Biology and Medicine
T1  - Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity
VL  - 129
SP  - 279
EP  - 285
DO  - 10.1016/j.freeradbiomed.2018.09.038
UR  - Kon_1320
ER  - 
@article{
author = "Božić, Bojana and Korać, Jelena and Stanković, Dalibor and Stanić, Marina and Romanović, Mima and Pristov-Bogdanović, Jelena and Spasić, Snežana and Popović-Bijelić, Ana and Spasojević, Ivan and Bajčetić, Milica",
year = "2018",
abstract = "An increase in the copper pool in body fluids has been related to a number of pathological conditions, including infections. Copper ions may affect antibiotics via the formation of coordination bonds and/or redox reactions. Herein, we analyzed the interactions of Cu2+ with eight β-lactam antibiotics using UV–Vis spectrophotometry, EPR spectroscopy, and electrochemical methods. Penicillin G did not show any detectable interactions with Cu2+. Ampicillin, amoxicillin and cephalexin formed stable colored complexes with octahedral coordination environment of Cu2+ with tetragonal distortion, and primary amine group as the site of coordinate bond formation. These β-lactams increased the solubility of Cu2+ in the phosphate buffer. Ceftazidime and Cu2+ formed a complex with a similar geometry and gave rise to an organic radical. Ceftriaxone-Cu2+ complex appears to exhibit different geometry. All complexes showed 1:1 stoichiometry. Cefaclor reduced Cu2+ to Cu1+ that further reacted with molecular oxygen to produce hydrogen peroxide. Finally, meropenem underwent degradation in the presence of copper. The analysis of activity against Escherichia coli and Staphylococcus aureus showed that the effects of meropenem, amoxicillin, ampicillin, and ceftriaxone were significantly hindered in the presence of copper ions. The interactions with copper ions should be taken into account regarding the problem of antibiotic resistance and in the selection of the most efficient antimicrobial therapy for patients with altered copper homeostasis. © 2018 Elsevier Inc.",
publisher = "Elsevier",
journal = "Free Radical Biology and Medicine",
title = "Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity",
volume = "129",
pages = "279-285",
doi = "10.1016/j.freeradbiomed.2018.09.038",
url = "Kon_1320"
}
Božić, B., Korać, J., Stanković, D., Stanić, M., Romanović, M., Pristov-Bogdanović, J., Spasić, S., Popović-Bijelić, A., Spasojević, I.,& Bajčetić, M.. (2018). Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity. in Free Radical Biology and Medicine
Elsevier., 129, 279-285.
https://doi.org/10.1016/j.freeradbiomed.2018.09.038
Kon_1320
Božić B, Korać J, Stanković D, Stanić M, Romanović M, Pristov-Bogdanović J, Spasić S, Popović-Bijelić A, Spasojević I, Bajčetić M. Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity. in Free Radical Biology and Medicine. 2018;129:279-285.
doi:10.1016/j.freeradbiomed.2018.09.038
Kon_1320 .
Božić, Bojana, Korać, Jelena, Stanković, Dalibor, Stanić, Marina, Romanović, Mima, Pristov-Bogdanović, Jelena, Spasić, Snežana, Popović-Bijelić, Ana, Spasojević, Ivan, Bajčetić, Milica, "Coordination and redox interactions of β-lactam antibiotics with Cu2+ in physiological settings and the impact on antibacterial activity" in Free Radical Biology and Medicine, 129 (2018):279-285,
https://doi.org/10.1016/j.freeradbiomed.2018.09.038 .,
Kon_1320 .
1
3
1
3

Supplementary data for the article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Romanović, M.; Pristov, J. B.; Spasić, S.; Popović-Bijelić, A.; Spasojević, I.; Bajčetić, M. Coordination and Redox Interactions of β-Lactam Antibiotics with Cu2+ in Physiological Settings and the Impact on Antibacterial Activity. Free Radical Biology and Medicine 2018, 129, 279–285. https://doi.org/10.1016/j.freeradbiomed.2018.09.038

Božić, Bojana; Korać, Jelena; Stanković, Dalibor; Stanić, Marina; Romanović, Mima; Pristov-Bogdanović, Jelena; Spasić, Snežana; Popović-Bijelić, Ana; Spasojević, Ivan; Bajčetić, Milica

(2018)

