Spasić, Mihajlo B.

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orcid::0000-0001-9046-0139
  • Spasić, Mihajlo B. (8)
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Author's Bibliography

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.; Spasić, Mihajlo B.; 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  - Spasić, Mihajlo B.
AU  - Miljević, Čedo
PY  - 2016
UR  - https://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
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 Spasić, Mihajlo B. 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"
}
Nikolić-Kokić, A., Mijušković, A., Tatalović, N., Nestorov, J., Miler, M., Oreščanin-Dušić, Z., Nikolić, M., Milošević, V., Blagojević, D. P., Spasić, M. B.,& 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
Nikolić-Kokić A, Mijušković A, Tatalović N, Nestorov J, Miler M, Oreščanin-Dušić Z, Nikolić M, Milošević V, Blagojević DP, Spasić MB, 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 .
Nikolić-Kokić, Aleksandra, Mijušković, Ana, Tatalović, Nikola, Nestorov, Jelena, Miler, Marko, Oreščanin-Dušić, Zorana, Nikolić, Milan, Milošević, Verica, Blagojević, Duško P., Spasić, Mihajlo B., 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 . .
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Effect of atypical antipsychotics on antioxidant enzyme activities in human erythrocytes (in vitro study)

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

(Wiley, Hoboken, 2013)

TY  - JOUR
AU  - Miljević, Čedo
AU  - Nikolić-Kokić, Aleksandra
AU  - Nikolić, Milan
AU  - Niketić, Vesna
AU  - Spasić, Mihajlo B.
AU  - Lecic-Tosevski, Dusica
AU  - Blagojević, Duško P.
PY  - 2013
UR  - https://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
ER  - 
@article{
author = "Miljević, Čedo and Nikolić-Kokić, Aleksandra and Nikolić, Milan and Niketić, Vesna and Spasić, 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"
}
Miljević, Č., Nikolić-Kokić, A., Nikolić, M., Niketić, V., Spasić, 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
Miljević Č, Nikolić-Kokić A, Nikolić M, Niketić V, Spasić 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 .
Miljević, Čedo, Nikolić-Kokić, Aleksandra, Nikolić, Milan, Niketić, Vesna, Spasić, 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 . .
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The reaction of methionine with hydroxyl radical: reactive intermediates and methanethiol production

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

(Springer Wien, Wien, 2012)

TY  - JOUR
AU  - Spasojević, Ivan
AU  - Pristov-Bogdanović, Jelena
AU  - Vujisić, Ljubodrag V.
AU  - Spasić, Mihajlo B.
PY  - 2012
UR  - https://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
ER  - 
@article{
author = "Spasojević, Ivan and Pristov-Bogdanović, Jelena and Vujisić, Ljubodrag V. and Spasić, Mihajlo B.",
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"
}
Spasojević, I., Pristov-Bogdanović, J., Vujisić, L. V.,& Spasić, M. B.. (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
Spasojević I, Pristov-Bogdanović J, Vujisić LV, Spasić MB. 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 .
Spasojević, Ivan, Pristov-Bogdanović, Jelena, Vujisić, Ljubodrag V., Spasić, Mihajlo B., "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 . .
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Lipid status, anti-oxidant enzyme defence and haemoglobin content in the blood of long-term clozapine-treated schizophrenic patients

Mijevic, Cedo; Nikolić, Milan; Nikolić-Kokić, Aleksandra; Jones, David R.; Niketić, Vesna; Lecic-Tosevski, Dusica; Spasić, Mihajlo B.

(Pergamon-Elsevier Science Ltd, Oxford, 2010)

