Stojanović, Srđan

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Authority KeyName Variants
orcid::0000-0002-1847-9318
  • Stojanović, Srđan (8)
  • Stojanović, S. (3)

Author's Bibliography

Oxidative stress and DNA damage in horses naturally infected with Theileria equi

Radaković, Milena; Davitkov, Darko; Borozan, Sunčica; Stojanović, S.; Stevanović, Jevrosima; Krstić, Vanja; Stanimirović, Zoran

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Radaković, Milena
AU  - Davitkov, Darko
AU  - Borozan, Sunčica
AU  - Stojanović, S.
AU  - Stevanović, Jevrosima
AU  - Krstić, Vanja
AU  - Stanimirović, Zoran
PY  - 2016
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1421
AB  - The aim of this study was to determine the concentrations of oxidative stress parameters and DNA damage in horses infected by Theileria equi. Initial screening of 110 horses with duplex PCR enabled the selection of 30 infected horses with T. equi and 30 free of infection (control). Specimens from the 60 horses were further analysed by determining the following oxidative stress parameters: extent of haemolysis (EH), plasma free haemoglobin (PHb), catalase (CAT), Cu,Zn superoxide dismutase (SOD1), paraoxonase (PON1), nitrite (NO2-), total nitrate and nitrite (NOx), malondialdehyde (MDA) and free thiol groups (-SH). In addition, relative distribution of lactate dehydrogenase (LDH1-LDH5) activity and the DNA-damaging effects of T. equi infection were evaluated. Compared to control horses, horses infected with T. equi had significantly higher SOD1 activities (P < 0.05) and PHb (P < 0.01), NO2- (P < 0.001), NOx (P < 0.05) and MDA concentrations (P < 0.001), and significantly-lower EH (P < 0.001), CAT (P < 0.01) and PON1 (P < 0.001) activities, and thiol group concentrations (P < 0.05). The comet assay demonstrated significantly increased DNA damage in T. equi infected cells compared to non-infected cells (P < 0.001). Infected horses had significantly increased LDH5 isoenzyme activities (P < 0.05). There was higher production of ROS/RNS in T. equi-infected horses, which resulted in changes in osmotic fragility, damage to lipids, proteins and DNA, haemolysis and hepatocellular damage. Oxidative stress in horses naturally infected with T equi could contribute to the pathogenesis of the infection.
PB  - Elsevier Sci Ltd, Oxford
T2  - Veterinary Journal
T1  - Oxidative stress and DNA damage in horses naturally infected with Theileria equi
VL  - 217
SP  - 112
EP  - 118
DO  - 10.1016/j.tvjl.2016.10.003
ER  - 
@article{
author = "Radaković, Milena and Davitkov, Darko and Borozan, Sunčica and Stojanović, S. and Stevanović, Jevrosima and Krstić, Vanja and Stanimirović, Zoran",
year = "2016",
abstract = "The aim of this study was to determine the concentrations of oxidative stress parameters and DNA damage in horses infected by Theileria equi. Initial screening of 110 horses with duplex PCR enabled the selection of 30 infected horses with T. equi and 30 free of infection (control). Specimens from the 60 horses were further analysed by determining the following oxidative stress parameters: extent of haemolysis (EH), plasma free haemoglobin (PHb), catalase (CAT), Cu,Zn superoxide dismutase (SOD1), paraoxonase (PON1), nitrite (NO2-), total nitrate and nitrite (NOx), malondialdehyde (MDA) and free thiol groups (-SH). In addition, relative distribution of lactate dehydrogenase (LDH1-LDH5) activity and the DNA-damaging effects of T. equi infection were evaluated. Compared to control horses, horses infected with T. equi had significantly higher SOD1 activities (P < 0.05) and PHb (P < 0.01), NO2- (P < 0.001), NOx (P < 0.05) and MDA concentrations (P < 0.001), and significantly-lower EH (P < 0.001), CAT (P < 0.01) and PON1 (P < 0.001) activities, and thiol group concentrations (P < 0.05). The comet assay demonstrated significantly increased DNA damage in T. equi infected cells compared to non-infected cells (P < 0.001). Infected horses had significantly increased LDH5 isoenzyme activities (P < 0.05). There was higher production of ROS/RNS in T. equi-infected horses, which resulted in changes in osmotic fragility, damage to lipids, proteins and DNA, haemolysis and hepatocellular damage. Oxidative stress in horses naturally infected with T equi could contribute to the pathogenesis of the infection.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Veterinary Journal",
title = "Oxidative stress and DNA damage in horses naturally infected with Theileria equi",
volume = "217",
pages = "112-118",
doi = "10.1016/j.tvjl.2016.10.003"
}
Radaković, M., Davitkov, D., Borozan, S., Stojanović, S., Stevanović, J., Krstić, V.,& Stanimirović, Z.. (2016). Oxidative stress and DNA damage in horses naturally infected with Theileria equi. in Veterinary Journal
Elsevier Sci Ltd, Oxford., 217, 112-118.
https://doi.org/10.1016/j.tvjl.2016.10.003
Radaković M, Davitkov D, Borozan S, Stojanović S, Stevanović J, Krstić V, Stanimirović Z. Oxidative stress and DNA damage in horses naturally infected with Theileria equi. in Veterinary Journal. 2016;217:112-118.
doi:10.1016/j.tvjl.2016.10.003 .
Radaković, Milena, Davitkov, Darko, Borozan, Sunčica, Stojanović, S., Stevanović, Jevrosima, Krstić, Vanja, Stanimirović, Zoran, "Oxidative stress and DNA damage in horses naturally infected with Theileria equi" in Veterinary Journal, 217 (2016):112-118,
https://doi.org/10.1016/j.tvjl.2016.10.003 . .
1
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26

Anion-pi interactions in complexes of proteins and halogen-containing amino acids

Borozan, Sunčica; Zlatović, Mario V.; Stojanović, Srđan

(Springer, New York, 2016)

