Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution

Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its associat...

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Bibliographic Details
Published in:PloS one 2015-07, Vol.10 (7), p.e0132455-e0132455
Main Authors: Sbardella, Diego, Tundo, Grazia Raffaella, Sciandra, Francesca, Bozzi, Manuela, Gioia, Magda, Ciaccio, Chiara, Tarantino, Umberto, Brancaccio, Andrea, Coletta, Massimo, Marini, Stefano
Format: Article
Language:English
Subjects:
Analysis
Blotting, Western
Catalysis
Cell Line, Tumor
Complex Mixtures
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Enzymatic activity
Enzymes
Fibroblasts
Gene Silencing
Heat shock proteins
Heat-Shock Response
Humans
Insulin
Insulysin
Insulysin - metabolism
Localization
Medicine
Metabolism
Mitochondria
Neuroblastoma - enzymology
Neuroblastoma - pathology
Oxidative stress
Peptidase
Physiological aspects
Proteasome 26S
Proteasome Endopeptidase Complex - metabolism
Protein Binding
Proteins
Stress, Physiological
Subcellular Fractions - metabolism
Time Factors
Tissues
Variation
Zinc
Zinc compounds
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Summary:Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a novel Heat Shock Protein-like behaviour of IDE and its association with the 26S proteasome. In the present study, we examine the mechanistic and molecular features of IDE-26S proteasome interaction in a cell experimental model, extending the investigation also to the effect of IDE on the enzymatic activities of the 26S proteasome. Further, kinetic investigations indicate that the 26S proteasome activity undergoes a functional modulation by IDE through an extra-catalytic mechanism. The IDE-26S proteasome interaction was analyzed during the Heat Shock Response and we report novel findings on IDE intracellular distribution that might be of critical relevance for cell metabolism.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0132455