TY  - JOUR
AU  - Nikolić-Kokić, Aleksandra
AU  - Oreščanin-Dušić, Zorana
AU  - Spasojević, Ivan
AU  - Blagojević, Duško
AU  - Stević, Zorica D
AU  - Andjus, Pavle R.
AU  - Spasić, Mihajlo
PY  - 2015
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/902
AB  - In this work we compared the mutated liver copper zinc-containing superoxide dismutase (SOD1) protein G93A of the transgenic rat model of familial amyotrophic lateral sclerosis (FALS), to wild-type (WT) rat SOD1. We examined their enzymatic activities and effects on isometric contractions of uteri of healthy virgin rats. G93A SOD1 showed a slightly higher activity than WT SOD1 and, in contrast to WT SOD1, G93A SOD1 did not induce smooth muscle relaxation. This result indicates that effects on smooth muscles are not related to SOD1 enzyme activity and suggest that heterodimers of G93A SOD1 form an ion-conducting pore that diminishes the relaxatory effects of SOD1. We propose that this type of pathogenic feedback affects neurons in FALS.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - The effects of wild-type and mutant sod1 on smooth muscle contraction
EP  - 192
IS  - 1
SP  - 187
VL  - 67
DO  - 10.2298/ABS141006023N
ER  - 

@article{
author = "Nikolić-Kokić, Aleksandra and Oreščanin-Dušić, Zorana and Spasojević, Ivan and Blagojević, Duško and Stević, Zorica D and Andjus, Pavle R. and Spasić, Mihajlo",
year = "2015",
abstract = "In this work we compared the mutated liver copper zinc-containing superoxide dismutase (SOD1) protein G93A of the transgenic rat model of familial amyotrophic lateral sclerosis (FALS), to wild-type (WT) rat SOD1. We examined their enzymatic activities and effects on isometric contractions of uteri of healthy virgin rats. G93A SOD1 showed a slightly higher activity than WT SOD1 and, in contrast to WT SOD1, G93A SOD1 did not induce smooth muscle relaxation. This result indicates that effects on smooth muscles are not related to SOD1 enzyme activity and suggest that heterodimers of G93A SOD1 form an ion-conducting pore that diminishes the relaxatory effects of SOD1. We propose that this type of pathogenic feedback affects neurons in FALS.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "The effects of wild-type and mutant sod1 on smooth muscle contraction",
pages = "192-187",
number = "1",
volume = "67",
doi = "10.2298/ABS141006023N"
}

Nikolić-Kokić, A., Oreščanin-Dušić, Z., Spasojević, I., Blagojević, D., Stević, Z. D., Andjus, P. R.,& Spasić, M.. (2015). The effects of wild-type and mutant sod1 on smooth muscle contraction. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 67(1), 187-192.
https://doi.org/10.2298/ABS141006023N

Nikolić-Kokić A, Oreščanin-Dušić Z, Spasojević I, Blagojević D, Stević ZD, Andjus PR, Spasić M. The effects of wild-type and mutant sod1 on smooth muscle contraction. in Archives of Biological Sciences. 2015;67(1):187-192.
doi:10.2298/ABS141006023N .

Nikolić-Kokić, Aleksandra, Oreščanin-Dušić, Zorana, Spasojević, Ivan, Blagojević, Duško, Stević, Zorica D, Andjus, Pavle R., Spasić, Mihajlo, "The effects of wild-type and mutant sod1 on smooth muscle contraction" in Archives of Biological Sciences, 67, no. 1 (2015):187-192,
https://doi.org/10.2298/ABS141006023N . .

