CHARACTERISTICS OF CYTOSKELETON ORGANIZATION OF HUMAN NORMAL POSTNATAL, SCAR AND EMBRYONIC SKIN FIBROBLASTS
SPREADING ON DIFFERENT PROTEINS OF EXTRACELLULAR MATRIX
N. M. Yudintseva,1 M. I. Blinova, G. P. Pinaev
Institute of Cytology RAS, St. Petersburg;
1 e-mail: yudintseva@mail15.com
Human dermal fibroblasts were obtained from various anatomical sites expressing different sets of genes. Distinction of their synthetic can be determined by the
microenvironment and composition of receptors on the surface of the cells. Earlier, we have shown that the cytoskeleton of cultured cells rapidly reacts to any
external modification, and characteristics of their spatial organization may reflect similarities and differences between cells if various origins under the same
conditions. The extracellular matrix proteins influence on the character of structures forming by actin cytoskeleton. In this work, we analyzed cytoskeleton
organization of the fibroblasts obtained from normal postnatal, scar an embryonic human skin, which were spreading on the basic proteins of extracellular matrix
such as collagen Type I and IV, laminin 2/4, and fibronectin. The results of confocal microscopy showed that fibroblasts of various origins had considerable differences
in organization of actin structures and distribution of focal contacts visualized by anti-vinculin antibodies. Furthermore, various fibroblasts spread on the same protein
of the extracellular matrix revealed essential modifications of actin structures and focal contacts with the similarity of spatial organization of the cytoskeleton.
Discovered variations of actin micro-filaments organization are evidence of different extent of cell interactions with various proteins. These variations may depend on
combination of integrins on the surface of a cell membrane. The data obtained give grounds to suppose considerable differences in morphogenic function of fibroblasts
of various origins.
Key words: fibroblasts, extracellular matrix protein, cytoskeleton, focal contact, vinculin
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