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Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer
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 a...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7461108/ https://www.ncbi.nlm.nih.gov/pubmed/32796496 http://dx.doi.org/10.3390/ijms21165742 |
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author | Krstić Ristivojević, Maja Grundström, Jeanette Apostolović, Danijela Radomirović, Mirjana Jovanović, Vesna Radoi, Vlad Kiewiet, M. B. Gea Vukojević, Vladana Ćirković Veličković, Tanja van Hage, Marianne |
author_facet | Krstić Ristivojević, Maja Grundström, Jeanette Apostolović, Danijela Radomirović, Mirjana Jovanović, Vesna Radoi, Vlad Kiewiet, M. B. Gea Vukojević, Vladana Ćirković Veličković, Tanja van Hage, Marianne |
author_sort | Krstić Ristivojević, Maja |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7461108 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-74611082020-09-14 Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer Krstić Ristivojević, Maja Grundström, Jeanette Apostolović, Danijela Radomirović, Mirjana Jovanović, Vesna Radoi, Vlad Kiewiet, M. B. Gea Vukojević, Vladana Ćirković Veličković, Tanja van Hage, Marianne Int J Mol Sci Article 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. MDPI 2020-08-11 /pmc/articles/PMC7461108/ /pubmed/32796496 http://dx.doi.org/10.3390/ijms21165742 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Krstić Ristivojević, Maja Grundström, Jeanette Apostolović, Danijela Radomirović, Mirjana Jovanović, Vesna 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 |
title | Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer |
title_full | Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer |
title_fullStr | Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer |
title_full_unstemmed | Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer |
title_short | Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer |
title_sort | alpha-gal on the protein surface hampers transcytosis through the caco-2 monolayer |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7461108/ https://www.ncbi.nlm.nih.gov/pubmed/32796496 http://dx.doi.org/10.3390/ijms21165742 |
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