Bladder Cancer Cells Interaction with Lectin-Coated Surfaces under Static and Flow Conditions

Sep 24, 2026

Uploaded by Levi

Aberrant glycan expression, especially oligosaccharides attached to proteins or lipids, is a hallmark of multiple cancers, including urothelial malignancies. Lectin binding to these glycans functions as molecular recognition and can illuminate disease mechanisms. The study develops a quantitative method to track glycan–lectin interactions during urothelial cell adhesion from initial contact to steady state. Adhesion between cell lines and lectin-coated surfaces was measured under static and flow conditions using single-cell force spectroscopy and adhesion assays, showing lectin-specific, selective binding patterns.

LanguageEnglish

CategoryHealthcare

FormatPDF

Pages20

Reading Time50 min

AccessFree to download

Introduction

Glycans and adhesion in cancer progression

Methods and experimental approach

Measuring adhesion in static and flow conditions

Single-cell force spectroscopy and adhesion assays

Results and implications

Lectin-specific binding to urothelial cells

Potential applications: label-free capture and biosensors

Article Bladder Cancer Cells Interaction with Lectin-Coated Surfaces under Static and Flow Conditions Renata Szydlak 1, Ingrid H. Øvreeide 2, Marcin Luty 1, Tomasz Zieli ´nski 1, Victorien E. Prot 3, Joanna Zemła 1, Bjørn T. Stokke 2, * and Małgorzata Lekka 1, * Citation: Szydlak, R.; Øvreeide, I.H.; Luty, M.; Zieli ´nski, T.; Prot, V.E.; Zemła, J.; Stokke, B.T.; Lekka, M. Bladder Cancer Cells Interaction with Lectin-Coated Surfaces under Static and Flow Conditions. Int. J. Mol. Sci. 2023, 24, 8213. [https://doi.org/](https://doi.org/)[ ](https://doi.org/)[10.3390/ijms24098213](10.3390/ijms24098213) Academic Editor: Yuri Lyubchenko Received: 30 March 2023 Revised: 21 April 2023 Accepted: 29 April 2023 Published: 4 May 2023 Copyright: © 2023 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 ([https://](https://)[ ](https://)[creativecommons.org/licenses/by/](creativecommons.org/licenses/by/)[ ](creativecommons.org/licenses/by/)[4.0/](4.0/)) . 1 Department of Biophysical Microstructures, Institute of Nuclear Physics, Polish Academy of Sciences, PL-31342 Krakâw, Poland; [renata.szydlak@ifj.edu.pl](renata.szydlak@ifj.edu.pl) (R.S.); [marcin.luty@ifj.edu.pl](marcin.luty@ifj.edu.pl) (M.L.); [tomasz.zielinski@ifj.edu.pl](tomasz.zielinski@ifj.edu.pl) (T.Z.); [joanna.zemla@ifj.edu.pl](joanna.zemla@ifj.edu.pl) (J.Z.) 2 Biophysics and Medical Technology, Department of Physics, The Norwegian University of Science and Technology (NTNU), NO-7491 Trondheim, Norway; ingrid.h.ovreeide@ntnu.no 3 Biomechanics, Department of Structural Engineering, The Norwegian University of Science and Technology (NTNU), NO-7491 Trondheim, Norway; [victorien.prot@ntnu.no](victorien.prot@ntnu.no) * [Correspondence: bjorn.stokke@ntnu.no](Correspondence: bjorn.stokke@ntnu.no) (B.T.S.); [malgorzata.lekka@ifj.edu.pl](malgorzata.lekka@ifj.edu.pl) (M.L.) Abstract: Aberrant expression of glycans, i.e., oligosaccharide moiety covalently attached to proteins or lipids, is characteristic of various cancers, including urothelial ones. The binding of lectins to glycans is classiﬁed as molecular recognition, which makes lectins a strong tool for understanding their role in developing diseases. Here, we present a quantitative approach to tracing glycan–lectin interactions in cells, from the initial to the steady phase of adhesion. The cell adhesion was measured between urothelial cell lines (non-malignant HCV29 and carcinoma HT1376 and T24 cells) and lectincoated surfaces. Depending on the timescale, single-cell force spectroscopy, and adhesion assays conducted in static and ﬂow conditions were applied. The obtained results reveal that the adhesion of urothelial cells to two speciﬁc lectins, i.e., phytohemagglutinin-L and wheat germ agglutinin, was speciﬁc and selective. Thus, these lectins can be applied to selectively capture, identify, and differentiate between cancer types in a label-free manner. These results open up the possibility of designing lectin-based biosensors for diagnostic or prognostic purposes and developing strategies for drug delivery that could target cancer-associated glycans. Keywords: urothelial and bladder cancers; adhesion; lectin–glycan interaction; single cell force spectroscopy (SCFS); microﬂuidics; cell sorting 1. Introduction Genetic mutations and molecular alterations on the cell surface are one of the various fundamental features of cancer cells [1] . Among others, they manifest a change in cell–cell and cell–extracellular matrix (ECM) interactions [2–4] that are associated with alterationsin the expression of adhesion molecules present in the plasma membrane, such as cadherins, integrins, selectins, or immunoglobulin-like superfamily [2,3] . These molecules frequently bear carbohydrate moieties (i.e., glycans) that actively regulate cell–cell and cell–ECM interactions [4,5] .

FAQs

Why are glycan–lectin interactions important in bladder cancer?

Aberrant glycan expression is characteristic of cancers, and lectins bind glycans through molecular recognition, helping reveal how glycan changes relate to disease development.

What experimental conditions were used to study cell adhesion?

Adhesion was measured between urothelial cell lines and lectin-coated surfaces using assays under both static and flow conditions.

Which lectins showed selective binding to urothelial cells?

Phytohemagglutinin-L and wheat germ agglutinin (WGA) produced specific and selective adhesion to urothelial cells.

Sep 24, 2026

Uploaded by Levi