TY  - JOUR
AU  - Nikolić, Milan R.
AU  - Stanić-Vučinić, Dragana
AU  - Baričević, Ivona I.
AU  - Jones, David R.B.
AU  - Nedić, Olgica
AU  - Niketić, Vesna
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4247
AB  - Objective: The interior of red blood cells (RBCs) contains a variable amount of cholesterol and phospholipids bound to haemoglobin (Hb). This current study was devised to determine if this pool of lipids (termed Hb-Ch) was available for exchange with plasma lipoproteins. Design and methods: We studied the in vitro efflux of lipids from human RBCs into fasting plasma in men with either low (control group) or high Hb-Ch (study group). Results: When plasma was incubated with a two-fold excess of autologous RBCs the plasma cholesterol level increased due to a decrease in the level of cholesterol from the RBC membrane (in the control group) and due to a decrease in the level of cholesterol both from the RBC membrane and the Hb-Ch fraction (in the study group). The loss of Hb-Ch-derived phospholipids during lipid efflux was roughly equal to that of Hb-Ch-derived cholesterol. The loss of RBC cholesterol into plasma high-density lipoproteins (HDL) was more pronounced in our study group and correlated with the loss of cholesterol from Hb-Ch. Conclusion: The Hb-Ch adduct significantly contributes to the lipid efflux from RBCs into plasma. The majority of cholesterol released from Hb-Ch appears in the plasma HDL fraction suggesting that Hb-Ch may play a role in reverse cholesterol transport in vivo.
PB  - Elsevier
T2  - Clinical Biochemistry
T1  - Efflux of cholesterol and phospholipids derived from the haemoglobin-lipid adduct in human red blood cells into plasma
VL  - 40
IS  - 5-6
SP  - 305
EP  - 309
DO  - 10.1016/j.clinbiochem.2006.11.005
ER  - 

@article{
author = "Nikolić, Milan R. and Stanić-Vučinić, Dragana and Baričević, Ivona I. and Jones, David R.B. and Nedić, Olgica and Niketić, Vesna",
year = "2007",
abstract = "Objective: The interior of red blood cells (RBCs) contains a variable amount of cholesterol and phospholipids bound to haemoglobin (Hb). This current study was devised to determine if this pool of lipids (termed Hb-Ch) was available for exchange with plasma lipoproteins. Design and methods: We studied the in vitro efflux of lipids from human RBCs into fasting plasma in men with either low (control group) or high Hb-Ch (study group). Results: When plasma was incubated with a two-fold excess of autologous RBCs the plasma cholesterol level increased due to a decrease in the level of cholesterol from the RBC membrane (in the control group) and due to a decrease in the level of cholesterol both from the RBC membrane and the Hb-Ch fraction (in the study group). The loss of Hb-Ch-derived phospholipids during lipid efflux was roughly equal to that of Hb-Ch-derived cholesterol. The loss of RBC cholesterol into plasma high-density lipoproteins (HDL) was more pronounced in our study group and correlated with the loss of cholesterol from Hb-Ch. Conclusion: The Hb-Ch adduct significantly contributes to the lipid efflux from RBCs into plasma. The majority of cholesterol released from Hb-Ch appears in the plasma HDL fraction suggesting that Hb-Ch may play a role in reverse cholesterol transport in vivo.",
publisher = "Elsevier",
journal = "Clinical Biochemistry",
title = "Efflux of cholesterol and phospholipids derived from the haemoglobin-lipid adduct in human red blood cells into plasma",
volume = "40",
number = "5-6",
pages = "305-309",
doi = "10.1016/j.clinbiochem.2006.11.005"
}

Nikolić, M. R., Stanić-Vučinić, D., Baričević, I. I., Jones, D. R.B., Nedić, O.,& Niketić, V.. (2007). Efflux of cholesterol and phospholipids derived from the haemoglobin-lipid adduct in human red blood cells into plasma. in Clinical Biochemistry
Elsevier., 40(5-6), 305-309.
https://doi.org/10.1016/j.clinbiochem.2006.11.005

Nikolić MR, Stanić-Vučinić D, Baričević II, Jones DR, Nedić O, Niketić V. Efflux of cholesterol and phospholipids derived from the haemoglobin-lipid adduct in human red blood cells into plasma. in Clinical Biochemistry. 2007;40(5-6):305-309.
doi:10.1016/j.clinbiochem.2006.11.005 .

Nikolić, Milan R., Stanić-Vučinić, Dragana, Baričević, Ivona I., Jones, David R.B., Nedić, Olgica, Niketić, Vesna, "Efflux of cholesterol and phospholipids derived from the haemoglobin-lipid adduct in human red blood cells into plasma" in Clinical Biochemistry, 40, no. 5-6 (2007):305-309,
https://doi.org/10.1016/j.clinbiochem.2006.11.005 . .

TY  - JOUR
AU  - Filipović, Miloš R.
AU  - Stanić-Vučinić, Dragana
AU  - Raičević, Smiljana
AU  - Spasić, Mihajlo B.
AU  - Niketić, Vesna
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4335
AB  - The present study demonstrates that manganese superoxide dismutase (MnSOD) Escherichia coli, binds nitric oxide (NO) and stimulates its decay under both anaerobic and aerobic conditions. The results indicate that previously observed MnSOD-catalyzed NO disproportionation (dismutation) into nitrosonium (NO + ) and nitroxyl (NO - ) species under anaerobic conditions is also operative in the presence of molecular oxygen. Upon sustained aerobic exposure to NO, MnSOD-derived NO - species initiate the formation of peroxynitrite (ONOO - ) leading to enzyme tyrosine nitration, oxidation and (partial) inactivation. The results suggest that both ONOO - decomposition and ONOO - -dependent tyrosine residue nitration and oxidation are enhanced by metal centre-mediated catalysis. We show that the generation of ONOO - is accompanied by the formation of substantial amounts of H 2 O 2 . MnSOD is a critical mitochondrial antioxidant enzyme, which has been found to undergo tyrosine nitration and inactivation in various pathologies associated with the overproduction of NO. The results of the present study can account for the molecular specificity of MnSOD nitration in vivo. The interaction of NO with MnSOD may represent a novel mechanism by which MnSOD protects the cell from deleterious effects associated with overproduction of NO.
PB  - USA :Taylor & Francis INC
T2  - Free Radical Research
T1  - Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide
VL  - 41
IS  - 1
SP  - 62
EP  - 72
DO  - 10.1080/10715760600944296
ER  - 

@article{
author = "Filipović, Miloš R. and Stanić-Vučinić, Dragana and Raičević, Smiljana and Spasić, Mihajlo B. and Niketić, Vesna",
year = "2007",
abstract = "The present study demonstrates that manganese superoxide dismutase (MnSOD) Escherichia coli, binds nitric oxide (NO) and stimulates its decay under both anaerobic and aerobic conditions. The results indicate that previously observed MnSOD-catalyzed NO disproportionation (dismutation) into nitrosonium (NO + ) and nitroxyl (NO - ) species under anaerobic conditions is also operative in the presence of molecular oxygen. Upon sustained aerobic exposure to NO, MnSOD-derived NO - species initiate the formation of peroxynitrite (ONOO - ) leading to enzyme tyrosine nitration, oxidation and (partial) inactivation. The results suggest that both ONOO - decomposition and ONOO - -dependent tyrosine residue nitration and oxidation are enhanced by metal centre-mediated catalysis. We show that the generation of ONOO - is accompanied by the formation of substantial amounts of H 2 O 2 . MnSOD is a critical mitochondrial antioxidant enzyme, which has been found to undergo tyrosine nitration and inactivation in various pathologies associated with the overproduction of NO. The results of the present study can account for the molecular specificity of MnSOD nitration in vivo. The interaction of NO with MnSOD may represent a novel mechanism by which MnSOD protects the cell from deleterious effects associated with overproduction of NO.",
publisher = "USA :Taylor & Francis INC",
journal = "Free Radical Research",
title = "Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide",
volume = "41",
number = "1",
pages = "62-72",
doi = "10.1080/10715760600944296"
}

Filipović, M. R., Stanić-Vučinić, D., Raičević, S., Spasić, M. B.,& Niketić, V.. (2007). Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide. in Free Radical Research
USA :Taylor & Francis INC., 41(1), 62-72.
https://doi.org/10.1080/10715760600944296

Filipović MR, Stanić-Vučinić D, Raičević S, Spasić MB, Niketić V. Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide. in Free Radical Research. 2007;41(1):62-72.
doi:10.1080/10715760600944296 .

