Abstract
Abstract: Exposure of HT4 cells (a mouse neuronal cell line) to a new potent permeable peptidyl aldehyde inhibitor of the chymotrypsin‐like activity of the multicatalytic proteinase complex (MPC) causes accumulation of ubiquitinylated proteins. In contrast, inhibition of calpain or treatment with a lysosomotropic agent failed to produce detectable ubiquitin‐protein conjugates. The appearance of such conjugates is not a nonspecific phenomenon because incubation with the peptidyl alcohol analogue of the inhibitor does not produce accumulation of ubiquitinylated proteins. The MPC inhibitor may therefore be a useful tool for identification and study of physiological pathways involving MPC. Furthermore, the inhibitor may help develop a model for the study of neurodegeneration where accumulation of ubiquitin‐protein conjugates is commonly detected in abnormal brain inclusions.
Original language | English (US) |
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Pages (from-to) | 1578-1581 |
Number of pages | 4 |
Journal | Journal of neurochemistry |
Volume | 63 |
Issue number | 4 |
DOIs | |
State | Published - Oct 1994 |
Externally published | Yes |
Keywords
- 20S proteasome
- Chymotrypsin‐like activity
- Multicatalytic proteinase complex inhibitor
- Neuronal cells
- Ubiquitin‐protein conjugates
ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience