Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer
Autori
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
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
α-Gal / transcytosis / glycoprotein / glycans / Caco-2 cells / mammalian meat allergyIzvor:
International Journal of Molecular Sciences, 2020, 21, 16, 5742-Izdavač:
- MDPI
Finansiranje / projekti:
- 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).
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200168 (Univerzitet u Beogradu, Hemijski fakultet) (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
Kolekcije
Institucija/grupa
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 . .