TY  - JOUR
AU  - Borozan, Sunčica
AU  - Zlatović, Mario V.
AU  - Stojanović, Srđan
PY  - 2016
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1387
AB  - We analyzed the potential influence of anion-pi interactions on the stability of complexes of proteins and halogen-containing non-natural amino acids. Anion-pi interactions are distance and orientation dependent and our ab initio calculations showed that their energy can be lower than -8 kcal mol(-1), while most of their interaction energies lie in the range from -1 to -4 kcal mol(-1). About 20 % of these interactions were found to be repulsive. We have observed that Tyr has the highest occurrence among the aromatic residues involved in anion-pi interactions, while His made the least contribution. Furthermore, our study showed that 67 % of total interactions in the dataset are multiple anion-pi interactions. Most of the amino acid residues involved in anion-pi interactions tend to be buried in the solvent-excluded environment. The majority of the anion-pi interacting residues are located in regions with helical secondary structure. Analysis of stabilization centers for these complexes showed that all of the six residues capable of anion-pi interactions are important in locating one or more of such centers. We found that anion-pi interacting residues are sometimes involved in simultaneous interactions with halogens as well. With all that in mind, we can conclude that the anion-pi interactions can show significant influence on molecular organization and on the structural stability of the complexes of proteins and halogen-containing non-natural amino acids. Their influence should not be neglected in supramolecular chemistry and crystal engineering fields as well.
PB  - Springer, New York
T2  - Journal of Biological Inorganic Chemistry
T1  - Anion-pi interactions in complexes of proteins and halogen-containing amino acids
VL  - 21
IS  - 3
SP  - 357
EP  - 368
DO  - 10.1007/s00775-016-1346-y
ER  - 
@article{
author = "Borozan, Sunčica and Zlatović, Mario V. and Stojanović, Srđan",
year = "2016",
abstract = "We analyzed the potential influence of anion-pi interactions on the stability of complexes of proteins and halogen-containing non-natural amino acids. Anion-pi interactions are distance and orientation dependent and our ab initio calculations showed that their energy can be lower than -8 kcal mol(-1), while most of their interaction energies lie in the range from -1 to -4 kcal mol(-1). About 20 % of these interactions were found to be repulsive. We have observed that Tyr has the highest occurrence among the aromatic residues involved in anion-pi interactions, while His made the least contribution. Furthermore, our study showed that 67 % of total interactions in the dataset are multiple anion-pi interactions. Most of the amino acid residues involved in anion-pi interactions tend to be buried in the solvent-excluded environment. The majority of the anion-pi interacting residues are located in regions with helical secondary structure. Analysis of stabilization centers for these complexes showed that all of the six residues capable of anion-pi interactions are important in locating one or more of such centers. We found that anion-pi interacting residues are sometimes involved in simultaneous interactions with halogens as well. With all that in mind, we can conclude that the anion-pi interactions can show significant influence on molecular organization and on the structural stability of the complexes of proteins and halogen-containing non-natural amino acids. Their influence should not be neglected in supramolecular chemistry and crystal engineering fields as well.",
publisher = "Springer, New York",
journal = "Journal of Biological Inorganic Chemistry",
title = "Anion-pi interactions in complexes of proteins and halogen-containing amino acids",
volume = "21",
number = "3",
pages = "357-368",
doi = "10.1007/s00775-016-1346-y"
}
Borozan, S., Zlatović, M. V.,& Stojanović, S.. (2016). Anion-pi interactions in complexes of proteins and halogen-containing amino acids. in Journal of Biological Inorganic Chemistry
Springer, New York., 21(3), 357-368.
https://doi.org/10.1007/s00775-016-1346-y
Borozan S, Zlatović MV, Stojanović S. Anion-pi interactions in complexes of proteins and halogen-containing amino acids. in Journal of Biological Inorganic Chemistry. 2016;21(3):357-368.
doi:10.1007/s00775-016-1346-y .
Borozan, Sunčica, Zlatović, Mario V., Stojanović, Srđan, "Anion-pi interactions in complexes of proteins and halogen-containing amino acids" in Journal of Biological Inorganic Chemistry, 21, no. 3 (2016):357-368,
https://doi.org/10.1007/s00775-016-1346-y . .
14
8
12

Implications of oxidative stress in occupational exposure to lead on a cellular level

Čabarkapa, Andrea; Borozan, Sunčica; Živković, Lada; Milanović-Čabarkapa, Mirjana; Stojanović, Srđan; Bajić, Vladan; Spremo-Potparević, Biljana

(Taylor & Francis Ltd, Abingdon, 2015)

TY  - JOUR
AU  - Čabarkapa, Andrea
AU  - Borozan, Sunčica
AU  - Živković, Lada
AU  - Milanović-Čabarkapa, Mirjana
AU  - Stojanović, Srđan
AU  - Bajić, Vladan
AU  - Spremo-Potparević, Biljana
PY  - 2015
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1827
AB  - The aim of this study was to determine oxidative alterations leading to cellular dysfunctions in Pb-exposed subjects by evaluating damage to all major classes of biomolecules in the cell, lipid peroxidation, protein and DNA damage and determine relationships between parameters of Pb toxicity and specific biomarkers of oxidative damage.Analysis was conducted of smelter workers with high blood Pb and urine aminolevulinic acid levels and slightly elevated values of coproporphyrin and erythrocyte protoporphyrin IX. Significant decreases of thiol groups and increases in carbonyl groups as protein degradation end products, and of nitrite were detected. Elevated rates of lipid peroxidation and rises in the activities of the antioxidant enzymes Cu-Zn superoxide dismutase and catalase were also observed. Both enzymes showed positive correlations with the blood lead levels and urine coproporphyrin, while thiol groups correlated negatively with the same indices. The genotoxic potential of lead was manifested through an increased number of DNA-damaged cells. Increased activities of serum lactate dehydrogenase isoenzymes indicated cellular damage in the lungs, kidneys, and liver. These lead-induced impairments should be taken into consideration in the assessment of Pb-related health hazards.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Toxicology
T1  - Implications of oxidative stress in occupational exposure to lead on a cellular level
VL  - 97
IS  - 6
SP  - 799
EP  - 813
DO  - 10.1080/02772248.2015.1060973
ER  - 
@article{
author = "Čabarkapa, Andrea and Borozan, Sunčica and Živković, Lada and Milanović-Čabarkapa, Mirjana and Stojanović, Srđan and Bajić, Vladan and Spremo-Potparević, Biljana",
year = "2015",
abstract = "The aim of this study was to determine oxidative alterations leading to cellular dysfunctions in Pb-exposed subjects by evaluating damage to all major classes of biomolecules in the cell, lipid peroxidation, protein and DNA damage and determine relationships between parameters of Pb toxicity and specific biomarkers of oxidative damage.Analysis was conducted of smelter workers with high blood Pb and urine aminolevulinic acid levels and slightly elevated values of coproporphyrin and erythrocyte protoporphyrin IX. Significant decreases of thiol groups and increases in carbonyl groups as protein degradation end products, and of nitrite were detected. Elevated rates of lipid peroxidation and rises in the activities of the antioxidant enzymes Cu-Zn superoxide dismutase and catalase were also observed. Both enzymes showed positive correlations with the blood lead levels and urine coproporphyrin, while thiol groups correlated negatively with the same indices. The genotoxic potential of lead was manifested through an increased number of DNA-damaged cells. Increased activities of serum lactate dehydrogenase isoenzymes indicated cellular damage in the lungs, kidneys, and liver. These lead-induced impairments should be taken into consideration in the assessment of Pb-related health hazards.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Toxicology",
title = "Implications of oxidative stress in occupational exposure to lead on a cellular level",
volume = "97",
number = "6",
pages = "799-813",
doi = "10.1080/02772248.2015.1060973"
}
Čabarkapa, A., Borozan, S., Živković, L., Milanović-Čabarkapa, M., Stojanović, S., Bajić, V.,& Spremo-Potparević, B.. (2015). Implications of oxidative stress in occupational exposure to lead on a cellular level. in Toxicology
Taylor & Francis Ltd, Abingdon., 97(6), 799-813.
https://doi.org/10.1080/02772248.2015.1060973
Čabarkapa A, Borozan S, Živković L, Milanović-Čabarkapa M, Stojanović S, Bajić V, Spremo-Potparević B. Implications of oxidative stress in occupational exposure to lead on a cellular level. in Toxicology. 2015;97(6):799-813.
doi:10.1080/02772248.2015.1060973 .
Čabarkapa, Andrea, Borozan, Sunčica, Živković, Lada, Milanović-Čabarkapa, Mirjana, Stojanović, Srđan, Bajić, Vladan, Spremo-Potparević, Biljana, "Implications of oxidative stress in occupational exposure to lead on a cellular level" in Toxicology, 97, no. 6 (2015):799-813,
https://doi.org/10.1080/02772248.2015.1060973 . .
5
3
5