TY  - JOUR
AU  - Mijevic, Cedo
AU  - Nikolić, Milan
AU  - Nikolić-Kokić, Aleksandra
AU  - Jones, David R.
AU  - Niketić, Vesna
AU  - Lecic-Tosevski, Dusica
AU  - Spasić, Mihajlo B.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1059
AB  - Objective: Despite clozapine's unique effectiveness in patients with schizophrenia, a number of adverse effects have been recognised including abnormalities in lipid and glucose metabolisms. A high clozapine level in red blood cells (RBCs) and disturbed anti-oxidant enzyme activities in blood from schizophrenic patients prompted us to investigate lipid status and anti-oxidant enzyme defence in the blood of chronic schizophrenic patients on long-term clozapine therapy. Methods: Plasma lipids, RBC anti-oxidant enzyme activities and haemoglobin (Hb) content were measured using established procedures in a group of eighteen chronically-medicated (average 630 days of therapy) schizophrenic patients receiving clozapine (average dose of 295 mg/day) and data were compared with those from a group of eighteen well-matched normal controls. Results: Significantly higher levels of plasma triglycerides (by 47%, p lt 0.01) and total cholesterol and phospholipids (by 8% and 11%, respectively p lt 0.05) in patients were found. CuZn-superoxide dismutase (SOD1) activity was markedly higher (by 35%, p lt 0.001) while selenium-dependent glutathione peroxidase (GSH-Px1) activity was markedly lower (by 41%, p lt 0.001) in patients. In addition, metHb and HbA1c levels in patients were significantly higher (by 58% and 25%. respectively p lt 0.001). SOD1 activity was negatively correlated (p lt 0.001) to GSH-Px1 activity in patients. Conclusions:The findings support the view that ongoing oxidative stress may be a mechanism by which clozapine induces some adverse effects that increase the risk of diabetes and metabolic syndrome. If valid, this would indicate that in parallel with long-term clozapine treatment, schizophrenic patients could be encouraged to make some lifestyle changes to limit the detrimental effects of the medication. (C) 2009 Elsevier Inc. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Progress in Neuro-psychopharmacology and Biological Psychiatry
T1  - Lipid status, anti-oxidant enzyme defence and haemoglobin content in the blood of long-term clozapine-treated schizophrenic patients
VL  - 34
IS  - 2
SP  - 303
EP  - 307
DO  - 10.1016/j.pnpbp.2009.11.024
ER  - 
@article{
author = "Mijevic, Cedo and Nikolić, Milan and Nikolić-Kokić, Aleksandra and Jones, David R. and Niketić, Vesna and Lecic-Tosevski, Dusica and Spasić, Mihajlo B.",
year = "2010",
abstract = "Objective: Despite clozapine's unique effectiveness in patients with schizophrenia, a number of adverse effects have been recognised including abnormalities in lipid and glucose metabolisms. A high clozapine level in red blood cells (RBCs) and disturbed anti-oxidant enzyme activities in blood from schizophrenic patients prompted us to investigate lipid status and anti-oxidant enzyme defence in the blood of chronic schizophrenic patients on long-term clozapine therapy. Methods: Plasma lipids, RBC anti-oxidant enzyme activities and haemoglobin (Hb) content were measured using established procedures in a group of eighteen chronically-medicated (average 630 days of therapy) schizophrenic patients receiving clozapine (average dose of 295 mg/day) and data were compared with those from a group of eighteen well-matched normal controls. Results: Significantly higher levels of plasma triglycerides (by 47%, p lt 0.01) and total cholesterol and phospholipids (by 8% and 11%, respectively p lt 0.05) in patients were found. CuZn-superoxide dismutase (SOD1) activity was markedly higher (by 35%, p lt 0.001) while selenium-dependent glutathione peroxidase (GSH-Px1) activity was markedly lower (by 41%, p lt 0.001) in patients. In addition, metHb and HbA1c levels in patients were significantly higher (by 58% and 25%. respectively p lt 0.001). SOD1 activity was negatively correlated (p lt 0.001) to GSH-Px1 activity in patients. Conclusions:The findings support the view that ongoing oxidative stress may be a mechanism by which clozapine induces some adverse effects that increase the risk of diabetes and metabolic syndrome. If valid, this would indicate that in parallel with long-term clozapine treatment, schizophrenic patients could be encouraged to make some lifestyle changes to limit the detrimental effects of the medication. (C) 2009 Elsevier Inc. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Progress in Neuro-psychopharmacology and Biological Psychiatry",
title = "Lipid status, anti-oxidant enzyme defence and haemoglobin content in the blood of long-term clozapine-treated schizophrenic patients",
volume = "34",
number = "2",
pages = "303-307",
doi = "10.1016/j.pnpbp.2009.11.024"
}
Mijevic, C., Nikolić, M., Nikolić-Kokić, A., Jones, D. R., Niketić, V., Lecic-Tosevski, D.,& Spasić, M. B.. (2010). Lipid status, anti-oxidant enzyme defence and haemoglobin content in the blood of long-term clozapine-treated schizophrenic patients. in Progress in Neuro-psychopharmacology and Biological Psychiatry
Pergamon-Elsevier Science Ltd, Oxford., 34(2), 303-307.
https://doi.org/10.1016/j.pnpbp.2009.11.024
Mijevic C, Nikolić M, Nikolić-Kokić A, Jones DR, Niketić V, Lecic-Tosevski D, Spasić MB. Lipid status, anti-oxidant enzyme defence and haemoglobin content in the blood of long-term clozapine-treated schizophrenic patients. in Progress in Neuro-psychopharmacology and Biological Psychiatry. 2010;34(2):303-307.
doi:10.1016/j.pnpbp.2009.11.024 .
Mijevic, Cedo, Nikolić, Milan, Nikolić-Kokić, Aleksandra, Jones, David R., Niketić, Vesna, Lecic-Tosevski, Dusica, Spasić, Mihajlo B., "Lipid status, anti-oxidant enzyme defence and haemoglobin content in the blood of long-term clozapine-treated schizophrenic patients" in Progress in Neuro-psychopharmacology and Biological Psychiatry, 34, no. 2 (2010):303-307,
https://doi.org/10.1016/j.pnpbp.2009.11.024 . .
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Does cholesterol bound to haemoglobin affect the anti-oxidant enzyme defence system in human erythrocytes?