Filipović, Miloš R., Stanić-Vučinić, Dragana, Raičević, Smiljana, Spasić, Mihajlo B., Niketić, Vesna, "Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide" in Free Radical Research, 41, no. 1 (2007):62-72,
https://doi.org/10.1080/10715760600944296 . .

TY  - JOUR
AU  - Nikolić, Milan
AU  - Nikolić -Kokić, Aleksandra
AU  - Stanić, Dragana
AU  - Blagojević, Duško
AU  - Vranić, Danijela
AU  - Jones, David R.
AU  - Niketić, Vesna
AU  - Spasić, Mihajlo B.
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4219
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 qudi, podeqenih 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.
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.
PB  - Belgrade : Serbian Chemical Society
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 and Vranić, Danijela and Jones, David R. and Niketić, Vesna and Spasić, Mihajlo B.",
year = "2007",
abstract = "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 qudi, podeqenih 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., 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.",
publisher = "Belgrade : Serbian Chemical Society",
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., 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
Belgrade : Serbian Chemical Society., 72(4), 339-345.
https://doi.org/10.2298/JSC0704339N

Nikolić M, Nikolić -Kokić A, Stanić D, Blagojević D, 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, 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 . .

TY  - JOUR
AU  - Stojanović, Srđan
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Raičević, Smiljana
AU  - Spasić, Mihajlo B.
AU  - Niketić, Vesna
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/215
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.
PB  - Serbian Chemical Society
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 and Stanić, Dragana and Nikolić, Milan and Raičević, Smiljana and Spasić, Mihajlo B. and Niketić, Vesna",
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 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.",
publisher = "Serbian Chemical Society",
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., Stanić, D., Nikolić, M., Raičević, S., Spasić, M. B.,& Niketić, V.. (2005). Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 70(4), 601-608.
https://doi.org/10.2298/JSC0504601S

Stojanović S, Stanić D, Nikolić M, Raičević S, Spasić MB, Niketić 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, Stanić, Dragana, Nikolić, Milan, Raičević, Smiljana, Spasić, Mihajlo B., Niketić, Vesna, "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 . .

TY  - JOUR
AU  - Stojanović, Srđan
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Spasić, Mihajlo
AU  - Niketić, Vesna
PY  - 2004
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2682
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  - Elsevier
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 and Stanić, Dragana and Nikolić, Milan and Spasić, Mihajlo and Niketić, Vesna",
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 = "Elsevier",
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., Stanić, D., Nikolić, M., Spasić, M.,& Niketić, V.. (2004). Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species. in Nitric Oxide: Biology and Chemistry
Elsevier., 11(3), 256-262.
https://doi.org/10.1016/j.niox.2004.09.007

