Ćirković-Veličković, Tanja

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  • Ćirković-Veličković, Tanja (3)

Author's Bibliography

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija M.; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/4169
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
EP  - 658
SP  - 644
VL  - 126
DO  - 10.1016/j.envint.2019.03.001
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija M. and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
pages = "658-644",
volume = "126",
doi = "10.1016/j.envint.2019.03.001"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L. M.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Pergamon-Elsevier Science Ltd, Oxford., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer LM, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija M., Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 . .
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Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion

Polović, Natalija; Pjanović, Rada; Burazer, Lidija M.; Veličković, Sava; Jankov, Ratko; Ćirković-Veličković, Tanja

(John Wiley & Sons Ltd, Chichester, 2009)

TY  - JOUR
AU  - Polović, Natalija
AU  - Pjanović, Rada
AU  - Burazer, Lidija M.
AU  - Veličković, Sava
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/1488
AB  - BACKGROUND: It is thought that food sensitisers must be able to reach the intestine in order to sensitise patients. Pectin is a gel-forming plant polysaccharide that can protect allergens from in vivo gastric digestion and in vitro pepsin digestion. The aim of this study was to examine if pectin gel formed in the acidic environment of the stomach can protect labile allergen from in vitro gastrointestinal digestion. RESULTS: Pectin forms a gel in the acidic conditions of gastric fluid up to a concentration of 1.0 +/- 0.14 g L(-1). Four allergenic fruits (kiwi, cherry, apple and banana) form gels in the same manner at the dilutions 14.8 +/- 0.4; 8.4 +/- 0.2, 9.4 +/- 0.35 and 29.1 +/- 0.2, respectively. The time necessary for dissolution of 50 g L(-1) pectin gel in intestinal fluid was found to be 70 +/- 0.2 min. Pectin gel formed in situ was able to protect Act c 1 from pepsin digestion for 1 h and from further intestinal digestion for one additional hour. CONCLUSION: Pectin gel in an acidic environment protects Act c 1 from pepsin digestion and dissolves slowly in the slightly basic environment of the intestine allowing the survival of fruit allergen for additional time and possible interaction with the gut immune system.
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion
EP  - 14
IS  - 1
SP  - 8
VL  - 89
DO  - 10.1002/jsfa.3404
ER  - 
@article{
author = "Polović, Natalija and Pjanović, Rada and Burazer, Lidija M. and Veličković, Sava and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "BACKGROUND: It is thought that food sensitisers must be able to reach the intestine in order to sensitise patients. Pectin is a gel-forming plant polysaccharide that can protect allergens from in vivo gastric digestion and in vitro pepsin digestion. The aim of this study was to examine if pectin gel formed in the acidic environment of the stomach can protect labile allergen from in vitro gastrointestinal digestion. RESULTS: Pectin forms a gel in the acidic conditions of gastric fluid up to a concentration of 1.0 +/- 0.14 g L(-1). Four allergenic fruits (kiwi, cherry, apple and banana) form gels in the same manner at the dilutions 14.8 +/- 0.4; 8.4 +/- 0.2, 9.4 +/- 0.35 and 29.1 +/- 0.2, respectively. The time necessary for dissolution of 50 g L(-1) pectin gel in intestinal fluid was found to be 70 +/- 0.2 min. Pectin gel formed in situ was able to protect Act c 1 from pepsin digestion for 1 h and from further intestinal digestion for one additional hour. CONCLUSION: Pectin gel in an acidic environment protects Act c 1 from pepsin digestion and dissolves slowly in the slightly basic environment of the intestine allowing the survival of fruit allergen for additional time and possible interaction with the gut immune system.",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion",
pages = "14-8",
number = "1",
volume = "89",
doi = "10.1002/jsfa.3404"
}
Polović, N., Pjanović, R., Burazer, L. M., Veličković, S., Jankov, R.,& Ćirković-Veličković, T.. (2009). Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 89(1), 8-14.
https://doi.org/10.1002/jsfa.3404
Polović N, Pjanović R, Burazer LM, Veličković S, Jankov R, Ćirković-Veličković T. Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion. in Journal of the Science of Food and Agriculture. 2009;89(1):8-14.
doi:10.1002/jsfa.3404 .
Polović, Natalija, Pjanović, Rada, Burazer, Lidija M., Veličković, Sava, Jankov, Ratko, Ćirković-Veličković, Tanja, "Acid-formed pectin gel delays major incomplete kiwi fruit allergen Act c 1 proteolysis in in vitro gastrointestinal digestion" in Journal of the Science of Food and Agriculture, 89, no. 1 (2009):8-14,
https://doi.org/10.1002/jsfa.3404 . .
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Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics

Prodanović, Radivoje; Milosavic, Nenad B.; Jovanović, Slobodan; Ćirković-Veličković, Tanja; Vujčić, Zoran; Jankov, Ratko M.

