Identification of an elastase-like activity, that decreased during the differentiation of MEL cells, as a prolyl endopeptidase.
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Key Findings
Abstract
1. A Suc-APA-MCA hydrolytic activity was significantly decreased in murine erythroleukemia cells during DMSO-induced differentiation, but not in DMSO-resistant cells. 2. The Suc-APA-MCA hydrolytic enzyme was purified by ion exchange, adsorption, gel filtration and affinity chromotographies. The results of the chromatographies showed that only one enzyme hydrolyzed Suc-APA-MCA in MEL cells. 3. This enzyme is more sensitive to hydrolysis by Suc-GPLGP-MCA than Suc-APA-MCA at slightly acidic pH, and its activity is stimulated by 2-mercaptoethanol. 4. A cysteine proteinase inhibitor did not affect the activity, but a specific inhibitor of prolyl endopeptidase, Z-thioprothiazolidine, completely inhibited it. These results suggest that the Suc-APA-MCA hydrolytic enzyme is identical to a prolyl endopeptidase.
Affiliation
National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan.
External References
- PubMed ID:
- 2022299
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