Stojanović S, Stanić D, Nikolić M, Spasić M, Niketić 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, Stanić, Dragana, Nikolić, Milan, Spasić, Mihajlo, Niketić, Vesna, "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 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Niketić, Vesna
PY  - 2004
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2680
AB  - Recently, it was demonstrated that prolonged hyperinsulinism associated with hypoglycemia, both in vivo and in vitro, caused covalent glycoinositolphospholipid (GPI) binding to the C termini of both hemoglobin beta-chains, which resulted in the formation of a novel, hitherto unrecognized, minor hemoglobin fraction (GPI-Hb) (Niketic et al. Biochem. Biophys. Res. Commun. 239 (1997)435). In this study, it was demonstrated that exposure of erythrocyte membranes to insulin causes the activation of membrane protease as well as that the formation of GPI-Hb parallels its activity. It is suggested that the insulin-activated protease is able to catalyze. albeit slowly, the transpeptidation, i.e., the replacement of the carboxy-terminal amino acid(s) residues of the Hb beta-chains with GPI as an exogenous nucleophile. To our knowledge the present results show for the first time that insulin stimulates protease activity in erythrocyte membranes, as well as that insulin-activated protease may be involved in post-translational GPI binding to proteins.
AB  - U našim ranijim radovima pokazano je da u uslovima hiperinsulinizma i hipoglikemije, in vivo i in vitro, dolazi do kovalentnog vezivanja glikoinozitolfosfolipida (GPI) za karboksilne krajeve oba β-niza molekula hemoglobina (Hb), što se manifestuje nastajanjem nove, do tada nepoznate, manje frakcije hemoglobina (GPI-Hb) (Niketić et al., Biochem. Biophys. Res. Commun. 239 (1997) 435). U ovom radu je pokazano da vezivanje insulina za membrane eritrocita izaziva aktiviranje membranske proteaze, te da je nastajanje GPI-Hb u korelaciji sa proteaznom aktivnošću. Pretpostavljeno je da proteaza aktivirana insulinom može, mada sporo, da katalizuje reakciju transpeptidacije, tj. zamenu aminokiselinskih ostataka sa karboksilnog kraja β-nizova molekula Hb sa GPI-lipidom kao egzogenim nukleofilom. Prema našem saznanju opisani rezultati prvi puta pokazuju da insulin stimuliše proteaznu aktivnost u eritrocitima, te da je ova aktivnost povezana sa post-translacionim vezivanjem GPI-lipida za proteine.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Covalent glycoinositolphospholipid (GPI) binding to hemoglobin is associated with insulin-activation of erythrocyte membrane protease
T1  - Kovalentno vezivanje glikoinozitolfosfolipida (GPI) za hemoglobin pod dejstvom insulina praćeno je aktiviranjem proteaze iz membrane eritrocita
VL  - 69
IS  - 5
SP  - 343
EP  - 348
DO  - 10.2298/JSC0405343S
ER  - 

@article{
author = "Stanić, Dragana and Nikolić, Milan and Niketić, Vesna",
year = "2004",
abstract = "Recently, it was demonstrated that prolonged hyperinsulinism associated with hypoglycemia, both in vivo and in vitro, caused covalent glycoinositolphospholipid (GPI) binding to the C termini of both hemoglobin beta-chains, which resulted in the formation of a novel, hitherto unrecognized, minor hemoglobin fraction (GPI-Hb) (Niketic et al. Biochem. Biophys. Res. Commun. 239 (1997)435). In this study, it was demonstrated that exposure of erythrocyte membranes to insulin causes the activation of membrane protease as well as that the formation of GPI-Hb parallels its activity. It is suggested that the insulin-activated protease is able to catalyze. albeit slowly, the transpeptidation, i.e., the replacement of the carboxy-terminal amino acid(s) residues of the Hb beta-chains with GPI as an exogenous nucleophile. To our knowledge the present results show for the first time that insulin stimulates protease activity in erythrocyte membranes, as well as that insulin-activated protease may be involved in post-translational GPI binding to proteins., U našim ranijim radovima pokazano je da u uslovima hiperinsulinizma i hipoglikemije, in vivo i in vitro, dolazi do kovalentnog vezivanja glikoinozitolfosfolipida (GPI) za karboksilne krajeve oba β-niza molekula hemoglobina (Hb), što se manifestuje nastajanjem nove, do tada nepoznate, manje frakcije hemoglobina (GPI-Hb) (Niketić et al., Biochem. Biophys. Res. Commun. 239 (1997) 435). U ovom radu je pokazano da vezivanje insulina za membrane eritrocita izaziva aktiviranje membranske proteaze, te da je nastajanje GPI-Hb u korelaciji sa proteaznom aktivnošću. Pretpostavljeno je da proteaza aktivirana insulinom može, mada sporo, da katalizuje reakciju transpeptidacije, tj. zamenu aminokiselinskih ostataka sa karboksilnog kraja β-nizova molekula Hb sa GPI-lipidom kao egzogenim nukleofilom. Prema našem saznanju opisani rezultati prvi puta pokazuju da insulin stimuliše proteaznu aktivnost u eritrocitima, te da je ova aktivnost povezana sa post-translacionim vezivanjem GPI-lipida za proteine.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Covalent glycoinositolphospholipid (GPI) binding to hemoglobin is associated with insulin-activation of erythrocyte membrane protease, Kovalentno vezivanje glikoinozitolfosfolipida (GPI) za hemoglobin pod dejstvom insulina praćeno je aktiviranjem proteaze iz membrane eritrocita",
volume = "69",
number = "5",
pages = "343-348",
doi = "10.2298/JSC0405343S"
}

Stanić, D., Nikolić, M.,& Niketić, V.. (2004). Covalent glycoinositolphospholipid (GPI) binding to hemoglobin is associated with insulin-activation of erythrocyte membrane protease. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 69(5), 343-348.
https://doi.org/10.2298/JSC0405343S

Stanić D, Nikolić M, Niketić V. Covalent glycoinositolphospholipid (GPI) binding to hemoglobin is associated with insulin-activation of erythrocyte membrane protease. in Journal of the Serbian Chemical Society. 2004;69(5):343-348.
doi:10.2298/JSC0405343S .