TY  - DATA
AU  - Božić, Bojana
AU  - Korać, Jelena
AU  - Stanković, Dalibor
AU  - Stanić, Marina
AU  - Romanović, Mima
AU  - Pristov-Bogdanović, Jelena
AU  - Spasić, Snežana
AU  - Popović-Bijelić, Ana
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2941
T2  - Free Radical Biology and Medicine
T1  - Supplementary data for the article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Romanović, M.; Pristov, J. B.; Spasić, S.; Popović-Bijelić, A.; Spasojević, I.; Bajčetić, M. Coordination and Redox Interactions of β-Lactam Antibiotics with Cu2+ in Physiological Settings and the Impact on Antibacterial Activity. Free Radical Biology and Medicine 2018, 129, 279–285. https://doi.org/10.1016/j.freeradbiomed.2018.09.038
VL  - 129
SP  - 279
EP  - 285
UR  - Kon_1320
ER  - 
@misc{
author = "Božić, Bojana and Korać, Jelena and Stanković, Dalibor and Stanić, Marina and Romanović, Mima and Pristov-Bogdanović, Jelena and Spasić, Snežana and Popović-Bijelić, Ana and Spasojević, Ivan and Bajčetić, Milica",
year = "2018",
journal = "Free Radical Biology and Medicine",
title = "Supplementary data for the article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Romanović, M.; Pristov, J. B.; Spasić, S.; Popović-Bijelić, A.; Spasojević, I.; Bajčetić, M. Coordination and Redox Interactions of β-Lactam Antibiotics with Cu2+ in Physiological Settings and the Impact on Antibacterial Activity. Free Radical Biology and Medicine 2018, 129, 279–285. https://doi.org/10.1016/j.freeradbiomed.2018.09.038",
volume = "129",
pages = "279-285",
url = "Kon_1320"
}
Božić, B., Korać, J., Stanković, D., Stanić, M., Romanović, M., Pristov-Bogdanović, J., Spasić, S., Popović-Bijelić, A., Spasojević, I.,& Bajčetić, M.. (2018). Supplementary data for the article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Romanović, M.; Pristov, J. B.; Spasić, S.; Popović-Bijelić, A.; Spasojević, I.; Bajčetić, M. Coordination and Redox Interactions of β-Lactam Antibiotics with Cu2+ in Physiological Settings and the Impact on Antibacterial Activity. Free Radical Biology and Medicine 2018, 129, 279–285. https://doi.org/10.1016/j.freeradbiomed.2018.09.038. in Free Radical Biology and Medicine, 129, 279-285.
Kon_1320
Božić B, Korać J, Stanković D, Stanić M, Romanović M, Pristov-Bogdanović J, Spasić S, Popović-Bijelić A, Spasojević I, Bajčetić M. Supplementary data for the article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Romanović, M.; Pristov, J. B.; Spasić, S.; Popović-Bijelić, A.; Spasojević, I.; Bajčetić, M. Coordination and Redox Interactions of β-Lactam Antibiotics with Cu2+ in Physiological Settings and the Impact on Antibacterial Activity. Free Radical Biology and Medicine 2018, 129, 279–285. https://doi.org/10.1016/j.freeradbiomed.2018.09.038. in Free Radical Biology and Medicine. 2018;129:279-285.
Kon_1320 .
Božić, Bojana, Korać, Jelena, Stanković, Dalibor, Stanić, Marina, Romanović, Mima, Pristov-Bogdanović, Jelena, Spasić, Snežana, Popović-Bijelić, Ana, Spasojević, Ivan, Bajčetić, Milica, "Supplementary data for the article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Romanović, M.; Pristov, J. B.; Spasić, S.; Popović-Bijelić, A.; Spasojević, I.; Bajčetić, M. Coordination and Redox Interactions of β-Lactam Antibiotics with Cu2+ in Physiological Settings and the Impact on Antibacterial Activity. Free Radical Biology and Medicine 2018, 129, 279–285. https://doi.org/10.1016/j.freeradbiomed.2018.09.038" in Free Radical Biology and Medicine, 129 (2018):279-285,
Kon_1320 .

Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine

Božić, Bojana; Korać, Jelena; Stanković, Dalibor; Stanić, Marina; Popović-Bijelić, Ana; Bogdanović Pristov, Jelena; Spasojević, Ivan; Bajčetić, Milica

(Elsevier Ireland Ltd, Clare, 2017)

TY  - JOUR
AU  - Božić, Bojana
AU  - Korać, Jelena
AU  - Stanković, Dalibor
AU  - Stanić, Marina
AU  - Popović-Bijelić, Ana
AU  - Bogdanović Pristov, Jelena
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3105
AB  - Toxic effects of unconjugated bilirubin (BR) in neonatal hyperbilirubinemia have been related to redox and/or coordinate interactions with Cu2+. However, the development and mechanisms of such interactions at physiological pH have not been resolved. This study shows that BR reduces Cu2+ to Cu1+ in 1:1 stoichiometry. Apparently, BR undergoes degradation, i.e. BR and Cu2+ do not form stable complexes. The binding of Cu2+ to inorganic phosphates, liposomal phosphate groups, or to chelating drug penicillamine, impedes redox interactions with BR. Cu1+ undergoes spontaneous oxidation by O-2 resulting in hydrogen peroxide accumulation and hydroxyl radical production. In relation to this, copper and BR induced synergistic oxidative/damaging effects on erythrocytes membrane, which were alleviated by penicillamine. The production of reactive oxygen species by BR and copper represents a plausible cause of BR toxic effects and cell damage in hyperbilirubinemia. Further examination of therapeutic potentials of copper chelators in the treatment of severe neonatal hyperbilirubinemia is needed.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine
VL  - 278
SP  - 129
EP  - 134
DO  - 10.1016/j.cbi.2017.10.022
ER  - 
@article{
author = "Božić, Bojana and Korać, Jelena and Stanković, Dalibor and Stanić, Marina and Popović-Bijelić, Ana and Bogdanović Pristov, Jelena and Spasojević, Ivan and Bajčetić, Milica",
year = "2017",
abstract = "Toxic effects of unconjugated bilirubin (BR) in neonatal hyperbilirubinemia have been related to redox and/or coordinate interactions with Cu2+. However, the development and mechanisms of such interactions at physiological pH have not been resolved. This study shows that BR reduces Cu2+ to Cu1+ in 1:1 stoichiometry. Apparently, BR undergoes degradation, i.e. BR and Cu2+ do not form stable complexes. The binding of Cu2+ to inorganic phosphates, liposomal phosphate groups, or to chelating drug penicillamine, impedes redox interactions with BR. Cu1+ undergoes spontaneous oxidation by O-2 resulting in hydrogen peroxide accumulation and hydroxyl radical production. In relation to this, copper and BR induced synergistic oxidative/damaging effects on erythrocytes membrane, which were alleviated by penicillamine. The production of reactive oxygen species by BR and copper represents a plausible cause of BR toxic effects and cell damage in hyperbilirubinemia. Further examination of therapeutic potentials of copper chelators in the treatment of severe neonatal hyperbilirubinemia is needed.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine",
volume = "278",
pages = "129-134",
doi = "10.1016/j.cbi.2017.10.022"
}
Božić, B., Korać, J., Stanković, D., Stanić, M., Popović-Bijelić, A., Bogdanović Pristov, J., Spasojević, I.,& Bajčetić, M.. (2017). Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 278, 129-134.
https://doi.org/10.1016/j.cbi.2017.10.022
Božić B, Korać J, Stanković D, Stanić M, Popović-Bijelić A, Bogdanović Pristov J, Spasojević I, Bajčetić M. Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine. in Chemico-Biological Interactions. 2017;278:129-134.
doi:10.1016/j.cbi.2017.10.022 .
Božić, Bojana, Korać, Jelena, Stanković, Dalibor, Stanić, Marina, Popović-Bijelić, Ana, Bogdanović Pristov, Jelena, Spasojević, Ivan, Bajčetić, Milica, "Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine" in Chemico-Biological Interactions, 278 (2017):129-134,
https://doi.org/10.1016/j.cbi.2017.10.022 . .
3
2
3

