Lectin-mediated bioadhesion: binding characteristics of plant lectins on the enterocyte-like cell lines Caco-2, HT-29 and HCT-8
Abstract
In order to take advantage of the biorecognition between lectins and specific carbohydrates for targeted drug delivery, fluorescein-labelled lectins of different carbohydrate specificities were screened for binding to human colorectal carcinoma cell lines by flow cytometry and confocal microscopy. The lectin-binding rate increased as follows: Dolichos biflorus agglutinin, DBA<peanut agglutinin, PNA<Lens culinaris agglutinin, LCA<Solanum tuberosum lectin, STL<Ulex europaeus isoagglutinin I, UEA-I<wheat germ agglutinin, WGA (Caco-2); PNA<UEA-I<WGA (HT-29); DBA<UEA-I<WGA (HCT-8), thus reflecting the glycosylation pattern of the cells. Compared to the BSA-binding capacity of the cells, the extent of nonspecific binding was strongly dependent on the type of cell line and lectin under investigation being lower than 2% in the case of WGA, STL and UEA-I/Caco-2 and HT-29 cells. Whereas 50% of DBA was bound nonspecifically to Caco-2 cells, the interactions DBA/HCT-8 and PNA/HT-29 were due to nonspecific binding. By competitive inhibition of lectin-adhesion to the cells upon addition of the complementary carbohydrate, specificity of lectin-binding was confirmed except for the interaction of DBA/HCT-8 and PNA/HT-29. Following on from this work, we consider WGA-, STL- and UEA-I-mediated drug delivery to be a promising approach for peroral bioadhesive formulations adhering to absorptive enterocytes.
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WGA and AAL are nontoxic and highly resistant to gastric digestion, and enhance retention time and transepithelial transport of MPs at GI mucosa, improving efficacy.
“The targeting substances WGA [120] and AAL are nontoxic and highly resistant against gastric digestion [Diesner SC, Schultz C, Wang X-Y et al., Unpublished Data] and enhance the retention time and transepithelial transport of MPs at the GI mucosa, finally resulting in improved efficacy, as reviewed by Des Rieux et al. [23].”
From Use of lectin-functionalized particles for oral immunotherapy (2012) · cites this paper as [120]
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References 20 · Cited by 78
- Authors
- Gabor, F., Stangl, M., & Wirth, M.
- Affiliations
- University of Vienna (AT)
- Corresponding author
- Gabor, Franz
- Venue
- Journal of Controlled Release
- Publisher
- Elsevier BV
- Published
- 1998-11
- Volume
- 55
- Issue
- 2-3
- Pages
- 131-142
- ISSN
- 0168-3659 (ISSN-L)
- OpenAlex
- W2004781745
- Cited by
- 78
- References
- 20
- Citations by year
- 2023: 1 · 2022: 1 · 2021: 2 · 2020: 1 · 2018: 4 · 2016: 3 · 2015: 4 · 2014: 4 · 2013: 3 · 2012: 2
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Controlled Release (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
- Life Sciences › Immunology and Microbiology › Immunology › Toxin Mechanisms and Immunotoxins
- Keywords
- lectin binding, plant lectins, bioadhesion, enterocytes, Caco-2 cells, HT-29 cells, HCT-8 cells, colorectal cancer cell lines, targeted drug delivery, carbohydrate specificity, Dolichos biflorus agglutinin, peanut agglutinin, Lens culinaris agglutinin, wheat germ agglutinin
- MeSH terms
- Cell Adhesion, Humans, Intestinal Mucosa, Intestines, Microscopy, Fluorescence, Plants, Protein Binding, Tumor Cells, Cultured, Microscopy, Confocal, Caco-2 Cells, HT29 Cells, Lectins, Plant Lectins
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