(Serbian Chemical Soc, Belgrade, 2006)

TY  - JOUR
AU  - Prodanović, Radivoje
AU  - Milosavic, Nenad B.
AU  - Jovanović, Slobodan
AU  - Ćirković-Veličković, Tanja
AU  - Vujčić, Zoran
AU  - Jankov, Ratko M.
PY  - 2006
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/5458
AB  - alpha-Glucosidase from baker's yeast was immobilized on macroporous copolymers of ethylene glycol dimethacrylate and glycidyl methacrylate, poly(GMA-co-EGDMA), with various surface characteristics and pore sizes ranging from 44 nm to 270 nm. Immobilization was done by glutaraldehyde on the copolymer previously modified with 1,2-diaminoethane. The specific activity of the obtained immobilized enzyme varied from 27 to 81 U/g depending on the employed copolymer. The half lives of the immobilized enzyme in cosolvents were influenced by the surface characteristics of the copolymer, ranging from 60 to 150 min in 35 % methanol and from 10 to 44 min in 45 % dimethyl sulphoxide (DMSO). The best stabilities were obtained when the enzyme was immobilized onto a copolymer having a pore size of 48 rim in methanol and 270 nm in DMSO.
AB  - α-Glukozidaza izolovana iz pekarskog kvasca je imobilizovana na makroporoznim glicidil-metakrilatima različitih površinskih karakteristika i veličina pora od 44 do 270 nm. Imobilizacija je izvedena glutaraldehidom na polimeru prethodno modifikovanom sa 1,2-diaminoetanom. Specifična aktivnost dobijenog imobilizovanog enzima je varirala od 27 do 81U/g u zavisnosti od vrste korišćenog polimera. Poluživoti imobilizovanog enzima u korastvaračima su zavisili od površinskih karakteristika polimera i kretali su se u opsegu od 60 do 150 min u 35%(v/v) metanolu i od 10 do 44 min u 45 % (v/v) dimetilsufoksidu. Najveća stabilnost u metanolu je dobijena imobilizacijom enzima na polimeru sa veličinom pora od 48 nm a u dimetilsulfoksidu na polimeru sa veličinom pora od 270 nm.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics
T1  - Stabilizacija α-glukozidaze u organskim rastvaračima imobilizacijom na makroporoznim (poli) glicidil metakrilatima različitih površinskih karakteristika
EP  - 347
IS  - 4
SP  - 339
VL  - 71
DO  - 10.2298/JSC0604339P
ER  - 
@article{
author = "Prodanović, Radivoje and Milosavic, Nenad B. and Jovanović, Slobodan and Ćirković-Veličković, Tanja and Vujčić, Zoran and Jankov, Ratko M.",
year = "2006",
abstract = "alpha-Glucosidase from baker's yeast was immobilized on macroporous copolymers of ethylene glycol dimethacrylate and glycidyl methacrylate, poly(GMA-co-EGDMA), with various surface characteristics and pore sizes ranging from 44 nm to 270 nm. Immobilization was done by glutaraldehyde on the copolymer previously modified with 1,2-diaminoethane. The specific activity of the obtained immobilized enzyme varied from 27 to 81 U/g depending on the employed copolymer. The half lives of the immobilized enzyme in cosolvents were influenced by the surface characteristics of the copolymer, ranging from 60 to 150 min in 35 % methanol and from 10 to 44 min in 45 % dimethyl sulphoxide (DMSO). The best stabilities were obtained when the enzyme was immobilized onto a copolymer having a pore size of 48 rim in methanol and 270 nm in DMSO., α-Glukozidaza izolovana iz pekarskog kvasca je imobilizovana na makroporoznim glicidil-metakrilatima različitih površinskih karakteristika i veličina pora od 44 do 270 nm. Imobilizacija je izvedena glutaraldehidom na polimeru prethodno modifikovanom sa 1,2-diaminoetanom. Specifična aktivnost dobijenog imobilizovanog enzima je varirala od 27 do 81U/g u zavisnosti od vrste korišćenog polimera. Poluživoti imobilizovanog enzima u korastvaračima su zavisili od površinskih karakteristika polimera i kretali su se u opsegu od 60 do 150 min u 35%(v/v) metanolu i od 10 do 44 min u 45 % (v/v) dimetilsufoksidu. Najveća stabilnost u metanolu je dobijena imobilizacijom enzima na polimeru sa veličinom pora od 48 nm a u dimetilsulfoksidu na polimeru sa veličinom pora od 270 nm.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics, Stabilizacija α-glukozidaze u organskim rastvaračima imobilizacijom na makroporoznim (poli) glicidil metakrilatima različitih površinskih karakteristika",
pages = "347-339",
number = "4",
volume = "71",
doi = "10.2298/JSC0604339P"
}
Prodanović, R., Milosavic, N. B., Jovanović, S., Ćirković-Veličković, T., Vujčić, Z.,& Jankov, R. M.. (2006). Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 71(4), 339-347.
https://doi.org/10.2298/JSC0604339P
Prodanović R, Milosavic NB, Jovanović S, Ćirković-Veličković T, Vujčić Z, Jankov RM. Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics. in Journal of the Serbian Chemical Society. 2006;71(4):339-347.
doi:10.2298/JSC0604339P .
Prodanović, Radivoje, Milosavic, Nenad B., Jovanović, Slobodan, Ćirković-Veličković, Tanja, Vujčić, Zoran, Jankov, Ratko M., "Stabilization of alpha-glucosidase in organic solvents by immobilization on macroporous poly(GMA-co-EGDMA) with different surface characteristics" in Journal of the Serbian Chemical Society, 71, no. 4 (2006):339-347,
https://doi.org/10.2298/JSC0604339P . .
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