Nikolić, Milan; Nikolić-Kokić, Aleksandra; Stanić, Dragana; Blagojević, Duško P.; Vranić, Danijela; Jones, David R.; Niketić, Vesna; Spasić, Mihajlo B.

(Serbian Chemical Soc, Belgrade, 2007)

TY  - JOUR
AU  - Nikolić, Milan
AU  - Nikolić-Kokić, Aleksandra
AU  - Stanić, Dragana
AU  - Blagojević, Duško P.
AU  - Vranić, Danijela
AU  - Jones, David R.
AU  - Niketić, Vesna
AU  - Spasić, Mihajlo B.
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/837
AB  - In a previous study, it was shown that the lipid fraction, which is occasionally observed in red blood cell hemolysates, represents cholesterol (Ch) associated with phospholipid firmly bound to haemoglobin (termed Hb-Ch). The current study was conducted to investigate whether Hb-Ch could affect the primary anti-oxidant enzyme defence system in human erythrocytes. Sixty healthy volunteers were used for the current study. Group 1 consisted of 28 subjects without or with a low level of Hb-Ch. Group 2 comprised 32 subjects with a considerably higher level of Hb-Ch. The activities of erythrocyte superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase, as well as the content of methaemoglobin (metHb) were measured in both groups. The results indicated that the amount of Hb-Ch neither influenced the activities of the erythrocyte anti-oxidant enzymes nor altered the level of metHb. However, a higher amount of Hb-Ch changed the correlations in the part of the anti-oxidant defence system relating to glutathione, suggesting increased peroxidative pressure from plasma lipids. Group 2 also had significantly increased concentrations of total plasma Ch and triglycerides. Together, these facts are strong indications that the anti-oxidant defence system in human erythrocytes finely retunes its composition according to plasma oxidative demands.
AB  - U prethodnom radu pokazano je da lipidna frakcija koja se javlja u hemolizatu zdravih ljudi predstavlja holesterol (asosovan sa fosfolipidima) čvrsto vezan za hemoglobin (Hb-Ch). U ovom radu ispitivan je uticaj Hb-Ch na anti-oksidativni enzimski sistem u humanim eritrocitima. Određena je aktivnost superoksid-dizmutaze, katalaze, glutation-peroksidaze i glutation-reduktaze, kao i sadržaj met-hemoglobina (metHb) u eritrocitima 60 ljudi, podeljenih u dve grupe na osnovu količine Hb-Ch. Rezultati pokazuju da količina prisutnog Hb-Ch ne menja aktivnost merenih enzima, niti nivo metHb. Međutim, u grupi ispitanika sa povećanim sadržajem Hb-Ch zapažene su korelativne promene u delu anti-oksidativnog enzimskog sistema povezanog sa glutationom. U istoj grupi detektovane su i veće koncentracije ukupnog holesterola i triglicerida u plazmi, što zajedno ukazuje na povećani peroksidativni pritisak iz plazme. Ovi rezultati ukazuju da odbrambeni anti-oksidativni enzimski sistem u humanim eritrocitima prilagođava svoju organizaciju prema zahtevima iz svog okruženja. .
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Does cholesterol bound to haemoglobin affect the anti-oxidant enzyme defence system in human erythrocytes?
T1  - Da li holesterol vezan za hemoglobin utiče na anti-oksidativni enzimski sistem u humanim eritrocitima?
VL  - 72
IS  - 4
SP  - 339
EP  - 345
DO  - 10.2298/JSC0704339N
ER  - 
@article{
author = "Nikolić, Milan and Nikolić-Kokić, Aleksandra and Stanić, Dragana and Blagojević, Duško P. and Vranić, Danijela and Jones, David R. and Niketić, Vesna and Spasić, Mihajlo B.",
year = "2007",
