open access

Vol 49, No 4 (2011)
Original paper
Submitted: 2012-01-16
Published online: 2012-01-16
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Interaction of PC-3 cells with fibronectin adsorbed on sulfonated polystyrene surfaces

Anna Stachurska, Hanna M. Kowalczyńska
DOI: 10.5603/FHC.2011.0095
·
Folia Histochem Cytobiol 2011;49(4):706-718.

open access

Vol 49, No 4 (2011)
ORIGINAL PAPERS
Submitted: 2012-01-16
Published online: 2012-01-16

Abstract

The ability of cancer cells to invade neighboring tissues is crucial for cell dissemination and tumor metastasis. It is generally assumed that cell adhesion to extracellular matrix proteins is an important stage of cancer progression. Hence, adhesion of cancer cells under in vitro conditions to proteins adsorbed on a substratum surface has been studied to provide a better understanding of cell-protein interaction mechanisms. A protein, adsorbed in an appropriate conformation on a substratum surface, creates a biologically active layer that regulates such cell functions as adhesion, spreading, proliferation and migration. In our study, we examined the interaction of PC-3 cells under in vitro conditions with fibronectin adsorbed on sulfonated polystyrene surfaces of a defined chemical composition and topography. We investigated cell adhesion to fibronectin and cell spreading. Using automatic, sequential microscopic image registration, we are the first to present observations of the dynamics of PC-3 cell spreading and the cell shape during this process. Our results show that cell adhesion and the shape of spreading cells strongly depend on the time interaction with fibronectin. The analysis of images of cytoskeletal protein distribution in the cell region near the cell-substratum interface revealed that induction of a signal cascade took place, which led to the reorganization of the cytoskeletal proteins and the activation of focal adhesion kinase (FAK). (Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 4, pp. 706–718)

Abstract

The ability of cancer cells to invade neighboring tissues is crucial for cell dissemination and tumor metastasis. It is generally assumed that cell adhesion to extracellular matrix proteins is an important stage of cancer progression. Hence, adhesion of cancer cells under in vitro conditions to proteins adsorbed on a substratum surface has been studied to provide a better understanding of cell-protein interaction mechanisms. A protein, adsorbed in an appropriate conformation on a substratum surface, creates a biologically active layer that regulates such cell functions as adhesion, spreading, proliferation and migration. In our study, we examined the interaction of PC-3 cells under in vitro conditions with fibronectin adsorbed on sulfonated polystyrene surfaces of a defined chemical composition and topography. We investigated cell adhesion to fibronectin and cell spreading. Using automatic, sequential microscopic image registration, we are the first to present observations of the dynamics of PC-3 cell spreading and the cell shape during this process. Our results show that cell adhesion and the shape of spreading cells strongly depend on the time interaction with fibronectin. The analysis of images of cytoskeletal protein distribution in the cell region near the cell-substratum interface revealed that induction of a signal cascade took place, which led to the reorganization of the cytoskeletal proteins and the activation of focal adhesion kinase (FAK). (Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 4, pp. 706–718)
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Keywords

PC-3 cell line; fibronectin; cell adhesion and spreading; cytoskeleton; sulfonated polystyrene

About this article
Title

Interaction of PC-3 cells with fibronectin adsorbed on sulfonated polystyrene surfaces

Journal

Folia Histochemica et Cytobiologica

Issue

Vol 49, No 4 (2011)

Article type

Original paper

Pages

706-718

Published online

2012-01-16

DOI

10.5603/FHC.2011.0095

Bibliographic record

Folia Histochem Cytobiol 2011;49(4):706-718.

Keywords

PC-3 cell line
fibronectin
cell adhesion and spreading
cytoskeleton
sulfonated polystyrene

Authors

Anna Stachurska
Hanna M. Kowalczyńska

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