Stanić, Dragana, Nikolić, Milan, Niketić, Vesna, "Covalent glycoinositolphospholipid (GPI) binding to hemoglobin is associated with insulin-activation of erythrocyte membrane protease" in Journal of the Serbian Chemical Society, 69, no. 5 (2004):343-348,
https://doi.org/10.2298/JSC0405343S . .

TY  - JOUR
AU  - Nikolić, Milan
AU  - Stanić, Dragana
AU  - Antonijevic, Nadežda
AU  - Niketić, Vesna
PY  - 2004
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4167
AB  - Objective: To study lipid fraction that is occasionally observed in red blood cell (RBC) hemolysate (supernatants from which membranes were separated). Study design: Plasma lipid profiles, cholesterol (Ch) and phospholipids (PL) in intact RBCs, RBC membranes and hemolysates were examined in young healthy male population in winter and summer. Results: The RBC Ch and PL content was significantly higher than in membranes, both in winter and summer. The "excess" of cholesterol (associated with phospholipid) was bound to hemoglobin yielding Hb-lipid adduct (Hb-Ch), the pools in the RBC membrane remaining virtually unaltered. Levels of hemoglobin- lipid complex (Hb-Ch), which were significantly higher in winter than in summer (30% and 19% of the total Hb, respectively), positively correlated with plasma HDL cholesterol levels. Conclusion: To our knowledge, this is the first demonstration of cholesterol binding to Hb. The results suggest influence of plasma lipoprotein metabolism on the formation of Hb-Ch. (C) 2003 The Canadian Society of Clinical Chemists. All rights reserved.
PB  - Elsevier
T2  - Clinical Biochemistry
T1  - Cholesterol bound to hemoglobin in normal human erythrocytes: a new form of cholesterol in circulation?
VL  - 37
IS  - 1
SP  - 22
EP  - 26
DO  - 10.1016/j.clinbiochem.2003.10.002
ER  - 

@article{
author = "Nikolić, Milan and Stanić, Dragana and Antonijevic, Nadežda and Niketić, Vesna",
year = "2004",
abstract = "Objective: To study lipid fraction that is occasionally observed in red blood cell (RBC) hemolysate (supernatants from which membranes were separated). Study design: Plasma lipid profiles, cholesterol (Ch) and phospholipids (PL) in intact RBCs, RBC membranes and hemolysates were examined in young healthy male population in winter and summer. Results: The RBC Ch and PL content was significantly higher than in membranes, both in winter and summer. The "excess" of cholesterol (associated with phospholipid) was bound to hemoglobin yielding Hb-lipid adduct (Hb-Ch), the pools in the RBC membrane remaining virtually unaltered. Levels of hemoglobin- lipid complex (Hb-Ch), which were significantly higher in winter than in summer (30% and 19% of the total Hb, respectively), positively correlated with plasma HDL cholesterol levels. Conclusion: To our knowledge, this is the first demonstration of cholesterol binding to Hb. The results suggest influence of plasma lipoprotein metabolism on the formation of Hb-Ch. (C) 2003 The Canadian Society of Clinical Chemists. All rights reserved.",
publisher = "Elsevier",
journal = "Clinical Biochemistry",
title = "Cholesterol bound to hemoglobin in normal human erythrocytes: a new form of cholesterol in circulation?",
volume = "37",
number = "1",
pages = "22-26",
doi = "10.1016/j.clinbiochem.2003.10.002"
}

Nikolić, M., Stanić, D., Antonijevic, N.,& Niketić, V.. (2004). Cholesterol bound to hemoglobin in normal human erythrocytes: a new form of cholesterol in circulation?. in Clinical Biochemistry
Elsevier., 37(1), 22-26.
https://doi.org/10.1016/j.clinbiochem.2003.10.002

Nikolić M, Stanić D, Antonijevic N, Niketić V. Cholesterol bound to hemoglobin in normal human erythrocytes: a new form of cholesterol in circulation?. in Clinical Biochemistry. 2004;37(1):22-26.
doi:10.1016/j.clinbiochem.2003.10.002 .