Supplementary data for article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Popović-Bijelić, A.; Bogdanović Pristov, J.; Spasojević, I.; Bajčetić, M. Mechanisms of Redox Interactions of Bilirubin with Copper and the Effects of Penicillamine. Chemico-Biological Interactions 2017, 278, 129–134. https://doi.org/10.1016/j.cbi.2017.10.022

Božić, Bojana; Korać, Jelena; Stanković, Dalibor; Stanić, Marina; Popović-Bijelić, Ana; Bogdanović Pristov, Jelena; Spasojević, Ivan; Bajčetić, Milica

(Elsevier Ireland Ltd, Clare, 2017)

TY  - DATA
AU  - Božić, Bojana
AU  - Korać, Jelena
AU  - Stanković, Dalibor
AU  - Stanić, Marina
AU  - Popović-Bijelić, Ana
AU  - Bogdanović Pristov, Jelena
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3106
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Supplementary data for article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Popović-Bijelić, A.; Bogdanović Pristov, J.; Spasojević, I.; Bajčetić, M. Mechanisms of Redox Interactions of Bilirubin with Copper and the Effects of Penicillamine. Chemico-Biological Interactions 2017, 278, 129–134. https://doi.org/10.1016/j.cbi.2017.10.022
ER  - 
@misc{
author = "Božić, Bojana and Korać, Jelena and Stanković, Dalibor and Stanić, Marina and Popović-Bijelić, Ana and Bogdanović Pristov, Jelena and Spasojević, Ivan and Bajčetić, Milica",
year = "2017",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Supplementary data for article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Popović-Bijelić, A.; Bogdanović Pristov, J.; Spasojević, I.; Bajčetić, M. Mechanisms of Redox Interactions of Bilirubin with Copper and the Effects of Penicillamine. Chemico-Biological Interactions 2017, 278, 129–134. https://doi.org/10.1016/j.cbi.2017.10.022"
}
Božić, B., Korać, J., Stanković, D., Stanić, M., Popović-Bijelić, A., Bogdanović Pristov, J., Spasojević, I.,& Bajčetić, M.. (2017). Supplementary data for article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Popović-Bijelić, A.; Bogdanović Pristov, J.; Spasojević, I.; Bajčetić, M. Mechanisms of Redox Interactions of Bilirubin with Copper and the Effects of Penicillamine. Chemico-Biological Interactions 2017, 278, 129–134. https://doi.org/10.1016/j.cbi.2017.10.022. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare..
Božić B, Korać J, Stanković D, Stanić M, Popović-Bijelić A, Bogdanović Pristov J, Spasojević I, Bajčetić M. Supplementary data for article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Popović-Bijelić, A.; Bogdanović Pristov, J.; Spasojević, I.; Bajčetić, M. Mechanisms of Redox Interactions of Bilirubin with Copper and the Effects of Penicillamine. Chemico-Biological Interactions 2017, 278, 129–134. https://doi.org/10.1016/j.cbi.2017.10.022. in Chemico-Biological Interactions. 2017;..
Božić, Bojana, Korać, Jelena, Stanković, Dalibor, Stanić, Marina, Popović-Bijelić, Ana, Bogdanović Pristov, Jelena, Spasojević, Ivan, Bajčetić, Milica, "Supplementary data for article: Božić, B.; Korać, J.; Stanković, D. M.; Stanić, M.; Popović-Bijelić, A.; Bogdanović Pristov, J.; Spasojević, I.; Bajčetić, M. Mechanisms of Redox Interactions of Bilirubin with Copper and the Effects of Penicillamine. Chemico-Biological Interactions 2017, 278, 129–134. https://doi.org/10.1016/j.cbi.2017.10.022" in Chemico-Biological Interactions (2017).

Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine

Božić, Bojana; Korać, Jelena; Stanković, Dalibor; Stanić, Marina; Popović-Bijelić, Ana; Pristov-Bogdanović, Jelena; Spasojević, Ivan; Bajčetić, Milica

(Elsevier Ireland Ltd, Clare, 2017)

