TY  - JOUR
AU  - Bufan, Billjana
AU  - Ćuruvija, Ivana
AU  - Blagojević, Veljko
AU  - Grujić-Milanović, Jelica
AU  - Prijić, Ivana
AU  - Radosavljević, Tatjana
AU  - Samardžić, Janko
AU  - Radosavljević, Milica
AU  - Janković, Radmila
AU  - Đuretić, Jasmina
PY  - 2024
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1470
AB  - Aging is closely related to the main aspects of multiple sclerosis (MS). The average age ofthe MS population is increasing and the number of elderly MS patients is expected to increase. Inaddition to neurons,N-methyl-D-aspartate receptors (NMDARs) are also expressed on non-neuronalcells,  such  as  immune  cells.   The  aim  of  this  study  was  to  investigate  the  role  of  NMDARs  inexperimental autoimmune encephalomyelitis (EAE) in young and aged rats.  Memantine, a non-competitive NMDAR antagonist, was administered to young and agedDark Agoutirats from day7 after immunization.  Antagonizing NMDARs had a more favourable effect on clinical disease,reactivation, and apoptosis of CD4+T cells in the target organ of aged EAE rats. The expression ofthe fractalkine receptor CX3CR1 was increased in memantine-treated rats, but to a greater extent inaged rats. Additionally, memantine increased Nrf2 and Nrf2-regulated enzymes’ mRNA expressionin brain tissue. The concentrations of superoxide anion radicals, malondialdehyde, and advancedoxidation protein products in brain tissue were consistent with previous results. Overall, our resultssuggest that NMDARs play a more important role in the pathogenesis of EAE in aged than inyoung rats.
PB  - Basel, Switzerland : MDPI
T2  - Biomedicines
T1  - NMDA Receptor Antagonist Memantine AmelioratesExperimental Autoimmune Encephalomyelitis in Aged Rats
IS  - 4
SP  - 717
VL  - 12
DO  - 10.3390/biomedicines12040717
ER  - 

@article{
author = "Bufan, Billjana and Ćuruvija, Ivana and Blagojević, Veljko and Grujić-Milanović, Jelica and Prijić, Ivana and Radosavljević, Tatjana and Samardžić, Janko and Radosavljević, Milica and Janković, Radmila and Đuretić, Jasmina",
year = "2024",
abstract = "Aging is closely related to the main aspects of multiple sclerosis (MS). The average age ofthe MS population is increasing and the number of elderly MS patients is expected to increase. Inaddition to neurons,N-methyl-D-aspartate receptors (NMDARs) are also expressed on non-neuronalcells,  such  as  immune  cells.   The  aim  of  this  study  was  to  investigate  the  role  of  NMDARs  inexperimental autoimmune encephalomyelitis (EAE) in young and aged rats.  Memantine, a non-competitive NMDAR antagonist, was administered to young and agedDark Agoutirats from day7 after immunization.  Antagonizing NMDARs had a more favourable effect on clinical disease,reactivation, and apoptosis of CD4+T cells in the target organ of aged EAE rats. The expression ofthe fractalkine receptor CX3CR1 was increased in memantine-treated rats, but to a greater extent inaged rats. Additionally, memantine increased Nrf2 and Nrf2-regulated enzymes’ mRNA expressionin brain tissue. The concentrations of superoxide anion radicals, malondialdehyde, and advancedoxidation protein products in brain tissue were consistent with previous results. Overall, our resultssuggest that NMDARs play a more important role in the pathogenesis of EAE in aged than inyoung rats.",
publisher = "Basel, Switzerland : MDPI",
journal = "Biomedicines",
title = "NMDA Receptor Antagonist Memantine AmelioratesExperimental Autoimmune Encephalomyelitis in Aged Rats",
number = "4",
pages = "717",
volume = "12",
doi = "10.3390/biomedicines12040717"
}

Bufan, B., Ćuruvija, I., Blagojević, V., Grujić-Milanović, J., Prijić, I., Radosavljević, T., Samardžić, J., Radosavljević, M., Janković, R.,& Đuretić, J.. (2024). NMDA Receptor Antagonist Memantine AmelioratesExperimental Autoimmune Encephalomyelitis in Aged Rats. in Biomedicines
Basel, Switzerland : MDPI., 12(4), 717.
https://doi.org/10.3390/biomedicines12040717

Bufan B, Ćuruvija I, Blagojević V, Grujić-Milanović J, Prijić I, Radosavljević T, Samardžić J, Radosavljević M, Janković R, Đuretić J. NMDA Receptor Antagonist Memantine AmelioratesExperimental Autoimmune Encephalomyelitis in Aged Rats. in Biomedicines. 2024;12(4):717.
doi:10.3390/biomedicines12040717 .

Bufan, Billjana, Ćuruvija, Ivana, Blagojević, Veljko, Grujić-Milanović, Jelica, Prijić, Ivana, Radosavljević, Tatjana, Samardžić, Janko, Radosavljević, Milica, Janković, Radmila, Đuretić, Jasmina, "NMDA Receptor Antagonist Memantine AmelioratesExperimental Autoimmune Encephalomyelitis in Aged Rats" in Biomedicines, 12, no. 4 (2024):717,
https://doi.org/10.3390/biomedicines12040717 . .