Nikolić, Milan, Stanić, Dragana, Antonijevic, Nadežda, Niketić, Vesna, "Cholesterol bound to hemoglobin in normal human erythrocytes: a new form of cholesterol in circulation?" in Clinical Biochemistry, 37, no. 1 (2004):22-26,
https://doi.org/10.1016/j.clinbiochem.2003.10.002 . .

TY  - JOUR
AU  - Niketić, Vesna
AU  - Stojanović, Srđan
AU  - Spasić, Mihajlo
PY  - 1998
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3887
AB  - Recent evidence revealed that reactive oxygen species (ROS) such assuperoxide (O  ) and hydrogen peroxide (H O ), which are conventionally2.-22viewed as unwanted and toxic by-products of life in an aerobic environment,have  physiological  roles.  Appraisal  of  the  roles  of  reactive  NO  species(RNOS), such as nitrosonium (NO ) and nitroxyl (NO ) ions, peroxynitrite+-(OONO ), and higher nitrogen oxides (NO ) in NO mediated processes, is-xgrowing  at  a  rapid  rate.  ROS  and  RNOS  may  evoke  a  variety  of  cellularresponses, ranging from major changes in mammalian cell gene expressionto apoptotic death. The greater prevalence and reactivity of thiols over otherbiological nucleophiles makes them targets for both ROS and RNOS. Anyessential  protein  containing  cysteine  residue  that  is  strategically  located  ateither active or allosteric site should be considered as a target for regulationby  ROS  and/or  RNOS.  Candidate  molecules  include  proteins  that  are themselves involved in signal transduction processes, ion channels, receptors,G-proteins, protein-kinases, protein phosphatases, and transcription-activatingfactors. In this paper the mechanisms of generation of ROS and RNOS andtheir  reactions  with  thiols  are  briefly  described.  The  regulation  of  cellprocesses by ROS and RNOS is illustrated by the interference of ROS andRNOS effects with receptor tyrosine kinases signaling.
PB  - Yugoslav Union of Physiological Societies
T2  - Iugoslav. Physiol. Pharmacol. Acta
T1  - Regulation of cell processes by rective oxygen and nitric oxide species - Mechanisms of reactions
T1  - Regulacija ćelijskih procesa reaktivnim vrstama kiseonika i azot monoksida - Mehanizmi reakcija
VL  - 34
SP  - 463
EP  - 477
UR  - https://hdl.handle.net/21.15107/rcub_cer_3887
ER  - 

@article{
author = "Niketić, Vesna and Stojanović, Srđan and Spasić, Mihajlo",
year = "1998",
abstract = "Recent evidence revealed that reactive oxygen species (ROS) such assuperoxide (O  ) and hydrogen peroxide (H O ), which are conventionally2.-22viewed as unwanted and toxic by-products of life in an aerobic environment,have  physiological  roles.  Appraisal  of  the  roles  of  reactive  NO  species(RNOS), such as nitrosonium (NO ) and nitroxyl (NO ) ions, peroxynitrite+-(OONO ), and higher nitrogen oxides (NO ) in NO mediated processes, is-xgrowing  at  a  rapid  rate.  ROS  and  RNOS  may  evoke  a  variety  of  cellularresponses, ranging from major changes in mammalian cell gene expressionto apoptotic death. The greater prevalence and reactivity of thiols over otherbiological nucleophiles makes them targets for both ROS and RNOS. Anyessential  protein  containing  cysteine  residue  that  is  strategically  located  ateither active or allosteric site should be considered as a target for regulationby  ROS  and/or  RNOS.  Candidate  molecules  include  proteins  that  are themselves involved in signal transduction processes, ion channels, receptors,G-proteins, protein-kinases, protein phosphatases, and transcription-activatingfactors. In this paper the mechanisms of generation of ROS and RNOS andtheir  reactions  with  thiols  are  briefly  described.  The  regulation  of  cellprocesses by ROS and RNOS is illustrated by the interference of ROS andRNOS effects with receptor tyrosine kinases signaling.",
publisher = "Yugoslav Union of Physiological Societies",
journal = "Iugoslav. Physiol. Pharmacol. Acta",
title = "Regulation of cell processes by rective oxygen and nitric oxide species - Mechanisms of reactions, Regulacija ćelijskih procesa reaktivnim vrstama kiseonika i azot monoksida - Mehanizmi reakcija",
volume = "34",
pages = "463-477",
url = "https://hdl.handle.net/21.15107/rcub_cer_3887"
}