abstract = "In a previous study, it was shown that the lipid fraction, which is occasionally observed in red blood cell hemolysates, represents cholesterol (Ch) associated with phospholipid firmly bound to haemoglobin (termed Hb-Ch). The current study was conducted to investigate whether Hb-Ch could affect the primary anti-oxidant enzyme defence system in human erythrocytes. Sixty healthy volunteers were used for the current study. Group 1 consisted of 28 subjects without or with a low level of Hb-Ch. Group 2 comprised 32 subjects with a considerably higher level of Hb-Ch. The activities of erythrocyte superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase, as well as the content of methaemoglobin (metHb) were measured in both groups. The results indicated that the amount of Hb-Ch neither influenced the activities of the erythrocyte anti-oxidant enzymes nor altered the level of metHb. However, a higher amount of Hb-Ch changed the correlations in the part of the anti-oxidant defence system relating to glutathione, suggesting increased peroxidative pressure from plasma lipids. Group 2 also had significantly increased concentrations of total plasma Ch and triglycerides. Together, these facts are strong indications that the anti-oxidant defence system in human erythrocytes finely retunes its composition according to plasma oxidative demands., U prethodnom radu pokazano je da lipidna frakcija koja se javlja u hemolizatu zdravih ljudi predstavlja holesterol (asosovan sa fosfolipidima) čvrsto vezan za hemoglobin (Hb-Ch). U ovom radu ispitivan je uticaj Hb-Ch na anti-oksidativni enzimski sistem u humanim eritrocitima. Određena je aktivnost superoksid-dizmutaze, katalaze, glutation-peroksidaze i glutation-reduktaze, kao i sadržaj met-hemoglobina (metHb) u eritrocitima 60 ljudi, podeljenih u dve grupe na osnovu količine Hb-Ch. Rezultati pokazuju da količina prisutnog Hb-Ch ne menja aktivnost merenih enzima, niti nivo metHb. Međutim, u grupi ispitanika sa povećanim sadržajem Hb-Ch zapažene su korelativne promene u delu anti-oksidativnog enzimskog sistema povezanog sa glutationom. U istoj grupi detektovane su i veće koncentracije ukupnog holesterola i triglicerida u plazmi, što zajedno ukazuje na povećani peroksidativni pritisak iz plazme. Ovi rezultati ukazuju da odbrambeni anti-oksidativni enzimski sistem u humanim eritrocitima prilagođava svoju organizaciju prema zahtevima iz svog okruženja. .",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Does cholesterol bound to haemoglobin affect the anti-oxidant enzyme defence system in human erythrocytes?, Da li holesterol vezan za hemoglobin utiče na anti-oksidativni enzimski sistem u humanim eritrocitima?",
volume = "72",
number = "4",
pages = "339-345",
doi = "10.2298/JSC0704339N"
}
Nikolić, M., Nikolić-Kokić, A., Stanić, D., Blagojević, D. P., Vranić, D., Jones, D. R., Niketić, V.,& Spasić, M. B.. (2007). Does cholesterol bound to haemoglobin affect the anti-oxidant enzyme defence system in human erythrocytes?. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 72(4), 339-345.
https://doi.org/10.2298/JSC0704339N
Nikolić M, Nikolić-Kokić A, Stanić D, Blagojević DP, Vranić D, Jones DR, Niketić V, Spasić MB. Does cholesterol bound to haemoglobin affect the anti-oxidant enzyme defence system in human erythrocytes?. in Journal of the Serbian Chemical Society. 2007;72(4):339-345.
doi:10.2298/JSC0704339N .
Nikolić, Milan, Nikolić-Kokić, Aleksandra, Stanić, Dragana, Blagojević, Duško P., Vranić, Danijela, Jones, David R., Niketić, Vesna, Spasić, Mihajlo B., "Does cholesterol bound to haemoglobin affect the anti-oxidant enzyme defence system in human erythrocytes?" in Journal of the Serbian Chemical Society, 72, no. 4 (2007):339-345,
https://doi.org/10.2298/JSC0704339N . .
3
3
3
3

Could cholesterol bound to haemoglobin be a missing link for the occasional inverse relationship between superoxide dismutase and glutathione peroxidase activities?