TY  - JOUR
AU  - Božić, Bojana
AU  - Korać, Jelena
AU  - Stanković, Dalibor
AU  - Stanić, Marina
AU  - Popović-Bijelić, Ana
AU  - Pristov-Bogdanović, Jelena
AU  - Spasojević, Ivan
AU  - Bajčetić, Milica
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2570
AB  - Toxic effects of unconjugated bilirubin (BR) in neonatal hyperbilirubinemia have been related to redox and/or coordinate interactions with Cu2+. However, the development and mechanisms of such interactions at physiological pH have not been resolved. This study shows that BR reduces Cu2+ to Cu1+ in 1:1 stoichiometry. Apparently, BR undergoes degradation, i.e. BR and Cu2+ do not form stable complexes. The binding of Cu2+ to inorganic phosphates, liposomal phosphate groups, or to chelating drug penicillamine, impedes redox interactions with BR. Cu1+ undergoes spontaneous oxidation by O-2 resulting in hydrogen peroxide accumulation and hydroxyl radical production. In relation to this, copper and BR induced synergistic oxidative/damaging effects on erythrocytes membrane, which were alleviated by penicillamine. The production of reactive oxygen species by BR and copper represents a plausible cause of BR toxic effects and cell damage in hyperbilirubinemia. Further examination of therapeutic potentials of copper chelators in the treatment of severe neonatal hyperbilirubinemia is needed.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-biological Interactions
T1  - Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine
VL  - 278
SP  - 129
EP  - 134
DO  - 10.1016/j.cbi.2017.10.022
UR  - Kon_3386
ER  - 
@article{
author = "Božić, Bojana and Korać, Jelena and Stanković, Dalibor and Stanić, Marina and Popović-Bijelić, Ana and Pristov-Bogdanović, Jelena and Spasojević, Ivan and Bajčetić, Milica",
year = "2017",
abstract = "Toxic effects of unconjugated bilirubin (BR) in neonatal hyperbilirubinemia have been related to redox and/or coordinate interactions with Cu2+. However, the development and mechanisms of such interactions at physiological pH have not been resolved. This study shows that BR reduces Cu2+ to Cu1+ in 1:1 stoichiometry. Apparently, BR undergoes degradation, i.e. BR and Cu2+ do not form stable complexes. The binding of Cu2+ to inorganic phosphates, liposomal phosphate groups, or to chelating drug penicillamine, impedes redox interactions with BR. Cu1+ undergoes spontaneous oxidation by O-2 resulting in hydrogen peroxide accumulation and hydroxyl radical production. In relation to this, copper and BR induced synergistic oxidative/damaging effects on erythrocytes membrane, which were alleviated by penicillamine. The production of reactive oxygen species by BR and copper represents a plausible cause of BR toxic effects and cell damage in hyperbilirubinemia. Further examination of therapeutic potentials of copper chelators in the treatment of severe neonatal hyperbilirubinemia is needed.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-biological Interactions",
title = "Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine",
volume = "278",
pages = "129-134",
doi = "10.1016/j.cbi.2017.10.022",
url = "Kon_3386"
}
Božić, B., Korać, J., Stanković, D., Stanić, M., Popović-Bijelić, A., Pristov-Bogdanović, J., Spasojević, I.,& Bajčetić, M.. (2017). Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine. in Chemico-biological Interactions
Elsevier Ireland Ltd, Clare., 278, 129-134.
https://doi.org/10.1016/j.cbi.2017.10.022
Kon_3386
Božić B, Korać J, Stanković D, Stanić M, Popović-Bijelić A, Pristov-Bogdanović J, Spasojević I, Bajčetić M. Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine. in Chemico-biological Interactions. 2017;278:129-134.
doi:10.1016/j.cbi.2017.10.022
Kon_3386 .
Božić, Bojana, Korać, Jelena, Stanković, Dalibor, Stanić, Marina, Popović-Bijelić, Ana, Pristov-Bogdanović, Jelena, Spasojević, Ivan, Bajčetić, Milica, "Mechanisms of redox interactions of bilirubin with copper and the effects of penicillamine" in Chemico-biological Interactions, 278 (2017):129-134,
https://doi.org/10.1016/j.cbi.2017.10.022 .,
Kon_3386 .
3
2
3

Effects of antipsychotic drug administration on antioxidative defense enzymes in male rat kidney

Nikolić-Kokić, Aleksandra; Mijušković, Ana; Tatalović, Nikola; Nestorov, Jelena; Miler, Marko; Oreščanin-Dušić, Zorana; Nikolić, Milan; Milošević, Verica; Blagojević, Duško P.; Spasic, Mihajlo; Miljević, Čedo

(Taylor & Francis Inc, Philadelphia, 2016)

TY  - JOUR
AU  - Nikolić-Kokić, Aleksandra
AU  - Mijušković, Ana
AU  - Tatalović, Nikola
AU  - Nestorov, Jelena
AU  - Miler, Marko
AU  - Oreščanin-Dušić, Zorana
AU  - Nikolić, Milan
AU  - Milošević, Verica
AU  - Blagojević, Duško P.
