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ADHESION OF L1210 CELLS TO SULFONATED STYRENE COPOLYMER SURFACES: IMAGING OF F‐ACTIN AND α‐ACTININ
Author(s) -
KowalczyńSka H.M,
NowakWyrzykowska M.
Publication year - 1999
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1999.0358
Subject(s) - biophysics , actin , adhesion , cell , chemistry , cytoplasm , cell adhesion , actinin , cytoskeleton , microbiology and biotechnology , biochemistry , biology , organic chemistry
The static adhesion of living L1210 cells to sulfonated copolymer surfaces of different sulfonic group content and the actin cytoskeleton organization in the adhering cells were studied. The strength of the cell—substratum interaction was estimated by determining the relative number of cells remaining adherent despite experiencing a shearing force equal to 1.25×10 −11 N caused by the laminar flow of the medium. The cell—substratum interaction took place in a medium with or without serum. The distribution of F‐actin and α‐actinin in the adhering cells was determined in sequences of fluorescent images of cell optical slices with the use of a computer method of cell image analysis. It was shown that the surface sulfonic groups affect not only the rate and strength of cell—substratum adhesion but also the F‐actin and α‐actinin distribution (in the cell regions near the substratum surface) in cells adhering in the medium containing serum. These proteins, concentrated in the tips of microvilli, were observed as dots. The distinctness (discernibleness) and sizes of these dots depend on the surface content of sulfonic groups. F‐actin is located at the periphery of the cells in cells adhering in the medium without serum and α‐actinin is concentrated in small dots at the periphery and in the central part of the cells.