TY  - JOUR
AU  - Nikolić-Kokić, Aleksandra
AU  - Oreščanin-Dušić, Zorana
AU  - Slavić, Marija
AU  - Spasojević, Ivan
AU  - Stević, Zorica D
AU  - Spasić, Mihajlo
AU  - Blagojević, Duško P
PY  - 2013
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/680
AB  - Uvod: Mutirana bakar, cink superoksid-dizmutaza (SOD1) može da pravi agregate, sto predstavlja početni uzrok oštećenja motornog neurona može da izazove nastanak bolesti. U ovom radu su pokazani efekti humane bakar, cink super-oksid dizmutaze iz krvi pacijenata obolelih od familijarne amiotrofične lateralne skleroze (FALS) sa Leu144Phe (L144F) mutacijom i normalne (wild-type - WT) humane SOD1, iz krvi zdravih kontrola, na glatkom mišiću. Metode: Izolovali smo WT i L144F SOD1 enzime kod osam odabranih FALS pacijenata sa L144F mutacijom na egzonu 5 i pet zdravih kontrola. Dalje smo ispitivali aktivnost SOD1 u dobijenim uzorcima adrenalinskom metodom i elektro-foretski ih profilisali. Konačno, izolovanu WT i L144F SOD1 aplicirali smo na izolovani uterus pacova. Rezultati: Aktivnost L144F SOD1 je statistički značajno manja (p lt 0,05) u poređenju sa aktivnosti WT SOD1 zdravih kontrola. L144F ne izaziva relaksaciju glatkog mišića, kao sto je to slučaj sa WT SOD1. Zaključak: Naši rezultati pokazuju da izostanak relaksacije mišićnog tonusa u prisustvu mutirane SOD1 može imati štetni povratni efekat kod FALS pacijenata.
AB  - Background: Mutated copper, zinc-containing superoxide dismutase (SOD1) may self-aggregate, an event that could also be an initial cause of motor neuron malfunction leading to disease onset. The effects of human mutated SOD1 protein from the blood of familial amyotrophic lateral sclerosis (FALS) patients bearing Leu144Phe (L144F) mutation were compared to wild-type (WT) human SOD1 derived from healthy examinees, for enzymatic activity and the effects on isometric contractions of non-vascular smooth muscle. Methods: We isolated WT and L144F SOD1 enzymes from eight patients with FALS, L144F mutation in exon 5 and eight healthy controls. We then investigated SOD1 activities in the obtained samples by the adrenaline method and profiled them electrophoretically. Finally, we applied WT and L144F SOD1 on the isolated rat uterus. Results: L144F SOD1 showed lower superoxide-dismutating activity compared to WT human SOD1. We found that, in contrast to WT human SOD1, mutated L144F does not induce smooth muscle relaxation. Conclusions: Our data suggest that the lack of relaxation of muscle tonus in the presence of mutated SOD1 may have pathogenic feedback effects in FALS.
PB  - Društvo medicinskih biohemičara Srbije, Beograd i Versita
T2  - Journal of Medical Biochemistry
T1  - Efekti humane normalne i FALS mutirane L144P SOD1 na nevaskularne kontrakcije glatkih mišića
T1  - The effects of human wild-type and FALS mutant L144P SOD1 on non-vascular smooth muscle contractions
EP  - 379
IS  - 4
SP  - 375
VL  - 32
DO  - 10.2478/jomb-2013-0032
ER  - 

