Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer
Authors
Krstić-Ristivojević, MajaGrundström, Jeanette
Apostolović, Danijela
Radomirović, Mirjana Ž.
Jovanović, Vesna B.
Radoi, Vlad
Kiewiet, M. B. Gea
Vukojević, Vladana
Ćirković-Veličković, Tanja
van Hage, Marianne
Article (Published version)
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Show full item recordAbstract
Transepithelial transport of proteins is an important step in the immune response to food allergens. Mammalian meat allergy is characterized by an IgE response against the carbohydrate moiety galactosyl-α-1,3-galactose (α-Gal) present on mammalian glycoproteins and glycolipids, which causes severe allergic reactions several hours after red meat consumption. The delayed reaction may be related to the processing of α-Gal carrying proteins in the gastrointestinal tract. The aim of this study was to investigate how protein glycosylation by α-Gal affects the susceptibility to gastric digestion and transport through the Caco-2 cell monolayer. We found that α-Gal glycosylation altered protein susceptibility to gastric digestion, where large protein fragments bearing the α-Gal epitope remained for up to 2 h of digestion. Furthermore, α-Gal glycosylation of the protein hampered transcytosis of the protein through the Caco-2 monolayer. α-Gal epitope on the intact protein could be detected in the... endosomal fraction obtained by differential centrifugation of Caco-2 cell lysates. Furthermore, the level of galectin-3 in Caco-2 cells was not affected by the presence of α-Gal glycosylated BSA (bovine serum albumin) (BSA-α-Gal). Taken together, our data add new knowledge and shed light on the digestion and transport of α-Gal glycosylated proteins.
Keywords:
α-Gal / transcytosis / glycoprotein / glycans / Caco-2 cells / mammalian meat allergySource:
International Journal of Molecular Sciences, 2020, 21, 16, 5742-Publisher:
- MDPI
Funding / projects:
- EAACI Fellowship Award for 2015.
- The Swedish Research Council.
- Region Stockholm (ALF project).
- The Swedish Asthma and Allergy Association’s Research Foundation.
- The King Gustaf V 80th Birthday Foundation.
- The Swedish Heart-Lung Foundation.
- The Hesselman Foundation.
- The Konsul Th C Bergh Foundation.
- The Tore Nilson Foundation for Medical Research.
- The Swedish Cancer and Allergy Foundation.
- The Magnus Bergvall Foundation.
- FP7-HEALTH-2013-INNOVATION-1 Project GLORIA (No. 602919).
- Ministry of Science, Technological Development and Innovation of the Republic of Serbia, institutional funding - 200168 (University of Belgrade, Faculty of Chemistry) (RS-MESTD-inst-2020-200168)
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-H2020-810752)
- Serbian Academy of Sciences and Arts Project F-26.
DOI: 10.3390/ijms21165742
ISSN: 1422-0067
WoS: 000565143100001
Scopus: 2-s2.0-85089495029
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Krstić-Ristivojević, Maja AU - Grundström, Jeanette AU - Apostolović, Danijela AU - Radomirović, Mirjana Ž. AU - Jovanović, Vesna B. AU - Radoi, Vlad AU - Kiewiet, M. B. Gea AU - Vukojević, Vladana AU - Ćirković-Veličković, Tanja AU - van Hage, Marianne PY - 2020 UR - http://cherry.chem.bg.ac.rs/handle/123456789/4866 AB - Transepithelial transport of proteins is an important step in the immune response to food allergens. Mammalian meat allergy is characterized by an IgE response against the carbohydrate moiety galactosyl-α-1,3-galactose (α-Gal) present on mammalian glycoproteins and glycolipids, which causes severe allergic reactions several hours after red meat consumption. The delayed reaction may be related to the processing of α-Gal carrying proteins in the gastrointestinal tract. The aim of this study was to investigate how protein glycosylation by α-Gal affects the susceptibility to gastric digestion and transport through the Caco-2 cell monolayer. We found that α-Gal glycosylation altered protein susceptibility to gastric digestion, where large protein fragments bearing the α-Gal epitope remained for up to 2 h of digestion. Furthermore, α-Gal glycosylation of the protein hampered transcytosis of the protein through the Caco-2 monolayer. α-Gal epitope on the intact protein could be detected in the endosomal fraction obtained by differential centrifugation of Caco-2 cell lysates. Furthermore, the level of galectin-3 in Caco-2 cells was not affected by the presence of α-Gal glycosylated BSA (bovine serum albumin) (BSA-α-Gal). Taken together, our data add new knowledge and shed light on the digestion and transport of α-Gal glycosylated proteins. PB - MDPI T2 - International Journal of Molecular Sciences T1 - Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer VL - 21 IS - 16 SP - 5742 DO - 10.3390/ijms21165742 ER -
@article{ author = "Krstić-Ristivojević, Maja and Grundström, Jeanette and Apostolović, Danijela and Radomirović, Mirjana Ž. and Jovanović, Vesna B. and Radoi, Vlad and Kiewiet, M. B. Gea and Vukojević, Vladana and Ćirković-Veličković, Tanja and van Hage, Marianne", year = "2020", abstract = "Transepithelial transport of proteins is an important step in the immune response to food allergens. Mammalian meat allergy is characterized by an IgE response against the carbohydrate moiety galactosyl-α-1,3-galactose (α-Gal) present on mammalian glycoproteins and glycolipids, which causes severe allergic reactions several hours after red meat consumption. The delayed reaction may be related to the processing of α-Gal carrying proteins in the gastrointestinal tract. The aim of this study was to investigate how protein glycosylation by α-Gal affects the susceptibility to gastric digestion and transport through the Caco-2 cell monolayer. We found that α-Gal glycosylation altered protein susceptibility to gastric digestion, where large protein fragments bearing the α-Gal epitope remained for up to 2 h of digestion. Furthermore, α-Gal glycosylation of the protein hampered transcytosis of the protein through the Caco-2 monolayer. α-Gal epitope on the intact protein could be detected in the endosomal fraction obtained by differential centrifugation of Caco-2 cell lysates. Furthermore, the level of galectin-3 in Caco-2 cells was not affected by the presence of α-Gal glycosylated BSA (bovine serum albumin) (BSA-α-Gal). Taken together, our data add new knowledge and shed light on the digestion and transport of α-Gal glycosylated proteins.", publisher = "MDPI", journal = "International Journal of Molecular Sciences", title = "Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer", volume = "21", number = "16", pages = "5742", doi = "10.3390/ijms21165742" }
Krstić-Ristivojević, M., Grundström, J., Apostolović, D., Radomirović, M. Ž., Jovanović, V. B., Radoi, V., Kiewiet, M. B. G., Vukojević, V., Ćirković-Veličković, T.,& van Hage, M.. (2020). Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer. in International Journal of Molecular Sciences MDPI., 21(16), 5742. https://doi.org/10.3390/ijms21165742
Krstić-Ristivojević M, Grundström J, Apostolović D, Radomirović MŽ, Jovanović VB, Radoi V, Kiewiet MBG, Vukojević V, Ćirković-Veličković T, van Hage M. Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer. in International Journal of Molecular Sciences. 2020;21(16):5742. doi:10.3390/ijms21165742 .
Krstić-Ristivojević, Maja, Grundström, Jeanette, Apostolović, Danijela, Radomirović, Mirjana Ž., Jovanović, Vesna B., Radoi, Vlad, Kiewiet, M. B. Gea, Vukojević, Vladana, Ćirković-Veličković, Tanja, van Hage, Marianne, "Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer" in International Journal of Molecular Sciences, 21, no. 16 (2020):5742, https://doi.org/10.3390/ijms21165742 . .