Niketić, V., Stojanović, S.,& Spasić, M.. (1998). Regulation of cell processes by rective oxygen and nitric oxide species - Mechanisms of reactions. in Iugoslav. Physiol. Pharmacol. Acta
Yugoslav Union of Physiological Societies., 34, 463-477.
https://hdl.handle.net/21.15107/rcub_cer_3887

Niketić V, Stojanović S, Spasić M. Regulation of cell processes by rective oxygen and nitric oxide species - Mechanisms of reactions. in Iugoslav. Physiol. Pharmacol. Acta. 1998;34:463-477.
https://hdl.handle.net/21.15107/rcub_cer_3887 .

Niketić, Vesna, Stojanović, Srđan, Spasić, Mihajlo, "Regulation of cell processes by rective oxygen and nitric oxide species - Mechanisms of reactions" in Iugoslav. Physiol. Pharmacol. Acta, 34 (1998):463-477,
https://hdl.handle.net/21.15107/rcub_cer_3887 .

TY  - JOUR
AU  - Niketić, Vesna
AU  - Tomašević, N
AU  - Vajs, Vlatka
AU  - Bojić, Ž
PY  - 1996
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2794
AB  - In this work a novel hitherto unrecognised hemoglobin (Hb) fraction, HbA1x, which we detected previously in hemolysates of erythrocytes exposed to high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, was analysed. Both β chains of Hb in HbA1x were found to be modified by covalent binding of a substance containing sugar, phosphate and fatty acid residues. HbA1x was therefore termed glycophospholipid (GPL) adduct (Hb-GPL). To our knowledge, this is the first demonstration of such modification of Hb, as well as the first demonstration of post-translational GPL binding to proteins in response to insulin binding to a cell. The mechanism proposed for Hb-GPL formation is briefly described.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin
VL  - 61
IS  - 7
SP  - 535
EP  - 538
UR  - https://hdl.handle.net/21.15107/rcub_cer_2794
ER  - 

@article{
author = "Niketić, Vesna and Tomašević, N and Vajs, Vlatka and Bojić, Ž",
year = "1996",
abstract = "In this work a novel hitherto unrecognised hemoglobin (Hb) fraction, HbA1x, which we detected previously in hemolysates of erythrocytes exposed to high concentration of insulin under hypoglycemic conditions, both in vivo and in vitro, was analysed. Both β chains of Hb in HbA1x were found to be modified by covalent binding of a substance containing sugar, phosphate and fatty acid residues. HbA1x was therefore termed glycophospholipid (GPL) adduct (Hb-GPL). To our knowledge, this is the first demonstration of such modification of Hb, as well as the first demonstration of post-translational GPL binding to proteins in response to insulin binding to a cell. The mechanism proposed for Hb-GPL formation is briefly described.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin",
volume = "61",
number = "7",
pages = "535-538",
url = "https://hdl.handle.net/21.15107/rcub_cer_2794"
}

Niketić, V., Tomašević, N., Vajs, V.,& Bojić, Ž.. (1996). Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 61(7), 535-538.
https://hdl.handle.net/21.15107/rcub_cer_2794

Niketić V, Tomašević N, Vajs V, Bojić Ž. Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin. in Journal of the Serbian Chemical Society. 1996;61(7):535-538.
https://hdl.handle.net/21.15107/rcub_cer_2794 .

Niketić, Vesna, Tomašević, N, Vajs, Vlatka, Bojić, Ž, "Covalent glycophospholipid binding to hemoglobin. A new post-translational modification occurring in erythrocytes exposed to insulin" in Journal of the Serbian Chemical Society, 61, no. 7 (1996):535-538,
https://hdl.handle.net/21.15107/rcub_cer_2794 .