Implications of oxidative stress in occupational exposure to lead on a cellular level

Čabarkapa, Andrea; Borozan, Sunčica; Živković, Lada; Milanović-Čabarkapa, Mirjana; Stojanović, Srđan; Bajić, Vladan; Spremo-Potparević, Biljana

(Taylor & Francis Ltd, Abingdon, 2015)

TY  - JOUR
AU  - Čabarkapa, Andrea
AU  - Borozan, Sunčica
AU  - Živković, Lada
AU  - Milanović-Čabarkapa, Mirjana
AU  - Stojanović, Srđan
AU  - Bajić, Vladan
AU  - Spremo-Potparević, Biljana
PY  - 2015
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1249
AB  - The aim of this study was to determine oxidative alterations leading to cellular dysfunctions in Pb-exposed subjects by evaluating damage to all major classes of biomolecules in the cell, lipid peroxidation, protein and DNA damage and determine relationships between parameters of Pb toxicity and specific biomarkers of oxidative damage.Analysis was conducted of smelter workers with high blood Pb and urine aminolevulinic acid levels and slightly elevated values of coproporphyrin and erythrocyte protoporphyrin IX. Significant decreases of thiol groups and increases in carbonyl groups as protein degradation end products, and of nitrite were detected. Elevated rates of lipid peroxidation and rises in the activities of the antioxidant enzymes Cu-Zn superoxide dismutase and catalase were also observed. Both enzymes showed positive correlations with the blood lead levels and urine coproporphyrin, while thiol groups correlated negatively with the same indices. The genotoxic potential of lead was manifested through an increased number of DNA-damaged cells. Increased activities of serum lactate dehydrogenase isoenzymes indicated cellular damage in the lungs, kidneys, and liver. These lead-induced impairments should be taken into consideration in the assessment of Pb-related health hazards.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Toxicological and Environmental Chemistry
T1  - Implications of oxidative stress in occupational exposure to lead on a cellular level
VL  - 97
IS  - 6
SP  - 799
EP  - 813
DO  - 10.1080/02772248.2015.1060973
ER  - 
@article{
author = "Čabarkapa, Andrea and Borozan, Sunčica and Živković, Lada and Milanović-Čabarkapa, Mirjana and Stojanović, Srđan and Bajić, Vladan and Spremo-Potparević, Biljana",
year = "2015",
abstract = "The aim of this study was to determine oxidative alterations leading to cellular dysfunctions in Pb-exposed subjects by evaluating damage to all major classes of biomolecules in the cell, lipid peroxidation, protein and DNA damage and determine relationships between parameters of Pb toxicity and specific biomarkers of oxidative damage.Analysis was conducted of smelter workers with high blood Pb and urine aminolevulinic acid levels and slightly elevated values of coproporphyrin and erythrocyte protoporphyrin IX. Significant decreases of thiol groups and increases in carbonyl groups as protein degradation end products, and of nitrite were detected. Elevated rates of lipid peroxidation and rises in the activities of the antioxidant enzymes Cu-Zn superoxide dismutase and catalase were also observed. Both enzymes showed positive correlations with the blood lead levels and urine coproporphyrin, while thiol groups correlated negatively with the same indices. The genotoxic potential of lead was manifested through an increased number of DNA-damaged cells. Increased activities of serum lactate dehydrogenase isoenzymes indicated cellular damage in the lungs, kidneys, and liver. These lead-induced impairments should be taken into consideration in the assessment of Pb-related health hazards.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Toxicological and Environmental Chemistry",
title = "Implications of oxidative stress in occupational exposure to lead on a cellular level",
volume = "97",
number = "6",
pages = "799-813",
doi = "10.1080/02772248.2015.1060973"
}
Čabarkapa, A., Borozan, S., Živković, L., Milanović-Čabarkapa, M., Stojanović, S., Bajić, V.,& Spremo-Potparević, B.. (2015). Implications of oxidative stress in occupational exposure to lead on a cellular level. in Toxicological and Environmental Chemistry
Taylor & Francis Ltd, Abingdon., 97(6), 799-813.
https://doi.org/10.1080/02772248.2015.1060973
Čabarkapa A, Borozan S, Živković L, Milanović-Čabarkapa M, Stojanović S, Bajić V, Spremo-Potparević B. Implications of oxidative stress in occupational exposure to lead on a cellular level. in Toxicological and Environmental Chemistry. 2015;97(6):799-813.
doi:10.1080/02772248.2015.1060973 .
Čabarkapa, Andrea, Borozan, Sunčica, Živković, Lada, Milanović-Čabarkapa, Mirjana, Stojanović, Srđan, Bajić, Vladan, Spremo-Potparević, Biljana, "Implications of oxidative stress in occupational exposure to lead on a cellular level" in Toxicological and Environmental Chemistry, 97, no. 6 (2015):799-813,
https://doi.org/10.1080/02772248.2015.1060973 . .
5
3
5

CaNa(2)EDTA chelation attenuates cell damage in workers exposed to lead-a pilot study