Nikolić, Milan; Vranić, Danijela; Spiric, Aurelija; Batas, Valentina; Nikolić-Kokić, Aleksandra; Radetic, Petar; Turubatovic, Lazar; Blagojević, Duško P.; Jones, David R.; Niketić, Vesna; Spasić, Mihajlo B.

(Academic Press Inc Elsevier Science, San Diego, 2006)

TY  - JOUR
AU  - Nikolić, Milan
AU  - Vranić, Danijela
AU  - Spiric, Aurelija
AU  - Batas, Valentina
AU  - Nikolić-Kokić, Aleksandra
AU  - Radetic, Petar
AU  - Turubatovic, Lazar
AU  - Blagojević, Duško P.
AU  - Jones, David R.
AU  - Niketić, Vesna
AU  - Spasić, Mihajlo B.
PY  - 2006
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/797
AB  - The concept of an anti-oxidant defence system as a means to prevent oxidative cell damage implies balanced activities of anti-oxidant defence enzymes. As well as positive correlations between anti-oxidant enzyme activities in human erythrocytes, it has been observed that sometimes when glutathione peroxidase activity is increased, CuZn-superoxide dismutase activity is decreased. In our current study we have examined the plasma lipid profile and the anti-oxidant defence enzymes in erythrocytes from humans, pigs, and bulls. We found that a negative correlation existed between CuZn-superoxide dismutase and glutathione peroxidase activities in human erythrocytes when the concentrations of both plasma triglycerides and total cholesterol were high. This correlation was also found in pig erythrocytes, but not in bull erythrocytes. We propose that cholesterol could affect membrane lipid peroxiclation and superoxide generation in erythrocytes via the recently found fraction of cholesterol bound to haemoglobin, termed haemoglobin-cholesterol. (c) 2006 Elsevier Inc. All rights reserved.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Biochemical and Biophysical Research Communications
T1  - Could cholesterol bound to haemoglobin be a missing link for the occasional inverse relationship between superoxide dismutase and glutathione peroxidase activities?
VL  - 348
IS  - 1
SP  - 265
EP  - 270
DO  - 10.1016/j.bbrc.2006.06.199
ER  - 
@article{
author = "Nikolić, Milan and Vranić, Danijela and Spiric, Aurelija and Batas, Valentina and Nikolić-Kokić, Aleksandra and Radetic, Petar and Turubatovic, Lazar and Blagojević, Duško P. and Jones, David R. and Niketić, Vesna and Spasić, Mihajlo B.",
year = "2006",
abstract = "The concept of an anti-oxidant defence system as a means to prevent oxidative cell damage implies balanced activities of anti-oxidant defence enzymes. As well as positive correlations between anti-oxidant enzyme activities in human erythrocytes, it has been observed that sometimes when glutathione peroxidase activity is increased, CuZn-superoxide dismutase activity is decreased. In our current study we have examined the plasma lipid profile and the anti-oxidant defence enzymes in erythrocytes from humans, pigs, and bulls. We found that a negative correlation existed between CuZn-superoxide dismutase and glutathione peroxidase activities in human erythrocytes when the concentrations of both plasma triglycerides and total cholesterol were high. This correlation was also found in pig erythrocytes, but not in bull erythrocytes. We propose that cholesterol could affect membrane lipid peroxiclation and superoxide generation in erythrocytes via the recently found fraction of cholesterol bound to haemoglobin, termed haemoglobin-cholesterol. (c) 2006 Elsevier Inc. All rights reserved.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Biochemical and Biophysical Research Communications",
title = "Could cholesterol bound to haemoglobin be a missing link for the occasional inverse relationship between superoxide dismutase and glutathione peroxidase activities?",
volume = "348",
number = "1",
pages = "265-270",
doi = "10.1016/j.bbrc.2006.06.199"
}
Nikolić, M., Vranić, D., Spiric, A., Batas, V., Nikolić-Kokić, A., Radetic, P., Turubatovic, L., Blagojević, D. P., Jones, D. R., Niketić, V.,& Spasić, M. B.. (2006). Could cholesterol bound to haemoglobin be a missing link for the occasional inverse relationship between superoxide dismutase and glutathione peroxidase activities?. in Biochemical and Biophysical Research Communications
Academic Press Inc Elsevier Science, San Diego., 348(1), 265-270.
https://doi.org/10.1016/j.bbrc.2006.06.199
Nikolić M, Vranić D, Spiric A, Batas V, Nikolić-Kokić A, Radetic P, Turubatovic L, Blagojević DP, Jones DR, Niketić V, Spasić MB. Could cholesterol bound to haemoglobin be a missing link for the occasional inverse relationship between superoxide dismutase and glutathione peroxidase activities?. in Biochemical and Biophysical Research Communications. 2006;348(1):265-270.
doi:10.1016/j.bbrc.2006.06.199 .
Nikolić, Milan, Vranić, Danijela, Spiric, Aurelija, Batas, Valentina, Nikolić-Kokić, Aleksandra, Radetic, Petar, Turubatovic, Lazar, Blagojević, Duško P., Jones, David R., Niketić, Vesna, Spasić, Mihajlo B., "Could cholesterol bound to haemoglobin be a missing link for the occasional inverse relationship between superoxide dismutase and glutathione peroxidase activities?" in Biochemical and Biophysical Research Communications, 348, no. 1 (2006):265-270,
https://doi.org/10.1016/j.bbrc.2006.06.199 . .
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4

Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration

Stojanović, Srđan Đ.; Stanić, Dragana; Nikolić, Milan; Raicevic, S; Spasić, Mihajlo B.; Niketic, V

(Serbian Chemical Soc, Belgrade, 2005)

TY  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Raicevic, S
AU  - Spasić, Mihajlo B.
AU  - Niketic, V
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/713
AB  - The peroxynitrite-induced nitration of manganese superoxide dismutase (MnSOD) tyrosine residue, which causes enzyme inactivation, is well established, This led to suggestions that MnSOD nitration and inactivation in vivo, detected in various diseases associated with oxidative stress and overproduction of nitric monoxide (NO), conditions which favor peroxynitrite formation, is also caused by peroxynitrite. However, our previous ill vitro study demonstrated that exposure of MnSOD to NO led to NO conversion into nitrosonium (NO+) and nitroxyl (NO-) species, which caused enzyme modifications and inactivation. Here it is reported that MnSOD is tyrosine nitrated upon exposure to NO, as well as that MnSOD nitration contributes to inactivation of the enzyme. Collectively, these observations provide a compelling argument supporting the generation of nitrating species in MnSOD exposed to NO and shed a new light on MnSOD tyrosine nitration and inactivation ill vivo. This may represent a novel mechanism by which MnSOD protects cell from deleterious effects associated with overproduction of NO. However, extensive MnSOD modification and inactivation associated with prolonged exposure to NO will amplify the toxic effects caused by increased cell superoxide and NO levels.
AB  - Dobro je poznato da peroksinitrit izaziva nitrovanje ostataka tirozina u mangan-superoksid- dismutazi (MnSOD) što dovodi do inaktivacije enzima. Pokazano je da nitrovanje i inaktivacija MnSOD-a nastaje u raznim bolestima za koje je karakteristič an oksidativni stres i povećana produkcija azot-monoksida (NO). Pošto se pri ovim uslovima očekuje nastajanje peroksinitrita predloženo je da peroksinitrit izaziva nitrovanje i inaktivaciju MnSOD in vivo. U našem prethodnom radu pokazali smo da MnSOD katalizuje transformaciju NO u nitrozonijum (NO+) i nitroksil (NO–) reaktivne vrste, te identifikovali neke od modifikacija molekula enzima koje pri tome nastaju izazivajući njegovu inaktivaciju. U ovom radu je pokazano da pri izlaganju MnSOD azot-monoksidu dolazi i do nitrovanja ostatka tirozina u molekulu enzima, što doprinosi njegovoj inaktivaciji. Ovi rezultati ukazuju da pri interakciji MnSOD sa NO dolazi do nastajanja nitrujućih vrsta, što baca novo svetlo na proces nitrovanja ostataka tirozina i inaktivaciju MnSOD in vivo. Ovo može da predstavlja novi mehanizam kojim MnSOD štiti ćeliju odštetnih efekata izazvanih hiperprodukcijom azot-monoksida. Međutim ekstenzivne modifikacije i inaktivacija MnSOD do kojih dolazi pri produženom izlaganju enzima NO, uvećaće toksične efekte izazvane povećanim koncentracijama superoksida i NO u ćeliji.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration
T1  - Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina
VL  - 70
IS  - 4
SP  - 601
EP  - 608
DO  - 10.2298/JSC0504601S
ER  - 
@article{
author = "Stojanović, Srđan Đ. and Stanić, Dragana and Nikolić, Milan and Raicevic, S and Spasić, Mihajlo B. and Niketic, V",
year = "2005",
