ABSTRACT
Study of the expression of the aspartyl cathepsin D-like and cysteine cathepsin L-like proteinases was carried out on a model system of rat embryo fibroblasts. The model system employed makes it possible to distinguish two discrete successive stages of transformation in vitro: immortalization and tumorigenic transformation. The dynamics of expression and subcellular distribution of proteinases throughout the transformation process was followed. It was shown that in immortalized and transformed cells the activities of the aspartyl and cysteine proteinases were expressed to a variable degree and the expression was dependent on the time of cell cultivation. The increase in both the aspartyl cathepsin D-like proteinase and cysteine cathepsin L- and B-like proteinase activities was correlated with the stage of fibroblast transformation. At all stages studied of transformation, the major part of cathepsin L-like proteinase activity was localized within the cell, while among secreted proteinases the cathepsin D-like proteinase was apparently predominant. It was found that the secreted cathepsin D-like proteinase in all cell cultures studied was complexed with the inhibitor.
