The interactions of cells with the extracellular matrix (ECM) proteins are essential for cells survival and motility. It has been reported, that lumican, the member of the small leucine-rich proteoglycans (SLRPs) family of ECM, plays a regulatory role in cancer cells adhesion and migration. Tumor cells motility depends on the dynamic reorganization of actin cytoskeleton in the response to some external stimuli, acting via focal adhesions complexes. As we have previously shown, lumican induces actin cytoskeleton rearrangement in A375 cells. Actin filaments are required for cell motility and they are linked to the plasma membrane by vinculin, the one of focal adhesion plaques proteins. Our current studies are focused on the distribution of vinculin in melanoma cells growing on the different concentrations of human recombinant lumican in comparison to the cells growing on other ECM substrata (fibronectin; type-1 collagen) and glass. Actin filaments were visualized by rodamine-conjugated phalloidin staining and vinculin distribution was observed in fluorescence confocal microscope. Vinculin was labeled with monoclonal antibodies, followed by Alexa Fluor 488-conjugated secondary antibodies. The number of vinculin-containing adhesion plaques in A375 cells (growing on tested substrata) was counted and correlated with the number of spread cells. The condensed sub-membrane localization of actin filaments was observed in melanoma cells growing in the presence of lumican to distinguish from control cells - presenting actin filaments evenly spread through the whole cell body. The changes in actin cytoskeleton organization in A375 cells were followed by the decrease in the number of vinculin-containing focal adhesion sites. The data suggest that lumican may take part in the signal transduction pathway, leading to the changes in the migratory potential of melanoma cells.

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