Vol 49, No 4 (2011)
Original paper
Submitted: 2012-01-16
Published online: 2012-01-16
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.
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)
Keywords
PC-3 cell line; fibronectin; cell adhesion and spreading; cytoskeleton; sulfonated polystyrene
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
Page views
1538
Article views/downloads
2363
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