Čabarkapa, Andrea; Borozan, Sunčica; Zivković, L.; Stojanović, S.; Milanović-Čabarkapa, Mirjana; Bajić, Vladan; Spremo-Potparević, Biljana

(Elsevier Ireland Ltd, Clare, 2015)

TY  - JOUR
AU  - Čabarkapa, Andrea
AU  - Borozan, Sunčica
AU  - Zivković, L.
AU  - Stojanović, S.
AU  - Milanović-Čabarkapa, Mirjana
AU  - Bajić, Vladan
AU  - Spremo-Potparević, Biljana
PY  - 2015
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1310
AB  - Lead induced oxidative cellular damage and long-term persistence of associated adverse effects increases risk of late-onset diseases. CaNa(2)EDTA chelation is known to remove contaminating metals and to reduce free radical production. The objective was to investigate the impact of chelation therapy on modulation of lead induced cellular damage, restoration of altered enzyme activities and lipid homeostasis in peripheral blood of workers exposed to lead, by comparing the selected biomarkers obtained prior and after five-day CaNa(2)EDTA chelation intervention. The group of smelting factory workers diagnosed with lead intoxication and current lead exposure 5.8 +/- 1.2 years were administered five-day CaNa(2)EDTA chelation. Elevated baseline activity of antioxidant enzymes Cu, Zn-SOD and CAT as well as depleted thiols and increased protein degradation products-carbonyl groups and nitrites, pointing to Pb induced oxidative damage, were restored toward normal values following the treatment. Lead showed inhibitor potency on both RBC AChE and BChE in exposed workers, and chelation re-established the activity of BChE, while RBC AChE remained unaffected. Also, genotoxic effect of lead detected in peripheral blood lymphocytes was significantly decreased after therapy, exhibiting 18.9% DNA damage reduction. Administration of chelation reversed the depressed activity of serum PON 1 and significantly decreased lipid peroxidation detected by the post-chelation reduction of MDA levels. Lactate dehydrogenase LDF1-5 isoenzymes levels showed evident but no significant trend of restoring toward normal control values following chelation. CaNa(2)EDTA chelation ameliorates the alterations linked with Pb mediated oxidative stress, indicating possible benefits in reducing health risks associated with increased oxidative damage in lead exposed populations.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - CaNa(2)EDTA chelation attenuates cell damage in workers exposed to lead-a pilot study
VL  - 242
SP  - 171
EP  - 178
DO  - 10.1016/j.cbi.2015.10.002
ER  - 
@article{
author = "Čabarkapa, Andrea and Borozan, Sunčica and Zivković, L. and Stojanović, S. and Milanović-Čabarkapa, Mirjana and Bajić, Vladan and Spremo-Potparević, Biljana",
year = "2015",
abstract = "Lead induced oxidative cellular damage and long-term persistence of associated adverse effects increases risk of late-onset diseases. CaNa(2)EDTA chelation is known to remove contaminating metals and to reduce free radical production. The objective was to investigate the impact of chelation therapy on modulation of lead induced cellular damage, restoration of altered enzyme activities and lipid homeostasis in peripheral blood of workers exposed to lead, by comparing the selected biomarkers obtained prior and after five-day CaNa(2)EDTA chelation intervention. The group of smelting factory workers diagnosed with lead intoxication and current lead exposure 5.8 +/- 1.2 years were administered five-day CaNa(2)EDTA chelation. Elevated baseline activity of antioxidant enzymes Cu, Zn-SOD and CAT as well as depleted thiols and increased protein degradation products-carbonyl groups and nitrites, pointing to Pb induced oxidative damage, were restored toward normal values following the treatment. Lead showed inhibitor potency on both RBC AChE and BChE in exposed workers, and chelation re-established the activity of BChE, while RBC AChE remained unaffected. Also, genotoxic effect of lead detected in peripheral blood lymphocytes was significantly decreased after therapy, exhibiting 18.9% DNA damage reduction. Administration of chelation reversed the depressed activity of serum PON 1 and significantly decreased lipid peroxidation detected by the post-chelation reduction of MDA levels. Lactate dehydrogenase LDF1-5 isoenzymes levels showed evident but no significant trend of restoring toward normal control values following chelation. CaNa(2)EDTA chelation ameliorates the alterations linked with Pb mediated oxidative stress, indicating possible benefits in reducing health risks associated with increased oxidative damage in lead exposed populations.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "CaNa(2)EDTA chelation attenuates cell damage in workers exposed to lead-a pilot study",
volume = "242",
pages = "171-178",
doi = "10.1016/j.cbi.2015.10.002"
}
Čabarkapa, A., Borozan, S., Zivković, L., Stojanović, S., Milanović-Čabarkapa, M., Bajić, V.,& Spremo-Potparević, B.. (2015). CaNa(2)EDTA chelation attenuates cell damage in workers exposed to lead-a pilot study. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 242, 171-178.
https://doi.org/10.1016/j.cbi.2015.10.002
Čabarkapa A, Borozan S, Zivković L, Stojanović S, Milanović-Čabarkapa M, Bajić V, Spremo-Potparević B. CaNa(2)EDTA chelation attenuates cell damage in workers exposed to lead-a pilot study. in Chemico-Biological Interactions. 2015;242:171-178.
doi:10.1016/j.cbi.2015.10.002 .
Čabarkapa, Andrea, Borozan, Sunčica, Zivković, L., Stojanović, S., Milanović-Čabarkapa, Mirjana, Bajić, Vladan, Spremo-Potparević, Biljana, "CaNa(2)EDTA chelation attenuates cell damage in workers exposed to lead-a pilot study" in Chemico-Biological Interactions, 242 (2015):171-178,
https://doi.org/10.1016/j.cbi.2015.10.002 . .
10
7
9

Anion-pi interactions in protein-porphyrin complexes

Zlatović, Mario V.; Borozan, Sunčica; Nikolić, Milan R.; Stojanović, Srđan

(Royal Soc Chemistry, Cambridge, 2015)

