A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin-protein conjugates in a neuronal cell

Maria E. Figueiredo‐Pereira, Kelly A. Berg, Sherwin Wilk

Research output: Contribution to journalArticlepeer-review

182 Scopus citations

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 languageEnglish (US)
Pages (from-to)1578-1581
Number of pages4
JournalJournal of neurochemistry
Volume63
Issue number4
StatePublished - Oct 1994
Externally publishedYes

Keywords

  • 20S proteasome
  • Chymotrypsin-like activity
  • Multicatalytic proteinase complex inhibitor
  • Neuronal cells
  • Ubiquitin-protein conjugates

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Biochemistry

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