ArticleInternational journal of molecular sciences2020
Alpha-Gal on the Protein Surface Hampers Transcytosis through the Caco-2 Monolayer.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 8 citations in OpenAlex.
- ImmunoCAP-Based Detection of Alpha-Gal Syndrome: A Reproducible Diagnostic Protocol for Human Patients.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Probing the genomic and proteomic basis of encystment inmSystems · 2026Article
- Alpha-Gal syndrome unveiled: decoding the glycan-driven red meat allergy.Glycoconjugate journal · 2026Review
- Linear Epitope-Mediated Immunological Cross-Reactivity in Livestock Product Allergens.International journal of molecular sciences · 2026Review
- Immunologic comparison of alpha-gal sensitized and non-sensitized groups from a community based sample.Frontiers in immunology · 2026Article
- Ticked Off: Allergic Effector Cells in the Pathogenesis of Alpha-gal Syndrome.Current allergy and asthma reports · 2025Review
- The α-Gal epitope - the cause of a global allergic disease.Frontiers in immunology · 2024Review
- Where's the Beef? Understanding Allergic Responses to Red Meat in Alpha-Gal Syndrome.Journal of immunology (Baltimore, Md. : 1950) · 2022Review
- The Meat of the Matter: Understanding and Managing Alpha-Gal Syndrome.ImmunoTargets and therapy · 2022Review
- The α-Gal Syndrome and Potential Mechanisms.Frontiers in allergy · 2021Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.