@article{
author = "Nikolić-Kokić, Aleksandra and Oreščanin-Dušić, Zorana and Slavić, Marija and Spasojević, Ivan and Stević, Zorica D and Spasić, Mihajlo and Blagojević, Duško P",
year = "2013",
abstract = "Uvod: Mutirana bakar, cink superoksid-dizmutaza (SOD1) može da pravi agregate, sto predstavlja početni uzrok oštećenja motornog neurona može da izazove nastanak bolesti. U ovom radu su pokazani efekti humane bakar, cink super-oksid dizmutaze iz krvi pacijenata obolelih od familijarne amiotrofične lateralne skleroze (FALS) sa Leu144Phe (L144F) mutacijom i normalne (wild-type - WT) humane SOD1, iz krvi zdravih kontrola, na glatkom mišiću. Metode: Izolovali smo WT i L144F SOD1 enzime kod osam odabranih FALS pacijenata sa L144F mutacijom na egzonu 5 i pet zdravih kontrola. Dalje smo ispitivali aktivnost SOD1 u dobijenim uzorcima adrenalinskom metodom i elektro-foretski ih profilisali. Konačno, izolovanu WT i L144F SOD1 aplicirali smo na izolovani uterus pacova. Rezultati: Aktivnost L144F SOD1 je statistički značajno manja (p lt 0,05) u poređenju sa aktivnosti WT SOD1 zdravih kontrola. L144F ne izaziva relaksaciju glatkog mišića, kao sto je to slučaj sa WT SOD1. Zaključak: Naši rezultati pokazuju da izostanak relaksacije mišićnog tonusa u prisustvu mutirane SOD1 može imati štetni povratni efekat kod FALS pacijenata., Background: Mutated copper, zinc-containing superoxide dismutase (SOD1) may self-aggregate, an event that could also be an initial cause of motor neuron malfunction leading to disease onset. The effects of human mutated SOD1 protein from the blood of familial amyotrophic lateral sclerosis (FALS) patients bearing Leu144Phe (L144F) mutation were compared to wild-type (WT) human SOD1 derived from healthy examinees, for enzymatic activity and the effects on isometric contractions of non-vascular smooth muscle. Methods: We isolated WT and L144F SOD1 enzymes from eight patients with FALS, L144F mutation in exon 5 and eight healthy controls. We then investigated SOD1 activities in the obtained samples by the adrenaline method and profiled them electrophoretically. Finally, we applied WT and L144F SOD1 on the isolated rat uterus. Results: L144F SOD1 showed lower superoxide-dismutating activity compared to WT human SOD1. We found that, in contrast to WT human SOD1, mutated L144F does not induce smooth muscle relaxation. Conclusions: Our data suggest that the lack of relaxation of muscle tonus in the presence of mutated SOD1 may have pathogenic feedback effects in FALS.",
publisher = "Društvo medicinskih biohemičara Srbije, Beograd i Versita",
journal = "Journal of Medical Biochemistry",
title = "Efekti humane normalne i FALS mutirane L144P SOD1 na nevaskularne kontrakcije glatkih mišića, The effects of human wild-type and FALS mutant L144P SOD1 on non-vascular smooth muscle contractions",
pages = "379-375",
number = "4",
volume = "32",
doi = "10.2478/jomb-2013-0032"
}

Nikolić-Kokić, A., Oreščanin-Dušić, Z., Slavić, M., Spasojević, I., Stević, Z. D., Spasić, M.,& Blagojević, D. P.. (2013). Efekti humane normalne i FALS mutirane L144P SOD1 na nevaskularne kontrakcije glatkih mišića. in Journal of Medical Biochemistry
Društvo medicinskih biohemičara Srbije, Beograd i Versita., 32(4), 375-379.
https://doi.org/10.2478/jomb-2013-0032

Nikolić-Kokić A, Oreščanin-Dušić Z, Slavić M, Spasojević I, Stević ZD, Spasić M, Blagojević DP. Efekti humane normalne i FALS mutirane L144P SOD1 na nevaskularne kontrakcije glatkih mišića. in Journal of Medical Biochemistry. 2013;32(4):375-379.
doi:10.2478/jomb-2013-0032 .

Nikolić-Kokić, Aleksandra, Oreščanin-Dušić, Zorana, Slavić, Marija, Spasojević, Ivan, Stević, Zorica D, Spasić, Mihajlo, Blagojević, Duško P, "Efekti humane normalne i FALS mutirane L144P SOD1 na nevaskularne kontrakcije glatkih mišića" in Journal of Medical Biochemistry, 32, no. 4 (2013):375-379,
https://doi.org/10.2478/jomb-2013-0032 . .

