Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation
2018
Аутори
Peruško, Marijavan Roest, Manon
Stanić-Vučinić, Dragana
Simons, Peter J.
Pieters, Raymond
Ćirković-Veličković, Tanja
Smit, Joost
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 d...egraded 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.
Кључне речи:
beta-lactoglobulin / food allergens / food processing / Maillard reaction / uptake and degradation by DCsИзвор:
Molecular Nutrition and Food Research, 2018, 62, 17Издавач:
- Wiley, Hoboken
Финансирање / пројекти:
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-MESTD-Basic Research (BR or ON)-172024)
- COST Action [FA1402]
DOI: 10.1002/mnfr.201800341
ISSN: 1613-4125
PubMed: 30004175
WoS: 000443583100008
Scopus: 2-s2.0-85052760162
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - 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 - https://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", 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. in 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. in Molecular Nutrition and Food Research. 2018;62(17). doi:10.1002/mnfr.201800341 .
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" in Molecular Nutrition and Food Research, 62, no. 17 (2018), https://doi.org/10.1002/mnfr.201800341 . .