[Electron histochemical detection of intracellular and extracellular cathepsin D in the liver].

Cathepsin D localization was studied in the liver of white rats by ultrastructural cytochemistry. It was shown that the product of reaction was present in lysosomes of hepatocytes, Kupffer's and endothelial cells and in fibroblasts from portal tracts am small granules or their conglomerate of different electron density. The lowest activity of cathepsin D was observed in hepatocytes, the most intensive reaction--in Kupffer cells. The extracellular activity of cathepsin D in vivo was revealed. It means that besides participation in intracellular degradation of different proteins, cathepsin D is secreted to extracellular space by liver cells (hepatocytes, Kupffer cells, fibroblasts) and it may participate in catabolism of intercellular matrix.