TY  - JOUR
AU  - Nikodijević, Slavomir
AU  - Blagojević, Veljko
AU  - Ćuruvija, Ivana
AU  - Kosanović, Dejana
AU  - Đukić, Tamara
AU  - Đorđević, Brižita
AU  - Ilić, Vesna
AU  - Minić, Rajna
PY  - 2022
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1336
AB  - Increased interest in microbiota calls for the thorough analysis of antibody reactivity to different microorganisms. As salivary IgA represents the first line of defence against microorganisms contacting mucosal surfaces, we explored the binding and specificity of salivary IgA by testing the binding of purified, FITC-labelled salivary IgA to different microorganisms in flow cytometry and conclude that this kind of analysis enables the differentiation of species/strains with high IgA binding capacity, which should be corroborated on a larger sample size. Further we compare, with in-house ELISA, the binding of polyclonal salivary IgA with the binding of polyclonal serum IgA from the same individuals to whole microbial cells and to purified microbial components. High correlations were obtained in total salivary IgA binding to Lactobacillus rhamnosus and Escherichia coli, very distant bacterial species, as well as to isolated bacterial components (r =.70–.97). The binding of total salivary IgA resembled the binding of both salivary IgA1 and IgA2, with IgA2 predominating. For serum polyclonal IgA repertoire, substantially higher specificity was obtained. Serum IgA binding to E. coli correlated best with serum IgA binding to lipopolysaccharide (r =.86), and serum IgA against L. rhamnosus correlated best with the anti-peptidoglycan IgA levels (r =.88). We have also detected that total serum IgA response is governed by either IgA1 or IgA2 response, depending on the nature of the antigen/s. We conclude that steady state salivary IgA repertoire, unlike serum IgA repertoire, consists of polyreactive antibodies with innate specificity, questioning its capacity to select resident microbiota.
PB  - Wiley-Blackwell
T2  - Scandinavian Journal of Immunology
T1  - Selectivity of polyclonal repertoire of anti‐microbial IgA and its subclasses in saliva and serum in humans
IS  - 6
SP  - e13223
VL  - 96
DO  - 10.1111/sji.13223
ER  - 

@article{
author = "Nikodijević, Slavomir and Blagojević, Veljko and Ćuruvija, Ivana and Kosanović, Dejana and Đukić, Tamara and Đorđević, Brižita and Ilić, Vesna and Minić, Rajna",
year = "2022",
abstract = "Increased interest in microbiota calls for the thorough analysis of antibody reactivity to different microorganisms. As salivary IgA represents the first line of defence against microorganisms contacting mucosal surfaces, we explored the binding and specificity of salivary IgA by testing the binding of purified, FITC-labelled salivary IgA to different microorganisms in flow cytometry and conclude that this kind of analysis enables the differentiation of species/strains with high IgA binding capacity, which should be corroborated on a larger sample size. Further we compare, with in-house ELISA, the binding of polyclonal salivary IgA with the binding of polyclonal serum IgA from the same individuals to whole microbial cells and to purified microbial components. High correlations were obtained in total salivary IgA binding to Lactobacillus rhamnosus and Escherichia coli, very distant bacterial species, as well as to isolated bacterial components (r =.70–.97). The binding of total salivary IgA resembled the binding of both salivary IgA1 and IgA2, with IgA2 predominating. For serum polyclonal IgA repertoire, substantially higher specificity was obtained. Serum IgA binding to E. coli correlated best with serum IgA binding to lipopolysaccharide (r =.86), and serum IgA against L. rhamnosus correlated best with the anti-peptidoglycan IgA levels (r =.88). We have also detected that total serum IgA response is governed by either IgA1 or IgA2 response, depending on the nature of the antigen/s. We conclude that steady state salivary IgA repertoire, unlike serum IgA repertoire, consists of polyreactive antibodies with innate specificity, questioning its capacity to select resident microbiota.",
publisher = "Wiley-Blackwell",
journal = "Scandinavian Journal of Immunology",
title = "Selectivity of polyclonal repertoire of anti‐microbial IgA and its subclasses in saliva and serum in humans",
number = "6",
pages = "e13223",
volume = "96",
doi = "10.1111/sji.13223"
}

Nikodijević, S., Blagojević, V., Ćuruvija, I., Kosanović, D., Đukić, T., Đorđević, B., Ilić, V.,& Minić, R.. (2022). Selectivity of polyclonal repertoire of anti‐microbial IgA and its subclasses in saliva and serum in humans. in Scandinavian Journal of Immunology
Wiley-Blackwell., 96(6), e13223.
https://doi.org/10.1111/sji.13223

Nikodijević S, Blagojević V, Ćuruvija I, Kosanović D, Đukić T, Đorđević B, Ilić V, Minić R. Selectivity of polyclonal repertoire of anti‐microbial IgA and its subclasses in saliva and serum in humans. in Scandinavian Journal of Immunology. 2022;96(6):e13223.
doi:10.1111/sji.13223 .

Nikodijević, Slavomir, Blagojević, Veljko, Ćuruvija, Ivana, Kosanović, Dejana, Đukić, Tamara, Đorđević, Brižita, Ilić, Vesna, Minić, Rajna, "Selectivity of polyclonal repertoire of anti‐microbial IgA and its subclasses in saliva and serum in humans" in Scandinavian Journal of Immunology, 96, no. 6 (2022):e13223,
https://doi.org/10.1111/sji.13223 . .