TY  - JOUR
AU  - Zlatović, Mario V.
AU  - Borozan, Sunčica
AU  - Nikolić, Milan R.
AU  - Stojanović, Srđan
PY  - 2015
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/1194
AB  - In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Anion-pi interactions in protein-porphyrin complexes
VL  - 5
IS  - 48
SP  - 38361
EP  - 38372
DO  - 10.1039/c5ra03373j
ER  - 
@article{
author = "Zlatović, Mario V. and Borozan, Sunčica and Nikolić, Milan R. and Stojanović, Srđan",
year = "2015",
abstract = "In this work, we have analyzed the influence of anion-pi interactions on the stability of high resolution protein-porphyrin complex crystal structures. The anion-pi interactions are distance and orientation dependent. Results of ab initio calculations of stabilization energies showed that they lie mostly in the range from -2 to -4 kcal mol(-1) with some of the anion-pi interactions having stabilization energies of up to -16 kcal mol(-1). In the anionic group, the numbers of anion-pi interactions involving Asp and Glu are similar, while His is more often involved in these interactions than other aromatic residues. Furthermore, our study showed that in the dataset used about 70% of the investigated anion-pi interactions are in fact multiple anion-pi interactions. Our results suggest that interacting residues are predominantly located in buried and partially buried regions. The secondary structure of the anion-pi interaction involving residues shows that most of the interacting residues preferred to be in helix conformations. Significant numbers of aromatic residues involved in anion-pi interactions have one or more stabilization centers, providing additional stability to the protein-porphyrin complexes. The conservation patterns indicate that more than half of the residues involved in these interactions are evolutionarily conserved, indicating that the contribution of the anion-pi interaction is an important factor for the structural stability of the investigated protein-porphyrin complexes.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Anion-pi interactions in protein-porphyrin complexes",
volume = "5",
number = "48",
pages = "38361-38372",
doi = "10.1039/c5ra03373j"
}
Zlatović, M. V., Borozan, S., Nikolić, M. R.,& Stojanović, S.. (2015). Anion-pi interactions in protein-porphyrin complexes. in RSC Advances
Royal Soc Chemistry, Cambridge., 5(48), 38361-38372.
https://doi.org/10.1039/c5ra03373j
Zlatović MV, Borozan S, Nikolić MR, Stojanović S. Anion-pi interactions in protein-porphyrin complexes. in RSC Advances. 2015;5(48):38361-38372.
doi:10.1039/c5ra03373j .
Zlatović, Mario V., Borozan, Sunčica, Nikolić, Milan R., Stojanović, Srđan, "Anion-pi interactions in protein-porphyrin complexes" in RSC Advances, 5, no. 48 (2015):38361-38372,
https://doi.org/10.1039/c5ra03373j . .
1
12
12
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Cation-pi interactions in high resolution protein-RNA complex crystal structures

Borozan, Sunčica; Dimitrijević, Blagoje; Stojanović, Srđan

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Borozan, Sunčica
AU  - Dimitrijević, Blagoje
AU  - Stojanović, Srđan
PY  - 2013
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/988
AB  - In this work, we have analyzed the influence of cation-pi interactions to the stability of 59 high resolution protein-RNA complex crystal structures. The total number of Lys and Arg are similar in the dataset as well as the number of their interactions. On the other hand, the aromatic chains of purines are exhibiting more cation-pi interactions than pyrimidines. 35% of the total interactions in the dataset are involved in the formation of multiple cation-pi interactions. The multiple cation-pi interactions have been conserved more than the single interactions. The analysis of the geometry of the cation-pi interactions has revealed that the average distance (d) value falls into distinct ranges corresponding to the multiple (4.28 angstrom) and single (5.50 angstrom) cation-pi interactions. The G-Arg pair has the strongest interaction energy of -3.68 kcal mol(-1) among all the possible pairs of amino acids and bases. Further, we found that the cation-pi interactions due to five-membered rings of A and G are stronger than that with the atoms in six-membered rings. 8.7% stabilizing residues are involved in building cation-pi interactions with the nucleic bases. There are three types of structural motifs significantly over-represented in protein-RNA interfaces: beta-turn-ir, niche-4r and st-staple. Tetraloops and kink-turns are the most abundant RNA motifs in protein-RNA interfaces. Amino acids deployed in the protein-RNA interfaces are deposited in helices, sheets and coils. Arg and Lys, involved in cation-pi interactions, prefer to be in the solvent exposed surface. The results from this study might be used for structure-based prediction and as scaffolds for future protein-RNA complex design.
PB  - Elsevier Sci Ltd, Oxford
T2  - Computational Biology and Chemistry
T1  - Cation-pi interactions in high resolution protein-RNA complex crystal structures
VL  - 47
SP  - 105
EP  - 112
DO  - 10.1016/j.compbiolchem.2013.08.005
ER  - 
@article{
author = "Borozan, Sunčica and Dimitrijević, Blagoje and Stojanović, Srđan",
year = "2013",
abstract = "In this work, we have analyzed the influence of cation-pi interactions to the stability of 59 high resolution protein-RNA complex crystal structures. The total number of Lys and Arg are similar in the dataset as well as the number of their interactions. On the other hand, the aromatic chains of purines are exhibiting more cation-pi interactions than pyrimidines. 35% of the total interactions in the dataset are involved in the formation of multiple cation-pi interactions. The multiple cation-pi interactions have been conserved more than the single interactions. The analysis of the geometry of the cation-pi interactions has revealed that the average distance (d) value falls into distinct ranges corresponding to the multiple (4.28 angstrom) and single (5.50 angstrom) cation-pi interactions. The G-Arg pair has the strongest interaction energy of -3.68 kcal mol(-1) among all the possible pairs of amino acids and bases. Further, we found that the cation-pi interactions due to five-membered rings of A and G are stronger than that with the atoms in six-membered rings. 8.7% stabilizing residues are involved in building cation-pi interactions with the nucleic bases. There are three types of structural motifs significantly over-represented in protein-RNA interfaces: beta-turn-ir, niche-4r and st-staple. Tetraloops and kink-turns are the most abundant RNA motifs in protein-RNA interfaces. Amino acids deployed in the protein-RNA interfaces are deposited in helices, sheets and coils. Arg and Lys, involved in cation-pi interactions, prefer to be in the solvent exposed surface. The results from this study might be used for structure-based prediction and as scaffolds for future protein-RNA complex design.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Computational Biology and Chemistry",
title = "Cation-pi interactions in high resolution protein-RNA complex crystal structures",
volume = "47",
pages = "105-112",
doi = "10.1016/j.compbiolchem.2013.08.005"
}
Borozan, S., Dimitrijević, B.,& Stojanović, S.. (2013). Cation-pi interactions in high resolution protein-RNA complex crystal structures. in Computational Biology and Chemistry
Elsevier Sci Ltd, Oxford., 47, 105-112.
https://doi.org/10.1016/j.compbiolchem.2013.08.005
Borozan S, Dimitrijević B, Stojanović S. Cation-pi interactions in high resolution protein-RNA complex crystal structures. in Computational Biology and Chemistry. 2013;47:105-112.
doi:10.1016/j.compbiolchem.2013.08.005 .
Borozan, Sunčica, Dimitrijević, Blagoje, Stojanović, Srđan, "Cation-pi interactions in high resolution protein-RNA complex crystal structures" in Computational Biology and Chemistry, 47 (2013):105-112,
https://doi.org/10.1016/j.compbiolchem.2013.08.005 . .
12
11
12

