Galectin‑3 promotes the adhesion, but not the migration of thyroid carcinoma cells in a β‑galactoside‑specific manner

Winter,Jochen; Glassmann,Alexander; Kraus,Dominik; Frede,Stilla; Veit,Nadine; Probstmeier,Rainer

doi:10.3892/wasj.2021.85

Galectin‑3 promotes the adhesion, but not the migration of thyroid carcinoma cells in a β‑galactoside‑specific manner

Authors:
- Jochen Winter
- Alexander Glassmann
- Dominik Kraus
- Stilla Frede
- Nadine Veit
- Rainer Probstmeier
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Affiliations: Oral Cell Biology Group, Department of Periodontology, Operative and Preventive Dentistry, University of Bonn, 53111 Bonn, Germany, Life Science Inkubator GmbH, 53175 Bonn, Germany, Department of Prosthodontics, Preclinical Education and Material Sciences, University of Bonn, 53111 Bonn, Germany, Department of Anesthesiology and Intensive Care Medicine, University Hospital Bonn, 53127 Bonn, Germany, Neuro‑ and Tumor Cell Biology Group, Department of Nuclear Medicine, University Hospital Bonn, 53127 Bonn, Germany
Published online on: January 14, 2021 https://doi.org/10.3892/wasj.2021.85
Article Number: 14
Copyright: © Winter et al. This is an open access article distributed under the terms of Creative Commons Attribution License.

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Abstract

In thyroid carcinoma cells, the soluble β‑galactoside‑specific lectin, galectin‑3, is extra‑ and intracellularly expressed and plays a significant role in thyroid cancer diagnosis. The functional relevance of this molecule, particularly in its extracellular environment however, warrants further elucidation. To gain insight into this topic, the present study characterized principal functional properties of galectin‑3 in 3 commonly used thyroid carcinoma cell lines (B‑CPAP, Cal‑62 and FTC‑133) that express the molecule intra‑ and extracellulary. Cell‑intrinsic galectin‑3 harbors a functional carbohydrate recognition domain as determined by affinity purification. Moreover, cell surface expressed galectin‑3 can be partially removed by treatment with lactose or asialofetuin, but not with sucrose. Thyroid carcinoma cells adhere to substrate‑bound galectin‑3 in a β‑galactoside‑specific manner, whereby only cell adhesion, but not cell migration is promoted. Thus, thyroid tumor cells harbor functional active galectin‑3 that, inter alia, specifically interacts with cell surface‑expressed molecular ligands in a β‑galactoside‑dependent manner, whereby the molecule can at least interfere with cell adhesion. The modulation of galectin‑3 expression level or its ligands in such tumor cells could be of therapeutic interest and needs further experimental clarification.

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