Smit, Joost

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  • Smit, Joost (14)
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Author's Bibliography

Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model

Nešić, Andrijana; Stam, Annemarie; Čavić, Milena; Ten Klooster, Jean Paul; Pieters, Raymond; Smit, Joost; Gavrović-Jankulović, Marija

(2019)

TY  - JOUR
AU  - Nešić, Andrijana
AU  - Stam, Annemarie
AU  - Čavić, Milena
AU  - Ten Klooster, Jean Paul
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2019
UR  - https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071845404&doi=10.1016%2fj.jff.2019.103556&partnerID=40&md5=c210fd8346babe18cc93e9b0994c4a1e
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3485
AB  - In this study, two intestinal models were employed to assess the modulatory potential of a major kiwifruit allergen on the innate immunity of epithelial cells. Effects of Act d 1 were analyzed in terms of gene expression and structural changes of tight junction (TJ) proteins, as well as up-regulation of pro-inflammatory cytokines in Caco-2 cells and, for the first time, in mouse-derived intestinal 2-dimensional (2D) organoids.

Biologically active Act d 1 induced up-regulation of TJ genes for CLDN-2, CLDN-3, CLDN-4, ZO-1, and on the protein level induced release of pro-inflammatory cytokines IL-1β, TNFα and IL-33 in both employed model systems. In 2D-organoids, active Act d 1 impaired the TJ protein networks of E-cadherin, claudin-3, and ZO-1.

2D-organoids generated from mouse intestine are a promising new model system for the assessment of allergen-induced intestinal cell responses and a useful tool for mitigation of risks associated with novel food proteins.
T2  - Journal of Functional Foods
T1  - Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model
VL  - 62
DO  - 10.1016/j.jff.2019.103556
ER  - 
@article{
author = "Nešić, Andrijana and Stam, Annemarie and Čavić, Milena and Ten Klooster, Jean Paul and Pieters, Raymond and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2019",
url = "https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071845404&doi=10.1016%2fj.jff.2019.103556&partnerID=40&md5=c210fd8346babe18cc93e9b0994c4a1e, http://cherry.chem.bg.ac.rs/handle/123456789/3485",
abstract = "In this study, two intestinal models were employed to assess the modulatory potential of a major kiwifruit allergen on the innate immunity of epithelial cells. Effects of Act d 1 were analyzed in terms of gene expression and structural changes of tight junction (TJ) proteins, as well as up-regulation of pro-inflammatory cytokines in Caco-2 cells and, for the first time, in mouse-derived intestinal 2-dimensional (2D) organoids.

Biologically active Act d 1 induced up-regulation of TJ genes for CLDN-2, CLDN-3, CLDN-4, ZO-1, and on the protein level induced release of pro-inflammatory cytokines IL-1β, TNFα and IL-33 in both employed model systems. In 2D-organoids, active Act d 1 impaired the TJ protein networks of E-cadherin, claudin-3, and ZO-1.

2D-organoids generated from mouse intestine are a promising new model system for the assessment of allergen-induced intestinal cell responses and a useful tool for mitigation of risks associated with novel food proteins.",
journal = "Journal of Functional Foods",
title = "Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model",
volume = "62",
doi = "10.1016/j.jff.2019.103556"
}
Nešić, A., Stam, A., Čavić, M., Ten Klooster, J. P., Pieters, R., Smit, J.,& Gavrović-Jankulović, M. (2019). Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model.
Journal of Functional Foods, 62.
https://doi.org/10.1016/j.jff.2019.103556
Nešić A, Stam A, Čavić M, Ten Klooster JP, Pieters R, Smit J, Gavrović-Jankulović M. Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model. Journal of Functional Foods. 2019;62
Nešić Andrijana, Stam Annemarie, Čavić Milena, Ten Klooster Jean Paul, Pieters Raymond, Smit Joost, Gavrović-Jankulović Marija, "Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model" Journal of Functional Foods, 62 (2019),
https://doi.org/10.1016/j.jff.2019.103556 .
2
1
1

The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines

Nešić, Andrijana N.; Čavić, Milena; Popović, Milica; Zlatanova, Milena; Pieters, Raymond; Smit, Joost; Gavrović-Jankulović, Marija

(MDPI, 2019)