Halogen bonding in complexes of proteins and non-natural amino acids

Borozan, Sunčica; Stojanović, Srđan

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Borozan, Sunčica
AU  - Stojanović, Srđan
PY  - 2013
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/987
AB  - In this work, we have analyzed the influence of halogen bonding to the stability of 44 complexes of proteins and non-natural amino acids. Fluorine- and chlorine-containing non-natural amino acids are more prevalent in the dataset, and an even larger number of contacts made by iodine-containing ligands are found. Only few halogen bonds with the hydroxyl oxygens and carboxylate side chains are found in the dataset. Halogen bonds with the nitrogen-containing side chains have higher occurrence than other acceptors. Backbone carbonyl oxygens and nitrogens are to a substantial extent involved in our dataset We have observed a small percentage of interactions involving water as hydrogen bond donors. Additionally, most of the interacting residues comprising the interfaces also show a great degree of conservation. There is a clear interaction hot spot at distances of 3.5-3.7 angstrom and Theta(1) angles of 100-120 degrees. There is also a cluster of contacts featuring short distances (2.6-2.9 angstrom) but only nearly optimal Theta(1) angles (140-160 degrees). 51.3% of stabilizing residues are involved in building halogen bonds with the non-natural amino acids. We discovered three types of structural motifs significantly over-represented: beta-turn-ir, beta-turn-il and niche-4r. The halogen-bonding statistics of the dataset do not show any preference for alpha-helices (36%), beta-sheets (36%), or turns/coils (28%) structures. Most of the amino acid residues that were involved in halogen bonds prefer to be in the solvent excluded environment (buried). Furthermore, we have shown that in amino acid-protein complexes halogen atoms can sometimes be involved in hydrogen bonding interactions with hydrogen bonding-donors. The results from this study might be used for the rational design of halogenated ligands as inhibitors and drugs, and in biomolecular engineering.
PB  - Elsevier Sci Ltd, Oxford
T2  - Computational Biology and Chemistry
T1  - Halogen bonding in complexes of proteins and non-natural amino acids
VL  - 47
SP  - 231
EP  - 239
DO  - 10.1016/j.compbiolchem.2013.10.002
ER  - 
@article{
author = "Borozan, Sunčica and Stojanović, Srđan",
year = "2013",
abstract = "In this work, we have analyzed the influence of halogen bonding to the stability of 44 complexes of proteins and non-natural amino acids. Fluorine- and chlorine-containing non-natural amino acids are more prevalent in the dataset, and an even larger number of contacts made by iodine-containing ligands are found. Only few halogen bonds with the hydroxyl oxygens and carboxylate side chains are found in the dataset. Halogen bonds with the nitrogen-containing side chains have higher occurrence than other acceptors. Backbone carbonyl oxygens and nitrogens are to a substantial extent involved in our dataset We have observed a small percentage of interactions involving water as hydrogen bond donors. Additionally, most of the interacting residues comprising the interfaces also show a great degree of conservation. There is a clear interaction hot spot at distances of 3.5-3.7 angstrom and Theta(1) angles of 100-120 degrees. There is also a cluster of contacts featuring short distances (2.6-2.9 angstrom) but only nearly optimal Theta(1) angles (140-160 degrees). 51.3% of stabilizing residues are involved in building halogen bonds with the non-natural amino acids. We discovered three types of structural motifs significantly over-represented: beta-turn-ir, beta-turn-il and niche-4r. The halogen-bonding statistics of the dataset do not show any preference for alpha-helices (36%), beta-sheets (36%), or turns/coils (28%) structures. Most of the amino acid residues that were involved in halogen bonds prefer to be in the solvent excluded environment (buried). Furthermore, we have shown that in amino acid-protein complexes halogen atoms can sometimes be involved in hydrogen bonding interactions with hydrogen bonding-donors. The results from this study might be used for the rational design of halogenated ligands as inhibitors and drugs, and in biomolecular engineering.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Computational Biology and Chemistry",
title = "Halogen bonding in complexes of proteins and non-natural amino acids",
volume = "47",
pages = "231-239",
doi = "10.1016/j.compbiolchem.2013.10.002"
}
Borozan, S.,& Stojanović, S.. (2013). Halogen bonding in complexes of proteins and non-natural amino acids. in Computational Biology and Chemistry
Elsevier Sci Ltd, Oxford., 47, 231-239.
https://doi.org/10.1016/j.compbiolchem.2013.10.002
Borozan S, Stojanović S. Halogen bonding in complexes of proteins and non-natural amino acids. in Computational Biology and Chemistry. 2013;47:231-239.
doi:10.1016/j.compbiolchem.2013.10.002 .
Borozan, Sunčica, Stojanović, Srđan, "Halogen bonding in complexes of proteins and non-natural amino acids" in Computational Biology and Chemistry, 47 (2013):231-239,
https://doi.org/10.1016/j.compbiolchem.2013.10.002 . .
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Morphological and morphometric characteristics of testicles of immunocastrated pigs

Ušćebrka, Gordana; Baltić, Milan Ž.; Stojanović, S.; Aleksić, Jelena

(Novi Sad : Faculty of Agriculture, 2012)

TY  - CONF
AU  - Ušćebrka, Gordana
AU  - Baltić, Milan Ž.
AU  - Stojanović, S.
AU  - Aleksić, Jelena
PY  - 2012
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/3717
PB  - Novi Sad : Faculty of Agriculture
C3  - International Conference Biological Food Safety & Quality, BFSQ, Belgrade, 4 - 5 October, 2012
T1  - Morphological and morphometric characteristics of testicles of immunocastrated pigs
SP  - 143
EP  - 145
UR  - https://hdl.handle.net/21.15107/rcub_veterinar_3717
ER  - 
@conference{
author = "Ušćebrka, Gordana and Baltić, Milan Ž. and Stojanović, S. and Aleksić, Jelena",
year = "2012",
publisher = "Novi Sad : Faculty of Agriculture",
journal = "International Conference Biological Food Safety & Quality, BFSQ, Belgrade, 4 - 5 October, 2012",
title = "Morphological and morphometric characteristics of testicles of immunocastrated pigs",
pages = "143-145",
url = "https://hdl.handle.net/21.15107/rcub_veterinar_3717"
}
Ušćebrka, G., Baltić, M. Ž., Stojanović, S.,& Aleksić, J.. (2012). Morphological and morphometric characteristics of testicles of immunocastrated pigs. in International Conference Biological Food Safety & Quality, BFSQ, Belgrade, 4 - 5 October, 2012
Novi Sad : Faculty of Agriculture., 143-145.
https://hdl.handle.net/21.15107/rcub_veterinar_3717
Ušćebrka G, Baltić MŽ, Stojanović S, Aleksić J. Morphological and morphometric characteristics of testicles of immunocastrated pigs. in International Conference Biological Food Safety & Quality, BFSQ, Belgrade, 4 - 5 October, 2012. 2012;:143-145.
https://hdl.handle.net/21.15107/rcub_veterinar_3717 .
Ušćebrka, Gordana, Baltić, Milan Ž., Stojanović, S., Aleksić, Jelena, "Morphological and morphometric characteristics of testicles of immunocastrated pigs" in International Conference Biological Food Safety & Quality, BFSQ, Belgrade, 4 - 5 October, 2012 (2012):143-145,
https://hdl.handle.net/21.15107/rcub_veterinar_3717 .