abstract = "The peroxynitrite-induced nitration of manganese superoxide dismutase (MnSOD) tyrosine residue, which causes enzyme inactivation, is well established, This led to suggestions that MnSOD nitration and inactivation in vivo, detected in various diseases associated with oxidative stress and overproduction of nitric monoxide (NO), conditions which favor peroxynitrite formation, is also caused by peroxynitrite. However, our previous ill vitro study demonstrated that exposure of MnSOD to NO led to NO conversion into nitrosonium (NO+) and nitroxyl (NO-) species, which caused enzyme modifications and inactivation. Here it is reported that MnSOD is tyrosine nitrated upon exposure to NO, as well as that MnSOD nitration contributes to inactivation of the enzyme. Collectively, these observations provide a compelling argument supporting the generation of nitrating species in MnSOD exposed to NO and shed a new light on MnSOD tyrosine nitration and inactivation ill vivo. This may represent a novel mechanism by which MnSOD protects cell from deleterious effects associated with overproduction of NO. However, extensive MnSOD modification and inactivation associated with prolonged exposure to NO will amplify the toxic effects caused by increased cell superoxide and NO levels., Dobro je poznato da peroksinitrit izaziva nitrovanje ostataka tirozina u mangan-superoksid- dismutazi (MnSOD) što dovodi do inaktivacije enzima. Pokazano je da nitrovanje i inaktivacija MnSOD-a nastaje u raznim bolestima za koje je karakteristič an oksidativni stres i povećana produkcija azot-monoksida (NO). Pošto se pri ovim uslovima očekuje nastajanje peroksinitrita predloženo je da peroksinitrit izaziva nitrovanje i inaktivaciju MnSOD in vivo. U našem prethodnom radu pokazali smo da MnSOD katalizuje transformaciju NO u nitrozonijum (NO+) i nitroksil (NO–) reaktivne vrste, te identifikovali neke od modifikacija molekula enzima koje pri tome nastaju izazivajući njegovu inaktivaciju. U ovom radu je pokazano da pri izlaganju MnSOD azot-monoksidu dolazi i do nitrovanja ostatka tirozina u molekulu enzima, što doprinosi njegovoj inaktivaciji. Ovi rezultati ukazuju da pri interakciji MnSOD sa NO dolazi do nastajanja nitrujućih vrsta, što baca novo svetlo na proces nitrovanja ostataka tirozina i inaktivaciju MnSOD in vivo. Ovo može da predstavlja novi mehanizam kojim MnSOD štiti ćeliju odštetnih efekata izazvanih hiperprodukcijom azot-monoksida. Međutim ekstenzivne modifikacije i inaktivacija MnSOD do kojih dolazi pri produženom izlaganju enzima NO, uvećaće toksične efekte izazvane povećanim koncentracijama superoksida i NO u ćeliji.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration, Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina",
volume = "70",
number = "4",
pages = "601-608",
doi = "10.2298/JSC0504601S"
}
Stojanović, S. Đ., Stanić, D., Nikolić, M., Raicevic, S., Spasić, M. B.,& Niketic, V.. (2005). Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 70(4), 601-608.
https://doi.org/10.2298/JSC0504601S
Stojanović SĐ, Stanić D, Nikolić M, Raicevic S, Spasić MB, Niketic V. Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration. in Journal of the Serbian Chemical Society. 2005;70(4):601-608.
doi:10.2298/JSC0504601S .
Stojanović, Srđan Đ., Stanić, Dragana, Nikolić, Milan, Raicevic, S, Spasić, Mihajlo B., Niketic, V, "Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration" in Journal of the Serbian Chemical Society, 70, no. 4 (2005):601-608,
https://doi.org/10.2298/JSC0504601S . .
3
3
3
3

Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species

Stojanović, Srđan Đ.; Stanić, Dragana; Nikolić, Milan; Spasić, Mihajlo B.; Niketic, V

(Academic Press Inc Elsevier Science, San Diego, 2004)