TY  - JOUR
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Popović, Milica
AU  - Zlatanova, Milena
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3799
AB  - Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to explore its potential to activate the NF-ĸB signaling pathway and to regulate expression of epithelial pro-allergenic cytokines. Influences of Act d 1 on TJP gene expression and pro-allergenic cytokines in the mouse intestine was analyzed by qPCR upon allergen administration by oral gavage. The effect on the in vivo intestinal permeability was assessed in ELISA by measuring the translocation of β-lactoglobulin (BLG) into circulation. The capacity of Act d 1 to activate the NF-ĸB pathway was tested in HEK293 cells by fluorescent microscopy and flow cytometry. Administration of Actinidin (Act d 1) increased intestinal permeability to the BLG. This was accompanied by changes in gene expression of TJP mRNA and pro-allergenic cytokines IL-25, IL-33, and thymic stromal lymphopoietin (TSLP) compared to the control. Act d 1 reduced TEER of the HEK293 monolayer, was positive in an NF-ĸB-reporter HEK293 cell assay, and induced secretion of TSLP. These findings shed more light on the molecular events in the sensitization process of kiwifruit but possibly also of other protease food allergens.
PB  - MDPI
T2  - Biomolecules
T1  - The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines
VL  - 9
IS  - 12
SP  - 816
DO  - 10.3390/biom9120816
ER  - 
@article{
author = "Nešić, Andrijana N. and Čavić, Milena and Popović, Milica and Zlatanova, Milena and Pieters, Raymond and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3799",
abstract = "Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to explore its potential to activate the NF-ĸB signaling pathway and to regulate expression of epithelial pro-allergenic cytokines. Influences of Act d 1 on TJP gene expression and pro-allergenic cytokines in the mouse intestine was analyzed by qPCR upon allergen administration by oral gavage. The effect on the in vivo intestinal permeability was assessed in ELISA by measuring the translocation of β-lactoglobulin (BLG) into circulation. The capacity of Act d 1 to activate the NF-ĸB pathway was tested in HEK293 cells by fluorescent microscopy and flow cytometry. Administration of Actinidin (Act d 1) increased intestinal permeability to the BLG. This was accompanied by changes in gene expression of TJP mRNA and pro-allergenic cytokines IL-25, IL-33, and thymic stromal lymphopoietin (TSLP) compared to the control. Act d 1 reduced TEER of the HEK293 monolayer, was positive in an NF-ĸB-reporter HEK293 cell assay, and induced secretion of TSLP. These findings shed more light on the molecular events in the sensitization process of kiwifruit but possibly also of other protease food allergens.",
publisher = "MDPI",
journal = "Biomolecules",
title = "The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines",
volume = "9",
number = "12",
pages = "816",
doi = "10.3390/biom9120816"
}
Nešić, A. N., Čavić, M., Popović, M., Zlatanova, M., Pieters, R., Smit, J.,& Gavrović-Jankulović, M. (2019). The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines.
Biomolecules
MDPI., 9(12), 816.
https://doi.org/10.3390/biom9120816
Nešić AN, Čavić M, Popović M, Zlatanova M, Pieters R, Smit J, Gavrović-Jankulović M. The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines. Biomolecules. 2019;9(12):816
Nešić Andrijana N., Čavić Milena, Popović Milica, Zlatanova Milena, Pieters Raymond, Smit Joost, Gavrović-Jankulović Marija, "The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines" Biomolecules, 9, no. 12 (2019):816,
https://doi.org/10.3390/biom9120816 .
1
3
2

Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - BOOK
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3205
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341
ER  - 
@book{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3205",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J. (2018). Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341.
Molecular Nutrition and Food Research
Wiley, Hoboken..
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341. Molecular Nutrition and Food Research. 2018;
Peruško Marija, van Roest Manon, Stanić-Vučinić Dragana, Simons Peter J., Pieters Raymond, Ćirković-Veličković Tanja, Smit Joost, "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341" Molecular Nutrition and Food Research (2018)

Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2212
AB  - Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation
VL  - 62
IS  - 17
DO  - 10.1002/mnfr.201800341
ER  - 
@article{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2212",
abstract = "Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation",
volume = "62",
number = "17",
doi = "10.1002/mnfr.201800341"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J. (2018). Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.
Molecular Nutrition and Food Research
Wiley, Hoboken., 62(17).
https://doi.org/10.1002/mnfr.201800341
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research. 2018;62(17)
Peruško Marija, van Roest Manon, Stanić-Vučinić Dragana, Simons Peter J., Pieters Raymond, Ćirković-Veličković Tanja, Smit Joost, "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation" Molecular Nutrition and Food Research, 62, no. 17 (2018),
https://doi.org/10.1002/mnfr.201800341 .
2
14
11
12

Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a

Mihajlović-Lalić, Ljiljana; Radosavljević, Jelena; Nordlund, Emilia; Krstić-Ristivojević, Maja; Bohn, Torsten; Smit, Joost; Buchert, Johanna; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - BOOK
AU  - Mihajlović-Lalić, Ljiljana
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3591
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a
ER  - 
@book{
author = "Mihajlović-Lalić, Ljiljana and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3591",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a"
}
Mihajlović-Lalić, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T. (2016). Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a.
Food and Function
Royal Soc Chemistry, Cambridge..
Mihajlović-Lalić L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a. Food and Function. 2016;
Mihajlović-Lalić Ljiljana, Radosavljević Jelena, Nordlund Emilia, Krstić-Ristivojević Maja, Bohn Torsten, Smit Joost, Buchert Johanna, Ćirković-Veličković Tanja, "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a" Food and Function (2016)

Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions

Grozdanović, Milica M.; Čavić, Milena; Nešić, Andrijana N.; Anđelković, Uroš; Akbari, Peyman; Smit, Joost; Gavrović-Jankulović, Marija

(Elsevier Science Bv, Amsterdam, 2016)

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Čavić, Milena
AU  - Nešić, Andrijana N.
AU  - Anđelković, Uroš
AU  - Akbari, Peyman
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3559
AB  - Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions
VL  - 1860
IS  - 3
SP  - 516
EP  - 526
DO  - 10.1016/j.bbagen.2015.12.005
ER  - 
@article{
author = "Grozdanović, Milica M. and Čavić, Milena and Nešić, Andrijana N. and Anđelković, Uroš and Akbari, Peyman and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3559",
abstract = "Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions",
volume = "1860",
number = "3",
pages = "516-526",
doi = "10.1016/j.bbagen.2015.12.005"
}
Grozdanović, M. M., Čavić, M., Nešić, A. N., Anđelković, U., Akbari, P., Smit, J.,& Gavrović-Jankulović, M. (2016). Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions.
Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1860(3), 516-526.
https://doi.org/10.1016/j.bbagen.2015.12.005
Grozdanović MM, Čavić M, Nešić AN, Anđelković U, Akbari P, Smit J, Gavrović-Jankulović M. Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions. Biochimica et Biophysica Acta: General Subjects. 2016;1860(3):516-526
Grozdanović Milica M., Čavić Milena, Nešić Andrijana N., Anđelković Uroš, Akbari Peyman, Smit Joost, Gavrović-Jankulović Marija, "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions" Biochimica et Biophysica Acta: General Subjects, 1860, no. 3 (2016):516-526,
https://doi.org/10.1016/j.bbagen.2015.12.005 .
4
21
18
21

Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions

Grozdanović, Milica M.; Čavić, Milena; Nešić, Andrijana N.; Anđelković, Uroš; Akbari, Peyman; Smit, Joost; Gavrović-Jankulović, Marija

(Elsevier Science Bv, Amsterdam, 2016)

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Čavić, Milena
AU  - Nešić, Andrijana N.
AU  - Anđelković, Uroš
AU  - Akbari, Peyman
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2039
AB  - Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions
VL  - 1860
IS  - 3
SP  - 516
EP  - 526
DO  - 10.1016/j.bbagen.2015.12.005
ER  - 
@article{
author = "Grozdanović, Milica M. and Čavić, Milena and Nešić, Andrijana N. and Anđelković, Uroš and Akbari, Peyman and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2039",
abstract = "Background: The intestinal epithelium forms a barrier that food allergens must cross in order to induce sensitization. The aim of this study was to evaluate the impact of the plant-derived food cysteine protease - actinidin (Act d1) on the integrity of intestinal epithelium tight junctions (TJs). Methods: Effects of Act d1 on the intestinal epithelium were evaluated in Caco-2 monolayers and in a mouse model by measuring transepithelial resistance and in vivo permeability. Integrity of the tight junctions was analyzed by confocal microscopy. Proteolysis of TJ protein occludin was evaluated by mass spectrometry. Results: Actinidin (1 mg/mL) reduced the transepithelial resistance of the cell monolayer by 18.1% (after 1 h) and 25.6% (after 4 h). This loss of barrier function was associated with Act d 1 disruption of the occludin and zonula occludens (ZO)-1 network. The effect on intestinal permeability in vivo was demonstrated by the significantly higher concentration of 40 kDa FITC-dextran (233 mu g/mL) that passed from the intestine into the serum of Act d1 treated mice in comparison to the control group (0.5 mu g/mL). Human occludin was fragmented, and putative Act d1 cleavage sites were identified in extracellular loops of human occludin. Conclusion: Act d1 caused protease-dependent disruption of tight junctions in confluent Caco-2 cells and increased intestinal permeability in mice. General significance: In line with the observed effects of food cysteine proteases in occupational allergy, these results suggest that disruption of tight junctions by food cysteine proteases may contribute to the process of sensitization in food allergy. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions",
volume = "1860",
number = "3",
pages = "516-526",
doi = "10.1016/j.bbagen.2015.12.005"
}
Grozdanović, M. M., Čavić, M., Nešić, A. N., Anđelković, U., Akbari, P., Smit, J.,& Gavrović-Jankulović, M. (2016). Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions.
Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1860(3), 516-526.
https://doi.org/10.1016/j.bbagen.2015.12.005
Grozdanović MM, Čavić M, Nešić AN, Anđelković U, Akbari P, Smit J, Gavrović-Jankulović M. Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions. Biochimica et Biophysica Acta: General Subjects. 2016;1860(3):516-526
Grozdanović Milica M., Čavić Milena, Nešić Andrijana N., Anđelković Uroš, Akbari Peyman, Smit Joost, Gavrović-Jankulović Marija, "Kiwifruit cysteine protease actinidin compromises the intestinal barrier by disrupting tight junctions" Biochimica et Biophysica Acta: General Subjects, 1860, no. 3 (2016):516-526,
https://doi.org/10.1016/j.bbagen.2015.12.005 .
4
21
18
20

Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase

Mihajlović-Lalić, Ljiljana; Radosavljević, Jelena; Nordlund, Emilia; Krstić-Ristivojević, Maja; Bohn, Torsten; Smit, Joost; Buchert, Johanna; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - JOUR
AU  - Mihajlović-Lalić, Ljiljana
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2254
AB  - Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase
VL  - 7
IS  - 5
SP  - 2357
EP  - 2366
DO  - 10.1039/c5fo01325a
ER  - 
@article{
author = "Mihajlović-Lalić, Ljiljana and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2254",
abstract = "Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase",
volume = "7",
number = "5",
pages = "2357-2366",
doi = "10.1039/c5fo01325a"
}
Mihajlović-Lalić, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T. (2016). Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase.
Food and Function
Royal Soc Chemistry, Cambridge., 7(5), 2357-2366.
https://doi.org/10.1039/c5fo01325a
Mihajlović-Lalić L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase. Food and Function. 2016;7(5):2357-2366
Mihajlović-Lalić Ljiljana, Radosavljević Jelena, Nordlund Emilia, Krstić-Ristivojević Maja, Bohn Torsten, Smit Joost, Buchert Johanna, Ćirković-Veličković Tanja, "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase" Food and Function, 7, no. 5 (2016):2357-2366,
https://doi.org/10.1039/c5fo01325a .
2
8
4
7

Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy

Radosavljević, Jelena; Nordlund, Emilia; Mihajlovic, Luka; Krstić-Ristivojević, Maja; Bohn, Torsten; Buchert, Johanna; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley-Blackwell, Hoboken, 2014)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Mihajlovic, Luka
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1510
AB  - ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy
VL  - 58
IS  - 3
SP  - 635
EP  - 646
DO  - 10.1002/mnfr.201300403
ER  - 
@article{
author = "Radosavljević, Jelena and Nordlund, Emilia and Mihajlovic, Luka and Krstić-Ristivojević, Maja and Bohn, Torsten and Buchert, Johanna and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1510",
abstract = "ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy",
volume = "58",
number = "3",
pages = "635-646",
doi = "10.1002/mnfr.201300403"
}
Radosavljević, J., Nordlund, E., Mihajlovic, L., Krstić-Ristivojević, M., Bohn, T., Buchert, J., Ćirković-Veličković, T.,& Smit, J. (2014). Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy.
Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 58(3), 635-646.
https://doi.org/10.1002/mnfr.201300403
Radosavljević J, Nordlund E, Mihajlovic L, Krstić-Ristivojević M, Bohn T, Buchert J, Ćirković-Veličković T, Smit J. Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. Molecular Nutrition and Food Research. 2014;58(3):635-646
Radosavljević Jelena, Nordlund Emilia, Mihajlovic Luka, Krstić-Ristivojević Maja, Bohn Torsten, Buchert Johanna, Ćirković-Veličković Tanja, Smit Joost, "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy" Molecular Nutrition and Food Research, 58, no. 3 (2014):635-646,
https://doi.org/10.1002/mnfr.201300403 .
8
24
22
24

Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome

Stojadinović, Marija M.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2014)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1755
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome
VL  - 281
SP  - 98
EP  - 98
ER  - 
@conference{
author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1755",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome",
volume = "281",
pages = "98-98"
}
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2014). Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 281, 98-98.
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome. FEBS Journal / Federation of European of Biochemical Societies. 2014;281:98-98
Stojadinović Marija M., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome" FEBS Journal / Federation of European of Biochemical Societies, 281 (2014):98-98

Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing

Stojadinović, Marija M.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Oxford Univ Press, Oxford, 2014)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1823
AB  - Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.
PB  - Oxford Univ Press, Oxford
T2  - Toxicological Sciences
T1  - Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing
VL  - 140
IS  - 1
SP  - 224
EP  - 235
DO  - 10.1093/toxsci/kfu062
ER  - 
@article{
author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1823",
abstract = "Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.",
publisher = "Oxford Univ Press, Oxford",
journal = "Toxicological Sciences",
title = "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing",
volume = "140",
number = "1",
pages = "224-235",
doi = "10.1093/toxsci/kfu062"
}
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2014). Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing.
Toxicological Sciences
Oxford Univ Press, Oxford., 140(1), 224-235.
https://doi.org/10.1093/toxsci/kfu062
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing. Toxicological Sciences. 2014;140(1):224-235
Stojadinović Marija M., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing" Toxicological Sciences, 140, no. 1 (2014):224-235,
https://doi.org/10.1093/toxsci/kfu062 .
2
39
33
38

Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin

Stojadinović, Marija M.; Ćirković-Veličković, Tanja; Pieters, Raymond; Smit, Joost

(Wiley-Blackwell, Hoboken, 2013)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Ćirković-Veličković, Tanja
AU  - Pieters, Raymond
AU  - Smit, Joost
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1417
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin
VL  - 280
SP  - 467
EP  - 467
ER  - 
@conference{
author = "Stojadinović, Marija M. and Ćirković-Veličković, Tanja and Pieters, Raymond and Smit, Joost",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1417",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin",
volume = "280",
pages = "467-467"
}
Stojadinović, M. M., Ćirković-Veličković, T., Pieters, R.,& Smit, J. (2013). Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 280, 467-467.
Stojadinović MM, Ćirković-Veličković T, Pieters R, Smit J. Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin. FEBS Journal / Federation of European of Biochemical Societies. 2013;280:467-467
Stojadinović Marija M., Ćirković-Veličković Tanja, Pieters Raymond, Smit Joost, "Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin" FEBS Journal / Federation of European of Biochemical Societies, 280 (2013):467-467

Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding

Mihajlović-Lalić, Ljiljana; Radosavljević, Jelena; Nordlund, Emilia; Smit, Joost; Buchert, Johanna; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2011)

TY  - CONF
AU  - Mihajlović-Lalić, Ljiljana
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1592
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding
VL  - 66
SP  - 536
EP  - 536
ER  - 
@conference{
author = "Mihajlović-Lalić, Ljiljana and Radosavljević, Jelena and Nordlund, Emilia and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2011",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1592",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding",
volume = "66",
pages = "536-536"
}
Mihajlović-Lalić, L., Radosavljević, J., Nordlund, E., Smit, J., Buchert, J.,& Ćirković-Veličković, T. (2011). Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding.
Allergy
Wiley-Blackwell, Hoboken., 66, 536-536.
Mihajlović-Lalić L, Radosavljević J, Nordlund E, Smit J, Buchert J, Ćirković-Veličković T. Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding. Allergy. 2011;66:536-536
Mihajlović-Lalić Ljiljana, Radosavljević Jelena, Nordlund Emilia, Smit Joost, Buchert Johanna, Ćirković-Veličković Tanja, "Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding" Allergy, 66 (2011):536-536

Allergenic potential of cross-linked peanut proteins

Radosavljević, Jelena; Luka, M.; Karina, W.; Emilia, S.; Johanna, B.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2010)

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Luka, M.
AU  - Karina, W.
AU  - Emilia, S.
AU  - Johanna, B.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1470
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Allergenic potential of cross-linked peanut proteins
VL  - 65
SP  - 403
EP  - 403
ER  - 
@conference{
author = "Radosavljević, Jelena and Luka, M. and Karina, W. and Emilia, S. and Johanna, B. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2010",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1470",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Allergenic potential of cross-linked peanut proteins",
volume = "65",
pages = "403-403"
}
Radosavljević, J., Luka, M., Karina, W., Emilia, S., Johanna, B., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2010). Allergenic potential of cross-linked peanut proteins.
Allergy
Wiley-Blackwell, Hoboken., 65, 403-403.
Radosavljević J, Luka M, Karina W, Emilia S, Johanna B, Pieters R, Smit J, Ćirković-Veličković T. Allergenic potential of cross-linked peanut proteins. Allergy. 2010;65:403-403
Radosavljević Jelena, Luka M., Karina W., Emilia S., Johanna B., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Allergenic potential of cross-linked peanut proteins" Allergy, 65 (2010):403-403