pi-pi and cation-pi interactions in protein-porphyrin complex crystal structures

Dimitrijević, Blagoje; Borozan, Sunčica; Stojanović, Srđan

(Royal Soc Chemistry, Cambridge, 2012)

TY  - JOUR
AU  - Dimitrijević, Blagoje
AU  - Borozan, Sunčica
AU  - Stojanović, Srđan
PY  - 2012
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/935
AB  - In this study we have described the pi-pi and cation-pi interactions between the porphyrin ring and the protein part of porphyrin-containing proteins to better understand their stabilizing role. The number of pi-pi interactions was higher than that of cation-pi interactions in the same set of proteins studied. The pyrrole groups of one porphyrin can be involved in pi-pi interactions with pi systems of another porphyrin in the protein. We have found 5.1% cation-pi interactions between porphyrin Fe2+ metal cations and pi systems of surrounding amino acids as well as the pyrrole rings of other porphyrins. We observed that most of the pi-pi interactions have an energy in the range -0.5 to -2.0 kcal mol(-1), while the cation-pi interactions showed an energy in the range 22 to -4 kcal mol(-1). Further, an appreciable number of metal/cation-pi interaction pairs have an energy in the range -6 to -13 kcal mol(-1). The preferred parallel-stacked orientation is found to be more stable than a T-shaped structure for the full set of pi-pi interaction pairs. In the case of cation-pi interactions, it was found that 44% of the cation-pi interactions involved planar stacking, 37% of the interactions belonged to the oblique category, and the remaining 19% of the interactions were of the orthogonal type. The separation distance between the cation group and the aromatic ring decreases as the interplanar angle decreases. Furthermore, in the present study we have found that 10.4% of pi residues and 3.9% of cationic residues were found to have one or more stabilization centers. Amino acids deployed in the environment of porphyrin rings are deposited in helices and coils. The results from this study might be used for structure-based porphyrin protein prediction and as scaffolds for future porphyrin-containing protein design.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - pi-pi and cation-pi interactions in protein-porphyrin complex crystal structures
VL  - 2
IS  - 33
SP  - 12963
EP  - 12972
DO  - 10.1039/c2ra21937a
ER  - 
@article{
author = "Dimitrijević, Blagoje and Borozan, Sunčica and Stojanović, Srđan",
year = "2012",
abstract = "In this study we have described the pi-pi and cation-pi interactions between the porphyrin ring and the protein part of porphyrin-containing proteins to better understand their stabilizing role. The number of pi-pi interactions was higher than that of cation-pi interactions in the same set of proteins studied. The pyrrole groups of one porphyrin can be involved in pi-pi interactions with pi systems of another porphyrin in the protein. We have found 5.1% cation-pi interactions between porphyrin Fe2+ metal cations and pi systems of surrounding amino acids as well as the pyrrole rings of other porphyrins. We observed that most of the pi-pi interactions have an energy in the range -0.5 to -2.0 kcal mol(-1), while the cation-pi interactions showed an energy in the range 22 to -4 kcal mol(-1). Further, an appreciable number of metal/cation-pi interaction pairs have an energy in the range -6 to -13 kcal mol(-1). The preferred parallel-stacked orientation is found to be more stable than a T-shaped structure for the full set of pi-pi interaction pairs. In the case of cation-pi interactions, it was found that 44% of the cation-pi interactions involved planar stacking, 37% of the interactions belonged to the oblique category, and the remaining 19% of the interactions were of the orthogonal type. The separation distance between the cation group and the aromatic ring decreases as the interplanar angle decreases. Furthermore, in the present study we have found that 10.4% of pi residues and 3.9% of cationic residues were found to have one or more stabilization centers. Amino acids deployed in the environment of porphyrin rings are deposited in helices and coils. The results from this study might be used for structure-based porphyrin protein prediction and as scaffolds for future porphyrin-containing protein design.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "pi-pi and cation-pi interactions in protein-porphyrin complex crystal structures",
volume = "2",
number = "33",
pages = "12963-12972",
doi = "10.1039/c2ra21937a"
}
Dimitrijević, B., Borozan, S.,& Stojanović, S.. (2012). pi-pi and cation-pi interactions in protein-porphyrin complex crystal structures. in RSC Advances
Royal Soc Chemistry, Cambridge., 2(33), 12963-12972.
https://doi.org/10.1039/c2ra21937a
Dimitrijević B, Borozan S, Stojanović S. pi-pi and cation-pi interactions in protein-porphyrin complex crystal structures. in RSC Advances. 2012;2(33):12963-12972.
doi:10.1039/c2ra21937a .
Dimitrijević, Blagoje, Borozan, Sunčica, Stojanović, Srđan, "pi-pi and cation-pi interactions in protein-porphyrin complex crystal structures" in RSC Advances, 2, no. 33 (2012):12963-12972,
https://doi.org/10.1039/c2ra21937a . .
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Effects of infection intensity with Strongyloides papillosus and albendazole treatment on development of oxidative/nitrosative stress in sheep

Dimitrijević, Blagoje; Borozan, Sunčica; Katić-Radivojević, Sofija; Stojanović, Srđan

(Elsevier, Amsterdam, 2012)

