Effects of thiol protease inhibitors on intracellular degradation of exogenous beta-galactosidase in cultured human skin fibroblasts.
The effects of low molecular weight (LMW) protease inhibitors of microbial origin were evaluated on the intracellular degradation of beta-galactosidase purified from Aspergillus oryzae and taken up by cultured human skin fibroblasts with beta-galactosidase deficiency. Only thiol protease inhibitors showed an effect to increase the enzyme activity. E-64, a specific inhibitor of thiol proteases, prolonged 3-fold a half life of the exogenous beta-galactosidase and when the enzyme was supplied as liposomes, the half life was prolonged 9-fold in these cells. The role of thiol proteases in the degradation of enzyme molecules was discussed.
D001692:Biological Transport / Q000187:drug effects; D002478:Cells, Cultured; D005347:Fibroblasts / Q000201:enzymology; D005696:Galactosidases / Q000378:metabolism*; D005733:Gangliosidoses / Q000201:enzymology*; D006207:Half-Life; D006801:Humans; D007700:Kinetics; D011480:Protease Inhibitors / Q000494:pharmacology*; D012867:Skin / Q000201:enzymology*; D001616:beta-Galactosidase / Q000378:metabolism*
D011480:Protease Inhibitors; D005696:Galactosidases; D001616:beta-Galactosidase