TY  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Spasić, Mihajlo B.
AU  - Niketic, V
PY  - 2004
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/675
AB  - The conversion of NO into its congeners, nitrosonium (NO+) and nitroxyl (HNO/NO-) species, has important consequences in NO metabolism. Dinitrosyl iron complex (DNIC) combined with thiol ligands was shown to catalyze the conversion of NO into NO+, resulting in the synthesis of S-nitrosothiols (RSNO) both in vitro and in vivo. The formation mechanism of DNIC was proposed to involve the intermediate release of nitroxyl. Since the detection of hydroxylamine (as the product of a rapid reaction of HNO/NO- with thiols) is taken as the evidence for nitroxyl generation, we examined the formation of hydroxylamine, RSNO, and nitrite (the product of a rapid reaction of NO+ with water) in neutral solutions containing iron ions and thiols exposed to NO under anaerobic conditions. Hydroxylamine was detected in NO treated solutions of iron ions in the presence of cysteine, but not glutathione (GSH). The addition of urate, a major "free" iron-binding agent in humans, to solutions of GSH and iron ions, and the subsequent treatment of these solutions with NO increased the synthesis of GSNO and resulted in the formation of hydroxylamine. This caused a loss of urate and yielded a novel nitrosative/nitration product. GSH attenuated the urate decomposition to such a degree that it could be reflected as the function of GSH:urate. Results described here contribute to the understanding of the role of iron ions in catalyzing the conversion of NO into HNO/NO- and point to the role of uric acid not previously described. (C) 2004 Elsevier Inc. All rights reserved.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Nitric Oxide: Biology and Chemistry
T1  - Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species
VL  - 11
IS  - 3
SP  - 256
EP  - 262
DO  - 10.1016/j.niox.2004.09.007
ER  - 
@article{
author = "Stojanović, Srđan Đ. and Stanić, Dragana and Nikolić, Milan and Spasić, Mihajlo B. and Niketic, V",
year = "2004",
abstract = "The conversion of NO into its congeners, nitrosonium (NO+) and nitroxyl (HNO/NO-) species, has important consequences in NO metabolism. Dinitrosyl iron complex (DNIC) combined with thiol ligands was shown to catalyze the conversion of NO into NO+, resulting in the synthesis of S-nitrosothiols (RSNO) both in vitro and in vivo. The formation mechanism of DNIC was proposed to involve the intermediate release of nitroxyl. Since the detection of hydroxylamine (as the product of a rapid reaction of HNO/NO- with thiols) is taken as the evidence for nitroxyl generation, we examined the formation of hydroxylamine, RSNO, and nitrite (the product of a rapid reaction of NO+ with water) in neutral solutions containing iron ions and thiols exposed to NO under anaerobic conditions. Hydroxylamine was detected in NO treated solutions of iron ions in the presence of cysteine, but not glutathione (GSH). The addition of urate, a major "free" iron-binding agent in humans, to solutions of GSH and iron ions, and the subsequent treatment of these solutions with NO increased the synthesis of GSNO and resulted in the formation of hydroxylamine. This caused a loss of urate and yielded a novel nitrosative/nitration product. GSH attenuated the urate decomposition to such a degree that it could be reflected as the function of GSH:urate. Results described here contribute to the understanding of the role of iron ions in catalyzing the conversion of NO into HNO/NO- and point to the role of uric acid not previously described. (C) 2004 Elsevier Inc. All rights reserved.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Nitric Oxide: Biology and Chemistry",
title = "Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species",
volume = "11",
number = "3",
pages = "256-262",
doi = "10.1016/j.niox.2004.09.007"
}
Stojanović, S. Đ., Stanić, D., Nikolić, M., Spasić, M. B.,& Niketic, V.. (2004). Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species. in Nitric Oxide: Biology and Chemistry
Academic Press Inc Elsevier Science, San Diego., 11(3), 256-262.
https://doi.org/10.1016/j.niox.2004.09.007
Stojanović SĐ, Stanić D, Nikolić M, Spasić MB, Niketic V. Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species. in Nitric Oxide: Biology and Chemistry. 2004;11(3):256-262.
doi:10.1016/j.niox.2004.09.007 .
Stojanović, Srđan Đ., Stanić, Dragana, Nikolić, Milan, Spasić, Mihajlo B., Niketic, V, "Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species" in Nitric Oxide: Biology and Chemistry, 11, no. 3 (2004):256-262,
https://doi.org/10.1016/j.niox.2004.09.007 . .
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