TY  - JOUR
AU  - Dimitrijević, Blagoje
AU  - Borozan, Sunčica
AU  - Katić-Radivojević, Sofija
AU  - Stojanović, Srđan
PY  - 2012
UR  - https://vet-erinar.vet.bg.ac.rs/handle/123456789/855
AB  - The objective of this study was to estimate and evaluate oxidative/nitrosative stress parameters in sheep infected with Strongyloides papillosus and after antihelminthic treatment with albendazole (ABZ). This parasite, especially during development stages can seriously damage parenchaematous organs during migration within the host. The presence of parasites leads to increased productions of reactive oxygen species (ROS) and reactive nitrogen species (RNS). It is also well known that certain drugs can be very harmful for the delicate oxidant-antioxidant equilibrium, provoking oxidative stress during their biotransformation. ABZ is a broad spectrum antihelminthic drug, frequently used in veterinary medicine for therapy of parasitic infections. The current research was performed on female Wurttemberg sheep (n = 48). The distribution of parasites in sheep was evaluated using the native smear coprological technique, by sedimentation and flotation methods, revealing the presence of S. papillosus. The degree of infection intensity per sheep was quantitatively established by the method of McMaster, the animals having been divided into three groups according to the intensity of infection; mild, moderate and high. The control group consisted of sheep negative to the parasites. After determining the type of parasite infection, the sheep were treated with ABZ, per orally, in single doses of 5 mg/kg per body weight. Sampling of feces for parasitological and blood for biochemical assaying was performed on the 0 and 21st day after treatment with ABZ. The oxidative stress parameters were measured for catalase activity (CAT), the red cell membrane damage by level of malondialdehyde (MDA), while carbonyl and thiol plasma protein group concentrations were used as indicators of the degree of protein oxidative modification. The activity of Cu,Zn-superoxide dismutase (SOD) and relative distribution of lactate dehydrogenase (LDH1-LDH5) activity were determined electrophoretically. The distribution of LDH isoenzymes in sheep moderately and highly infected with S. papillosus revealed that the parasite induced damage to the myocardial (LDH2), lung (LDH3) and liver cells (LDH5) in infected animals, while ABZ treatment only damaged liver cells (LDH5). The MDA concentration revealed that lipid peroxidation increased both in the presence of parasites and the antihelminthic formulation tested (p < 0.001) when compared to the control sheep, while the increase of carbonyl concentration (p < 0.001), as well as the observed decrease of thiol concentration (p < 0.001) indicated significant oxidative damage of plasma proteins in experimental sheep, when compared to the control animals. Our results indicate that S. papillosus induces oxidative/nitrosative stress in sheep. The antihelminthic treatment with ABZ further promotes the disbalance of oxidative-antioxidative equilibrium in all tested sheep.
PB  - Elsevier, Amsterdam
T2  - Veterinary Parasitology
T1  - Effects of infection intensity with Strongyloides papillosus and albendazole treatment on development of oxidative/nitrosative stress in sheep
VL  - 186
IS  - 3-4
SP  - 364
EP  - 375
DO  - 10.1016/j.vetpar.2011.11.017
ER  - 
@article{
author = "Dimitrijević, Blagoje and Borozan, Sunčica and Katić-Radivojević, Sofija and Stojanović, Srđan",
year = "2012",
abstract = "The objective of this study was to estimate and evaluate oxidative/nitrosative stress parameters in sheep infected with Strongyloides papillosus and after antihelminthic treatment with albendazole (ABZ). This parasite, especially during development stages can seriously damage parenchaematous organs during migration within the host. The presence of parasites leads to increased productions of reactive oxygen species (ROS) and reactive nitrogen species (RNS). It is also well known that certain drugs can be very harmful for the delicate oxidant-antioxidant equilibrium, provoking oxidative stress during their biotransformation. ABZ is a broad spectrum antihelminthic drug, frequently used in veterinary medicine for therapy of parasitic infections. The current research was performed on female Wurttemberg sheep (n = 48). The distribution of parasites in sheep was evaluated using the native smear coprological technique, by sedimentation and flotation methods, revealing the presence of S. papillosus. The degree of infection intensity per sheep was quantitatively established by the method of McMaster, the animals having been divided into three groups according to the intensity of infection; mild, moderate and high. The control group consisted of sheep negative to the parasites. After determining the type of parasite infection, the sheep were treated with ABZ, per orally, in single doses of 5 mg/kg per body weight. Sampling of feces for parasitological and blood for biochemical assaying was performed on the 0 and 21st day after treatment with ABZ. The oxidative stress parameters were measured for catalase activity (CAT), the red cell membrane damage by level of malondialdehyde (MDA), while carbonyl and thiol plasma protein group concentrations were used as indicators of the degree of protein oxidative modification. The activity of Cu,Zn-superoxide dismutase (SOD) and relative distribution of lactate dehydrogenase (LDH1-LDH5) activity were determined electrophoretically. The distribution of LDH isoenzymes in sheep moderately and highly infected with S. papillosus revealed that the parasite induced damage to the myocardial (LDH2), lung (LDH3) and liver cells (LDH5) in infected animals, while ABZ treatment only damaged liver cells (LDH5). The MDA concentration revealed that lipid peroxidation increased both in the presence of parasites and the antihelminthic formulation tested (p < 0.001) when compared to the control sheep, while the increase of carbonyl concentration (p < 0.001), as well as the observed decrease of thiol concentration (p < 0.001) indicated significant oxidative damage of plasma proteins in experimental sheep, when compared to the control animals. Our results indicate that S. papillosus induces oxidative/nitrosative stress in sheep. The antihelminthic treatment with ABZ further promotes the disbalance of oxidative-antioxidative equilibrium in all tested sheep.",
publisher = "Elsevier, Amsterdam",
journal = "Veterinary Parasitology",
title = "Effects of infection intensity with Strongyloides papillosus and albendazole treatment on development of oxidative/nitrosative stress in sheep",
volume = "186",
number = "3-4",
pages = "364-375",
doi = "10.1016/j.vetpar.2011.11.017"
}
Dimitrijević, B., Borozan, S., Katić-Radivojević, S.,& Stojanović, S.. (2012). Effects of infection intensity with Strongyloides papillosus and albendazole treatment on development of oxidative/nitrosative stress in sheep. in Veterinary Parasitology
Elsevier, Amsterdam., 186(3-4), 364-375.
https://doi.org/10.1016/j.vetpar.2011.11.017
Dimitrijević B, Borozan S, Katić-Radivojević S, Stojanović S. Effects of infection intensity with Strongyloides papillosus and albendazole treatment on development of oxidative/nitrosative stress in sheep. in Veterinary Parasitology. 2012;186(3-4):364-375.
doi:10.1016/j.vetpar.2011.11.017 .
Dimitrijević, Blagoje, Borozan, Sunčica, Katić-Radivojević, Sofija, Stojanović, Srđan, "Effects of infection intensity with Strongyloides papillosus and albendazole treatment on development of oxidative/nitrosative stress in sheep" in Veterinary Parasitology, 186, no. 3-4 (2012):364-375,
https://doi.org/10.1016/j.vetpar.2011.11.017 . .
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