AU  - Spasic, Mihajlo
AU  - Miljević, Čedo
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2319
AB  - The use of atypical antipsychotic drugs (APD) was reported to be associated with adverse effects on the kidneys. Thus, the aim of this study was to examine whether APD exerted their adverse effects by interfering with the renal antioxidant defense system. Male 3-mo-old Wistar rats were treated for 28 d with ziprasidone (ZIP), clozapine (CLO), or sertindole (SER) using a daily dose recommended for antipsychotic drug therapy. The expression and activities of antioxidant enzymes superoxide dismutase (SOD) type 1 and type 2, catalase (CAT), glutathione reductase (GR), and glutathione S-transferases (GSTs) activity were measured in the kidneys. Changes in the kidneys were also evaluated histologically. Ziprasidone, CLO, and SER reduced renal SOD type 1 and type 2 activities. Decreased CAT activity was observed only in SER-treated rats. An inhibition in GR activity and increased activity of GST was found only after treatment with CLO. Histological analysis showed dilatation of proximal tubules in kidneys with all three drugs. In conclusion, data indicate that redox disturbances may contribute to renal morphologic alterations in proximal tubules in rats treated with all APD.
PB  - Taylor & Francis Inc, Philadelphia
T2  - Journal of Toxicology and Environmental Health. Part A
T1  - Effects of antipsychotic drug administration on antioxidative defense enzymes in male rat kidney
VL  - 79
IS  - 20
SP  - 905
EP  - 911
DO  - 10.1080/15287394.2016.1201706
UR  - Kon_3135
ER  - 
@article{
author = "Nikolić-Kokić, Aleksandra and Mijušković, Ana and Tatalović, Nikola and Nestorov, Jelena and Miler, Marko and Oreščanin-Dušić, Zorana and Nikolić, Milan and Milošević, Verica and Blagojević, Duško P. and Spasic, Mihajlo and Miljević, Čedo",
year = "2016",
abstract = "The use of atypical antipsychotic drugs (APD) was reported to be associated with adverse effects on the kidneys. Thus, the aim of this study was to examine whether APD exerted their adverse effects by interfering with the renal antioxidant defense system. Male 3-mo-old Wistar rats were treated for 28 d with ziprasidone (ZIP), clozapine (CLO), or sertindole (SER) using a daily dose recommended for antipsychotic drug therapy. The expression and activities of antioxidant enzymes superoxide dismutase (SOD) type 1 and type 2, catalase (CAT), glutathione reductase (GR), and glutathione S-transferases (GSTs) activity were measured in the kidneys. Changes in the kidneys were also evaluated histologically. Ziprasidone, CLO, and SER reduced renal SOD type 1 and type 2 activities. Decreased CAT activity was observed only in SER-treated rats. An inhibition in GR activity and increased activity of GST was found only after treatment with CLO. Histological analysis showed dilatation of proximal tubules in kidneys with all three drugs. In conclusion, data indicate that redox disturbances may contribute to renal morphologic alterations in proximal tubules in rats treated with all APD.",
publisher = "Taylor & Francis Inc, Philadelphia",
journal = "Journal of Toxicology and Environmental Health. Part A",
title = "Effects of antipsychotic drug administration on antioxidative defense enzymes in male rat kidney",
volume = "79",
number = "20",
pages = "905-911",
doi = "10.1080/15287394.2016.1201706",
url = "Kon_3135"
}
Nikolić-Kokić, A., Mijušković, A., Tatalović, N., Nestorov, J., Miler, M., Oreščanin-Dušić, Z., Nikolić, M., Milošević, V., Blagojević, D. P., Spasic, M.,& Miljević, Č.. (2016). Effects of antipsychotic drug administration on antioxidative defense enzymes in male rat kidney. in Journal of Toxicology and Environmental Health. Part A
Taylor & Francis Inc, Philadelphia., 79(20), 905-911.
https://doi.org/10.1080/15287394.2016.1201706
Kon_3135
Nikolić-Kokić A, Mijušković A, Tatalović N, Nestorov J, Miler M, Oreščanin-Dušić Z, Nikolić M, Milošević V, Blagojević DP, Spasic M, Miljević Č. Effects of antipsychotic drug administration on antioxidative defense enzymes in male rat kidney. in Journal of Toxicology and Environmental Health. Part A. 2016;79(20):905-911.
doi:10.1080/15287394.2016.1201706
Kon_3135 .
Nikolić-Kokić, Aleksandra, Mijušković, Ana, Tatalović, Nikola, Nestorov, Jelena, Miler, Marko, Oreščanin-Dušić, Zorana, Nikolić, Milan, Milošević, Verica, Blagojević, Duško P., Spasic, Mihajlo, Miljević, Čedo, "Effects of antipsychotic drug administration on antioxidative defense enzymes in male rat kidney" in Journal of Toxicology and Environmental Health. Part A, 79, no. 20 (2016):905-911,
https://doi.org/10.1080/15287394.2016.1201706 .,
Kon_3135 .
3
4
4

