TY  - JOUR
AU  - Nikolić-Kokić, Aleksandra
AU  - Stević, Zorica D
AU  - Stojanović, Srđan D.
AU  - Blagojević, Duško
AU  - Jones, David R
AU  - Pavlović, Sanja
AU  - Niketić, Vesna P
AU  - Apostolski, Slobodan A
AU  - Spasić, Mihajlo
PY  - 2005
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/1689
AB  - Recent findings indicate that nitric oxide (NOcenter dot) over-production might be an important factor in the pathogenesis of sporadic amyotrophic lateral sclerosis (SALS). We measured significantly higher concentrations of uric acid and thiol group-containing molecules (R-SH groups) in the cerebrospinal fluid (CSF) from SALS patients compared to controls. The above factors, together with a slightly increased free iron concentration found in the CSF, favour conditions necessary for the formation of the dinitrosyl iron complex, capable of NOcenter dot bio-transformation. Thus, we performed ex vivo saturation of CSF ( from both SALS patients and controls) with NOcenter dot. A decrease in the level of R - SH was found. This was more pronounced in the CSF from SALS patients. In the CSF from SALS patients the production of nitrite and hydroxylamine was greater than that observed in the CSF from controls. Moreover, we also found increased Cu, Zn-SOD activity in the CSF from SALS patients ( when compared to control subjects) but no activity corresponding to Mn-SOD in any CSF samples. As Cu, Zn-SOD can react with nitroxyl forming NOcenter dot, the conditions for a closed, but continuous, loop of NOcenter dot biotransformation are present in the CSF of ALS patients.
T2  - Redox Report
T1  - Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients
IS  - 5
VL  - 10
EP  - 270
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_1689
ER  - 

@article{
author = "Nikolić-Kokić, Aleksandra and Stević, Zorica D and Stojanović, Srđan D. and Blagojević, Duško and Jones, David R and Pavlović, Sanja and Niketić, Vesna P and Apostolski, Slobodan A and Spasić, Mihajlo",
year = "2005",
abstract = "Recent findings indicate that nitric oxide (NOcenter dot) over-production might be an important factor in the pathogenesis of sporadic amyotrophic lateral sclerosis (SALS). We measured significantly higher concentrations of uric acid and thiol group-containing molecules (R-SH groups) in the cerebrospinal fluid (CSF) from SALS patients compared to controls. The above factors, together with a slightly increased free iron concentration found in the CSF, favour conditions necessary for the formation of the dinitrosyl iron complex, capable of NOcenter dot bio-transformation. Thus, we performed ex vivo saturation of CSF ( from both SALS patients and controls) with NOcenter dot. A decrease in the level of R - SH was found. This was more pronounced in the CSF from SALS patients. In the CSF from SALS patients the production of nitrite and hydroxylamine was greater than that observed in the CSF from controls. Moreover, we also found increased Cu, Zn-SOD activity in the CSF from SALS patients ( when compared to control subjects) but no activity corresponding to Mn-SOD in any CSF samples. As Cu, Zn-SOD can react with nitroxyl forming NOcenter dot, the conditions for a closed, but continuous, loop of NOcenter dot biotransformation are present in the CSF of ALS patients.",
journal = "Redox Report",
title = "Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients",
number = "5",
volume = "10",
pages = "270",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_1689"
}

Nikolić-Kokić, A., Stević, Z. D., Stojanović, S. D., Blagojević, D., Jones, D. R., Pavlović, S., Niketić, V. P., Apostolski, S. A.,& Spasić, M.. (2005). Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients. in Redox Report, 10(5).
https://hdl.handle.net/21.15107/rcub_ibiss_1689

Nikolić-Kokić A, Stević ZD, Stojanović SD, Blagojević D, Jones DR, Pavlović S, Niketić VP, Apostolski SA, Spasić M. Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients. in Redox Report. 2005;10(5):null-270.
https://hdl.handle.net/21.15107/rcub_ibiss_1689 .

Nikolić-Kokić, Aleksandra, Stević, Zorica D, Stojanović, Srđan D., Blagojević, Duško, Jones, David R, Pavlović, Sanja, Niketić, Vesna P, Apostolski, Slobodan A, Spasić, Mihajlo, "Biotransformation of nitric oxide in the cerebrospinal fluid of amyotrophic lateral sclerosis patients" in Redox Report, 10, no. 5 (2005),
https://hdl.handle.net/21.15107/rcub_ibiss_1689 .

TY  - JOUR
AU  - Stojanović, Srđan D.
AU  - Spasić, Mihajlo
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Raičević, Smiljana
AU  - Niketić, Vesna
PY  - 2005
PY  - 2005
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/550
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 in 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 in 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.
T2  - Journal of the Serbian Chemical Society
T1  - Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina
T1  - Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration
IS  - 4
VL  - 70
SP  - 601
EP  - 608
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_550
ER  - 

@article{
author = "Stojanović, Srđan D. and Spasić, Mihajlo and Stanić, Dragana and Nikolić, Milan and Raičević, Smiljana and Niketić, Vesna",
year = "2005, 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 in 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 in 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.",
journal = "Journal of the Serbian Chemical Society",
title = "Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina, Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration",
number = "4",
volume = "70",
pages = "601-608",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_550"
}

Stojanović, S. D., Spasić, M., Stanić, D., Nikolić, M., Raičević, S.,& Niketić, V.. (2005). Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina. in Journal of the Serbian Chemical Society, 70(4), 601-608.
https://hdl.handle.net/21.15107/rcub_ibiss_550

Stojanović SD, Spasić M, Stanić D, Nikolić M, Raičević S, Niketić V. Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina. in Journal of the Serbian Chemical Society. 2005;70(4):601-608.
https://hdl.handle.net/21.15107/rcub_ibiss_550 .

Stojanović, Srđan D., Spasić, Mihajlo, Stanić, Dragana, Nikolić, Milan, Raičević, Smiljana, Niketić, Vesna, "Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina" in Journal of the Serbian Chemical Society, 70, no. 4 (2005):601-608,
https://hdl.handle.net/21.15107/rcub_ibiss_550 .