Changes in proteinase activities during the differentiation of murine erythroleukemia cells |
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Authors: | T Tsukahara S Ishiura E Kominami H Sugita |
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Affiliation: | National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan. |
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Abstract: | Changes in intracellular proteinase activities were examined during DMSO-induced differentiation of murine erythroleukemia cells. Suc-APA-MCA hydrolytic activity was significantly decreased, and apparent ATP-dependent multicatalytic proteinase activity was also decreased with MEL cell differentiation. Cathepsin B and L activity was mainly present in the microsomal fraction of control cells, but a part of this activity had shifted to the lysosomal fraction of differentiated cells. With the translocation of cathepsin B from the microsomal to the lysosomal fraction, the pro-enzyme form of cathepsin B was converted into the mature enzyme. These results suggest that the lysosomal pathway contributes to the degradation of specific proteins with cell differentiation. |
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