Environmental Effects on Superoxide Dismutase and Catalase Activity and Expression in Honey Bee

Nikolić, Tatjana V.; Purać, Jelena S.; Orčić, Snežana M.; Kojić, Danijela K.; Vujanović, Dragana; Stanimirovic, Zoran; Gržetić, Ivan; Ilijević, Konstantin; Šikoparija, Branko; Blagojević, Duško P.

(Wiley-Blackwell, Hoboken, 2015)

TY  - JOUR
AU  - Nikolić, Tatjana V.
AU  - Purać, Jelena S.
AU  - Orčić, Snežana M.
AU  - Kojić, Danijela K.
AU  - Vujanović, Dragana
AU  - Stanimirovic, Zoran
AU  - Gržetić, Ivan
AU  - Ilijević, Konstantin
AU  - Šikoparija, Branko
AU  - Blagojević, Duško P.
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2005
AB  - Understanding the cellular stress response in honey bees will significantly contribute to their conservation. The aim of this study was to analyze the response of the antioxidative enzymes superoxide dismutase and catalase in honey bees related to the presence of toxic metals in different habitats. Three locations were selected: (i) Tunovo on the mountain Golija, as control area, without industry and large human impact, (ii) Belgrade as urban area, and (iii) Zajaca, as mining and industrial zone. Our results showed that the concentrations of lead (Pb) in whole body of bees vary according to habitat, but there was very significant increase of Pb in bees from investigated industrial area. Bees from urban and industrial area had increased expression of both Sod1 and Cat genes, suggesting adaptation to increased oxidative stress. However, in spite increased gene expression, the enzyme activity of catalase was lower in bees from industrial area suggesting inhibitory effect of Pb on catalase. (C) 2015 Wiley Periodicals, Inc.
PB  - Wiley-Blackwell, Hoboken
T2  - Archives of Insect Biochemistry and Physiology
T1  - Environmental Effects on Superoxide Dismutase and Catalase Activity and Expression in Honey Bee
VL  - 90
IS  - 4
SP  - 181
EP  - 194
DO  - 10.1002/arch.21253
UR  - Kon_2960
ER  - 
@article{
author = "Nikolić, Tatjana V. and Purać, Jelena S. and Orčić, Snežana M. and Kojić, Danijela K. and Vujanović, Dragana and Stanimirovic, Zoran and Gržetić, Ivan and Ilijević, Konstantin and Šikoparija, Branko and Blagojević, Duško P.",
year = "2015",
abstract = "Understanding the cellular stress response in honey bees will significantly contribute to their conservation. The aim of this study was to analyze the response of the antioxidative enzymes superoxide dismutase and catalase in honey bees related to the presence of toxic metals in different habitats. Three locations were selected: (i) Tunovo on the mountain Golija, as control area, without industry and large human impact, (ii) Belgrade as urban area, and (iii) Zajaca, as mining and industrial zone. Our results showed that the concentrations of lead (Pb) in whole body of bees vary according to habitat, but there was very significant increase of Pb in bees from investigated industrial area. Bees from urban and industrial area had increased expression of both Sod1 and Cat genes, suggesting adaptation to increased oxidative stress. However, in spite increased gene expression, the enzyme activity of catalase was lower in bees from industrial area suggesting inhibitory effect of Pb on catalase. (C) 2015 Wiley Periodicals, Inc.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Archives of Insect Biochemistry and Physiology",
title = "Environmental Effects on Superoxide Dismutase and Catalase Activity and Expression in Honey Bee",
volume = "90",
number = "4",
pages = "181-194",
doi = "10.1002/arch.21253",
url = "Kon_2960"
}
Nikolić, T. V., Purać, J. S., Orčić, S. M., Kojić, D. K., Vujanović, D., Stanimirovic, Z., Gržetić, I., Ilijević, K., Šikoparija, B.,& Blagojević, D. P.. (2015). Environmental Effects on Superoxide Dismutase and Catalase Activity and Expression in Honey Bee. in Archives of Insect Biochemistry and Physiology
Wiley-Blackwell, Hoboken., 90(4), 181-194.
https://doi.org/10.1002/arch.21253
Kon_2960
Nikolić TV, Purać JS, Orčić SM, Kojić DK, Vujanović D, Stanimirovic Z, Gržetić I, Ilijević K, Šikoparija B, Blagojević DP. Environmental Effects on Superoxide Dismutase and Catalase Activity and Expression in Honey Bee. in Archives of Insect Biochemistry and Physiology. 2015;90(4):181-194.
doi:10.1002/arch.21253
Kon_2960 .
Nikolić, Tatjana V., Purać, Jelena S., Orčić, Snežana M., Kojić, Danijela K., Vujanović, Dragana, Stanimirovic, Zoran, Gržetić, Ivan, Ilijević, Konstantin, Šikoparija, Branko, Blagojević, Duško P., "Environmental Effects on Superoxide Dismutase and Catalase Activity and Expression in Honey Bee" in Archives of Insect Biochemistry and Physiology, 90, no. 4 (2015):181-194,
https://doi.org/10.1002/arch.21253 .,
Kon_2960 .
1
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22
22

Mehanizmi relaksantnog efekta natrijum-sulfida na uterus pacova in vitro

Mijušković, Ana M.