TY  - JOUR
AU  - Ignjatović, Aleksandar
AU  - Stević, Zorica D
AU  - Lavrnic, Dragana S
AU  - Nikolić-Kokić, Aleksandra
AU  - Blagojević, Duško P
AU  - Spasić, Mihajlo
AU  - Spasojević, Ivan
PY  - 2012
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/535
AB  - ALS is characterized by oxidative damage in the brain and cerebrospinal fluid, which is exerted by pro-oxidative activity of iron. Such activity of iron can be drastically increased in the presence of inappropriate iron ligands that catalyze redox cycling of iron, thereby promoting hydroxyl radical generation. The aim of our study was to determine the relative level of inappropriate iron ligands in the cerebrospinal fluid of ALS patients. To determine the levels of inappropriate iron ligands and redox activity of iron in cerebrospinal fluid (10 samples from ALS patients and 10 controls), we applied electron paramagnetic resonance spectroscopy. We have shown that cerebrospinal fluid of ALS patients comprises twofold increased level of inappropriate iron ligands, proportionally increasing iron redox activity and hydroxyl radical production compared to controls. In conclusion, our results strongly support the pro-oxidative/detrimental role of inappropriately chelated iron in ALS pathophysiology. The identification of biomolecules that form such iron complexes and their therapeutic targeting may represent the future of ALS treatment.
PB  - Informa Healthcare, London
T2  - Amyotrophic Lateral Sclerosis
T1  - Inappropriately chelated iron in the cerebrospinal fluid of amyotrophic lateral sclerosis patients
EP  - 362
IS  - 4
SP  - 357
VL  - 13
DO  - 10.3109/17482968.2012.665929
ER  - 

@article{
author = "Ignjatović, Aleksandar and Stević, Zorica D and Lavrnic, Dragana S and Nikolić-Kokić, Aleksandra and Blagojević, Duško P and Spasić, Mihajlo and Spasojević, Ivan",
year = "2012",
abstract = "ALS is characterized by oxidative damage in the brain and cerebrospinal fluid, which is exerted by pro-oxidative activity of iron. Such activity of iron can be drastically increased in the presence of inappropriate iron ligands that catalyze redox cycling of iron, thereby promoting hydroxyl radical generation. The aim of our study was to determine the relative level of inappropriate iron ligands in the cerebrospinal fluid of ALS patients. To determine the levels of inappropriate iron ligands and redox activity of iron in cerebrospinal fluid (10 samples from ALS patients and 10 controls), we applied electron paramagnetic resonance spectroscopy. We have shown that cerebrospinal fluid of ALS patients comprises twofold increased level of inappropriate iron ligands, proportionally increasing iron redox activity and hydroxyl radical production compared to controls. In conclusion, our results strongly support the pro-oxidative/detrimental role of inappropriately chelated iron in ALS pathophysiology. The identification of biomolecules that form such iron complexes and their therapeutic targeting may represent the future of ALS treatment.",
publisher = "Informa Healthcare, London",
journal = "Amyotrophic Lateral Sclerosis",
title = "Inappropriately chelated iron in the cerebrospinal fluid of amyotrophic lateral sclerosis patients",
pages = "362-357",
number = "4",
volume = "13",
doi = "10.3109/17482968.2012.665929"
}

Ignjatović, A., Stević, Z. D., Lavrnic, D. S., Nikolić-Kokić, A., Blagojević, D. P., Spasić, M.,& Spasojević, I.. (2012). Inappropriately chelated iron in the cerebrospinal fluid of amyotrophic lateral sclerosis patients. in Amyotrophic Lateral Sclerosis
Informa Healthcare, London., 13(4), 357-362.
https://doi.org/10.3109/17482968.2012.665929

Ignjatović A, Stević ZD, Lavrnic DS, Nikolić-Kokić A, Blagojević DP, Spasić M, Spasojević I. Inappropriately chelated iron in the cerebrospinal fluid of amyotrophic lateral sclerosis patients. in Amyotrophic Lateral Sclerosis. 2012;13(4):357-362.
doi:10.3109/17482968.2012.665929 .

Ignjatović, Aleksandar, Stević, Zorica D, Lavrnic, Dragana S, Nikolić-Kokić, Aleksandra, Blagojević, Duško P, Spasić, Mihajlo, Spasojević, Ivan, "Inappropriately chelated iron in the cerebrospinal fluid of amyotrophic lateral sclerosis patients" in Amyotrophic Lateral Sclerosis, 13, no. 4 (2012):357-362,
https://doi.org/10.3109/17482968.2012.665929 . .