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Characterization of N‐cadherin unbinding properties in non‐malignant (HCV29) and malignant (T24) bladder cells
Author(s) -
Lekka Małgorzata,
Gil Dorota,
Dąbroś Wojciech,
Jaczewska Justyna,
Kulik Andrzej J.,
Lekki Janusz,
Stachura Zbigniew,
Stachura Jerzy,
Laidler Piotr
Publication year - 2011
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.1123
Subject(s) - cadherin , immunohistochemistry , bladder cancer , antibody , cancer cell , chemistry , atomic force microscopy , cancer , western blot , cancer research , malignant cells , blot , phenotype , extracellular , force spectroscopy , pathology , biology , molecule , cell , medicine , immunology , biochemistry , materials science , nanotechnology , gene , organic chemistry
The expression of N‐cadherin, characteristic of various cancers, very often leads to changes in the cells' adhesive properties. Thus, we sought to find out if N‐cadherin expressed in various, but cancer‐related cells, differs in its functional properties that could contribute to variations in cells' phenotypes. In our work, measurements of an unbinding force of a single N‐cadherin molecule, probed with the same antibody both on a surface of living non‐malignant (HCV29) and malignant cells (T24) of bladder cancer, were carried out with the use of an atomic force microscopy. The results show the enhanced N‐cadherin level in T24 malignant cells (8.7% vs. 3.6% obtained for non‐malignant one), confirmed by the Western blot and the immunohistochemical staining. The effect was accompanied by changes in unbinding properties of an individual N‐cadherin molecule. Lower unbinding force values (26.1 ± 7.1 pN) in non‐malignant cells reveal less stable N‐cadherin complexes, as compared to malignant cells (61.7 ± 14.6 pN). This suggests the cancer‐related changes in a structure of the binding site of the antibody, located at the extracellular domain of N‐cadherin. Copyright © 2011 John Wiley & Sons, Ltd.