(Универзитет у Београду, Хемијски факултет, 2015)

TY  - THES
AU  - Mijušković, Ana M.
PY  - 2015
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=3022
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:11254/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=47664911
UR  - http://nardus.mpn.gov.rs/123456789/5637
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2667
AB  - Kontrakcije uterusa su važne za regulaciju brojnih reproduktivnihfunkcija. Neregularna i neadekvatna aktivnost uterusa povezana je sa brojnimpatološkim stanjima: neplodnost, neadekavtna implantacija, dismenoreja, kasnetrudnoće i prevremeni porođaji. Kontraktilnost uterusa regulisana jekompleksnom elektrofiziološkom mrežom koja može biti modulirana različitimfarmakološkim i signalnim molekulima.Uterus se karakteriše izuzetnom osobinom, brzom adaptacijom iz stanjamirovanja u oscilatorne cikluse jakih kontrakcija. Ovo je omogućeno zahvaljujućiaktivnosti ćelija koje su sposobne da remodeliraju svoje signalne puteve.Endogeno-sintetisani vodonik-sulfid (H2S), koji je zajedno sa azotmonoksidomi ugljen-monoksidom prepoznat kao gasoviti transmiter, imasignalnu ulogu i u uterusu. Vodonik-sulfid redukuje kontrakcije uterusa iprepoznat je kao agens velikog potencijala u tretmanu oboljenja uterusa. Do sadanisu urađene detaljnije studije, koje su dale uvid u mehanizme njegovogrelaksantnog dejstva na uterusu, te je to od značajnog interesa. Nije poznatoda li subiološki efekti sulfida posredovani njegovim molekulskim oblikom (H2S) ilitiolatnim anjonom (HS−).Rezultati ove disertacije implicirali su da molekulska i anjonska forma nemogu imati identične farmakološke efekte, uključujući i regulaciju konraktilnosti.Efekti H2S/HS− na relaksaciju uterusa upoređeni su sa efektom metantiol (CH3SH,koji „imitira“ H2S). Uočene razlike mogu biti posljedica specifične aktivnosti HS−jona. Ujedno, ovo upoređivanje može biti jedan od načina za razlikovanje efekataH2S i HS−. Metabolizam CH3SH je povezan sa sulfidom, budući da se H2S metiluje doCH3SH i ova metilacija može biti novi način modulacije H2S efekata in vivo.Ispitivano je učešće jonskih kanala (K+, Ca2+, Cl−), kao posrednika u relaksacijiuterusa indukovanoj sa H2S/HS−. Nađeno je da sulfid izaziva reverzibilnukoncentracijski-zavisnu relaksaciju koja je posredovana DIDS-osjetljivim Cl−kanalom. Dodatno, pokazano je da je DIDS-osjetljivi CaCC kanal (engl. Ca2+-...
AB  - Uterine contractions are important in many reproductive functions.Improper or irregular uterine activity may underlie the common pathologicaldisorders such as infertility, improper implantation, dysmenorrhea, weak uterinecontraction during labor and preterm labor. The contractile activity of the uterus isregulated by the complex electrophysiologic network which is highly sensitive tovarious pharmacological and signaling molecules. Remarkably, uterus is able toswitch from quiescence to oscillatory cycles of strong contractions. This isdependent on the activity of the cells being able to remodel their signallingsystems.Endogenously produced hydrogen sulphide (H2S), which, together withNO and CO, is a recognized gasotransmitter, also appears to be a signallingmolecule in rat uterus. Hydrogen sulphide reduces uterine contractility, and it isrecognized as a promising treatment for uterine disorders. There were no studiesabout mechanistic insights of its relaxatory effect, done so far, and thus is ofpotential interest. It is not currently known whether the biological effects of H2Sare mediated directly by H2S or by its derivatives, the most important being thethiolate anion HS−. The results presented in this thesis imply that it appearsunlikely that molecular and anionic forms have pharmacologically identicalactions, including the regulation of contractility. Pharmacological effects ofH2S/HS− were compared to effects of methanethiol (CH3SH, mimicks H2S), andobserved differences might be a consequence of the specific actions of HS−. Thiscomparison may represent a useful tool for discrimination between differentactions of H2S and HS−. The metabolism of CH3SH is intertwined with hydrogensulfide (H2S), since the later is methylated to CH3SH and this methylation may be anew way of modulation of H2S effects in vivo.We investigated the involvement of ion channels (K+, Ca2+, Cl−) in therelaxation of rat uteri induced by H2S/HS−. We found that sulphide induces...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Mehanizmi relaksantnog efekta natrijum-sulfida na uterus pacova in vitro
T1  - reactive species and molecular targets
ER  - 
@phdthesis{
author = "Mijušković, Ana M.",
year = "2015",
abstract = "Kontrakcije uterusa su važne za regulaciju brojnih reproduktivnihfunkcija. Neregularna i neadekvatna aktivnost uterusa povezana je sa brojnimpatološkim stanjima: neplodnost, neadekavtna implantacija, dismenoreja, kasnetrudnoće i prevremeni porođaji. Kontraktilnost uterusa regulisana jekompleksnom elektrofiziološkom mrežom koja može biti modulirana različitimfarmakološkim i signalnim molekulima.Uterus se karakteriše izuzetnom osobinom, brzom adaptacijom iz stanjamirovanja u oscilatorne cikluse jakih kontrakcija. Ovo je omogućeno zahvaljujućiaktivnosti ćelija koje su sposobne da remodeliraju svoje signalne puteve.Endogeno-sintetisani vodonik-sulfid (H2S), koji je zajedno sa azotmonoksidomi ugljen-monoksidom prepoznat kao gasoviti transmiter, imasignalnu ulogu i u uterusu. Vodonik-sulfid redukuje kontrakcije uterusa iprepoznat je kao agens velikog potencijala u tretmanu oboljenja uterusa. Do sadanisu urađene detaljnije studije, koje su dale uvid u mehanizme njegovogrelaksantnog dejstva na uterusu, te je to od značajnog interesa. Nije poznatoda li subiološki efekti sulfida posredovani njegovim molekulskim oblikom (H2S) ilitiolatnim anjonom (HS−).Rezultati ove disertacije implicirali su da molekulska i anjonska forma nemogu imati identične farmakološke efekte, uključujući i regulaciju konraktilnosti.Efekti H2S/HS− na relaksaciju uterusa upoređeni su sa efektom metantiol (CH3SH,koji „imitira“ H2S). Uočene razlike mogu biti posljedica specifične aktivnosti HS−jona. Ujedno, ovo upoređivanje može biti jedan od načina za razlikovanje efekataH2S i HS−. Metabolizam CH3SH je povezan sa sulfidom, budući da se H2S metiluje doCH3SH i ova metilacija može biti novi način modulacije H2S efekata in vivo.Ispitivano je učešće jonskih kanala (K+, Ca2+, Cl−), kao posrednika u relaksacijiuterusa indukovanoj sa H2S/HS−. Nađeno je da sulfid izaziva reverzibilnukoncentracijski-zavisnu relaksaciju koja je posredovana DIDS-osjetljivim Cl−kanalom. Dodatno, pokazano je da je DIDS-osjetljivi CaCC kanal (engl. Ca2+-..., Uterine contractions are important in many reproductive functions.Improper or irregular uterine activity may underlie the common pathologicaldisorders such as infertility, improper implantation, dysmenorrhea, weak uterinecontraction during labor and preterm labor. The contractile activity of the uterus isregulated by the complex electrophysiologic network which is highly sensitive tovarious pharmacological and signaling molecules. Remarkably, uterus is able toswitch from quiescence to oscillatory cycles of strong contractions. This isdependent on the activity of the cells being able to remodel their signallingsystems.Endogenously produced hydrogen sulphide (H2S), which, together withNO and CO, is a recognized gasotransmitter, also appears to be a signallingmolecule in rat uterus. Hydrogen sulphide reduces uterine contractility, and it isrecognized as a promising treatment for uterine disorders. There were no studiesabout mechanistic insights of its relaxatory effect, done so far, and thus is ofpotential interest. It is not currently known whether the biological effects of H2Sare mediated directly by H2S or by its derivatives, the most important being thethiolate anion HS−. The results presented in this thesis imply that it appearsunlikely that molecular and anionic forms have pharmacologically identicalactions, including the regulation of contractility. Pharmacological effects ofH2S/HS− were compared to effects of methanethiol (CH3SH, mimicks H2S), andobserved differences might be a consequence of the specific actions of HS−. Thiscomparison may represent a useful tool for discrimination between differentactions of H2S and HS−. The metabolism of CH3SH is intertwined with hydrogensulfide (H2S), since the later is methylated to CH3SH and this methylation may be anew way of modulation of H2S effects in vivo.We investigated the involvement of ion channels (K+, Ca2+, Cl−) in therelaxation of rat uteri induced by H2S/HS−. We found that sulphide induces...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Mehanizmi relaksantnog efekta natrijum-sulfida na uterus pacova in vitro, reactive species and molecular targets"
}
Mijušković, A. M.. (2015). Mehanizmi relaksantnog efekta natrijum-sulfida na uterus pacova in vitro. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Mijušković AM. Mehanizmi relaksantnog efekta natrijum-sulfida na uterus pacova in vitro. in Универзитет у Београду. 2015;..
Mijušković, Ana M., "Mehanizmi relaksantnog efekta natrijum-sulfida na uterus pacova in vitro" in Универзитет у Београду (2015).

Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study)

Miljević, Čedo; Nikolić-Kokić, Aleksandra; Nikolić, Milan; Niketic, Vesna; Spasic, Mihajlo B.; Lecic-Tosevski, Dusica; Blagojević, Duško P.

(Wiley, Hoboken, 2013)

TY  - JOUR
AU  - Miljević, Čedo
AU  - Nikolić-Kokić, Aleksandra
AU  - Nikolić, Milan
AU  - Niketic, Vesna
AU  - Spasic, Mihajlo B.
AU  - Lecic-Tosevski, Dusica
AU  - Blagojević, Duško P.
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1581
AB  - Objective This study was set out to examine the impact of atypical antipsychotic drugs: aripiprazole, clozapine, ziprasidone, olanzapine, quetiapine, sertindole and amisulpride on the activity of antioxidant defence enzymes in human erythrocytes in vitro. Methods Cu,Zn-superoxide dismutase (SOD1), catalase (CAT), selenium-dependent glutathione peroxidase and glutathione reductase activities were determined after drugs incubation with blood of 15 apparently healthy non-smoking male volunteers (ages 2339) for 1?h at 37?degrees C. Results A statistically significant increase in SOD1 activity was found in samples incubated with aripiprazole (p? lt ?0.01) and quetiapine (p? lt ?0.05) compared with incubated control. SOD1 activity profile following native polyacrylamide gel electrophoresis indicates that aripiprazole and quetiapine protect enzyme activity from inhibition with hydrogen peroxide. Our results showed that sertindole decreases activity of CAT comparing with control non-treated erythrocytes. Moreover, in sertindole treated erythrocytes, negative correlation between SOD1 and glutathione peroxidase activities was found. Increased amount of hydrogen peroxide in such situation may leave erythrocytes and transform their role in circulation from anti-oxidative to pro-oxidative. Conclusions Our results indicate that mechanism through sertindole could express its in vivo toxic effects and point toward possible (neuro)protective effects of aripiprazole and quetiapine.
PB  - Wiley, Hoboken
T2  - Human Psychopharmacology: Clinical and Experimental
T1  - Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study)
VL  - 28
IS  - 1
SP  - 1
EP  - 6
DO  - 10.1002/hup.2272
UR  - Kon_2412
ER  - 
@article{
author = "Miljević, Čedo and Nikolić-Kokić, Aleksandra and Nikolić, Milan and Niketic, Vesna and Spasic, Mihajlo B. and Lecic-Tosevski, Dusica and Blagojević, Duško P.",
year = "2013",
abstract = "Objective This study was set out to examine the impact of atypical antipsychotic drugs: aripiprazole, clozapine, ziprasidone, olanzapine, quetiapine, sertindole and amisulpride on the activity of antioxidant defence enzymes in human erythrocytes in vitro. Methods Cu,Zn-superoxide dismutase (SOD1), catalase (CAT), selenium-dependent glutathione peroxidase and glutathione reductase activities were determined after drugs incubation with blood of 15 apparently healthy non-smoking male volunteers (ages 2339) for 1?h at 37?degrees C. Results A statistically significant increase in SOD1 activity was found in samples incubated with aripiprazole (p? lt ?0.01) and quetiapine (p? lt ?0.05) compared with incubated control. SOD1 activity profile following native polyacrylamide gel electrophoresis indicates that aripiprazole and quetiapine protect enzyme activity from inhibition with hydrogen peroxide. Our results showed that sertindole decreases activity of CAT comparing with control non-treated erythrocytes. Moreover, in sertindole treated erythrocytes, negative correlation between SOD1 and glutathione peroxidase activities was found. Increased amount of hydrogen peroxide in such situation may leave erythrocytes and transform their role in circulation from anti-oxidative to pro-oxidative. Conclusions Our results indicate that mechanism through sertindole could express its in vivo toxic effects and point toward possible (neuro)protective effects of aripiprazole and quetiapine.",
publisher = "Wiley, Hoboken",
journal = "Human Psychopharmacology: Clinical and Experimental",
title = "Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study)",
volume = "28",
number = "1",
pages = "1-6",
doi = "10.1002/hup.2272",
url = "Kon_2412"
}
Miljević, Č., Nikolić-Kokić, A., Nikolić, M., Niketic, V., Spasic, M. B., Lecic-Tosevski, D.,& Blagojević, D. P.. (2013). Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study). in Human Psychopharmacology: Clinical and Experimental
Wiley, Hoboken., 28(1), 1-6.
https://doi.org/10.1002/hup.2272
Kon_2412
Miljević Č, Nikolić-Kokić A, Nikolić M, Niketic V, Spasic MB, Lecic-Tosevski D, Blagojević DP. Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study). in Human Psychopharmacology: Clinical and Experimental. 2013;28(1):1-6.
doi:10.1002/hup.2272
Kon_2412 .
Miljević, Čedo, Nikolić-Kokić, Aleksandra, Nikolić, Milan, Niketic, Vesna, Spasic, Mihajlo B., Lecic-Tosevski, Dusica, Blagojević, Duško P., "Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study)" in Human Psychopharmacology: Clinical and Experimental, 28, no. 1 (2013):1-6,
https://doi.org/10.1002/hup.2272 .,
Kon_2412 .
1
18
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17

The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production

Spasojević, Ivan; Pristov-Bogdanović, Jelena; Vujisić, Ljubodrag V.; Spasic, Mihajlo

(Springer Wien, Wien, 2012)

TY  - JOUR
AU  - Spasojević, Ivan
AU  - Pristov-Bogdanović, Jelena
AU  - Vujisić, Ljubodrag V.
AU  - Spasic, Mihajlo
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1297
AB  - The mechanisms of reaction of methionine with hydroxyl radical are not fully understood. Here, we unequivocally show using electron paramagnetic resonance spin-trapping spectroscopy and GC-FID and GC-MS, the presence of specific carbon-, nitrogen- and sulfur-centered radicals as intermediates of this reaction, as well as the liberation of methanethiol as a gaseous end product. Taking into account the many roles that methionine has in eco- and biosystems, our results may elucidate redox chemistry of this amino acid and processes that methionine is involved in.
PB  - Springer Wien, Wien
T2  - Amino Acids
T1  - The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production
VL  - 42
IS  - 6
SP  - 2439
EP  - 2445
DO  - 10.1007/s00726-011-1049-1
UR  - Kon_2320
ER  - 
@article{
author = "Spasojević, Ivan and Pristov-Bogdanović, Jelena and Vujisić, Ljubodrag V. and Spasic, Mihajlo",
year = "2012",
abstract = "The mechanisms of reaction of methionine with hydroxyl radical are not fully understood. Here, we unequivocally show using electron paramagnetic resonance spin-trapping spectroscopy and GC-FID and GC-MS, the presence of specific carbon-, nitrogen- and sulfur-centered radicals as intermediates of this reaction, as well as the liberation of methanethiol as a gaseous end product. Taking into account the many roles that methionine has in eco- and biosystems, our results may elucidate redox chemistry of this amino acid and processes that methionine is involved in.",
publisher = "Springer Wien, Wien",
journal = "Amino Acids",
title = "The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production",
volume = "42",
number = "6",
pages = "2439-2445",
doi = "10.1007/s00726-011-1049-1",
url = "Kon_2320"
}
Spasojević, I., Pristov-Bogdanović, J., Vujisić, L. V.,& Spasic, M.. (2012). The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production. in Amino Acids
Springer Wien, Wien., 42(6), 2439-2445.
https://doi.org/10.1007/s00726-011-1049-1
Kon_2320
Spasojević I, Pristov-Bogdanović J, Vujisić LV, Spasic M. The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production. in Amino Acids. 2012;42(6):2439-2445.
doi:10.1007/s00726-011-1049-1
Kon_2320 .
Spasojević, Ivan, Pristov-Bogdanović, Jelena, Vujisić, Ljubodrag V., Spasic, Mihajlo, "The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production" in Amino Acids, 42, no. 6 (2012):2439-2445,
https://doi.org/10.1007/s00726-011-1049-1 .,
Kon_2320 .
11
10
11