Cited by 78Glycosylation and Glycoproteins ResearchGalectins and Cancer BiologyToxin Mechanisms and Immunotoxins

Lectin-mediated bioadhesion: binding characteristics of plant lectins on the enterocyte-like cell lines Caco-2, HT-29 and HCT-8

Gabor, Franz, Stangl, Martina, Wirth, Michael·1998·Journal of Controlled Release

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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Crossref · 10.1016/s0168-3659(98)00043-1

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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WGA [120] and AAL are nontoxic and highly resistant against gastric digestion [Diesner SC, Schultz C, Wang X-Y et al., Unpublished Data] and enhance the retention time and transepithelial transport of MPs at the GI mucosa, finally resulting in improved efficacy, as reviewed by Des Rieux et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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