Effect of proteasomal inhibition by MG-132 on inclusion body formation in astrocytes

Birte Meyer-Helms,Christiane Richter-Landsberg,Thomas Stahnke,Olaf Goldbaum

doi:10.1186/1471-2202-8-s1-p12

Birte Meyer-Helms, Christiane Richter-Landsberg + Show 2 more

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https://doi.org/10.1186/1471-2202-8-s1-p12

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Abstract

The small heat shock proteins (sHSPs), HSP25/27 and alpha B-crystallin, are more prominent in glia than in neurons, act as molecular chaperones and specifically interact with cytoskeletal elements. They represent prominent constituents in inclusion bodies originating in astrocytes and oligodendrocytes, and have been described to be involved in Alexander's disease, a human neurodegenerative disorder with astrocytic inclusions called Rosenthal fibres (RF). These protein aggregates also contain GFAP (glial fibrillary acidic protein) and ubiquitin, indicating that inclusion body formation might be causally related to an impairment of the ubiquitin proteasome pathway (UPS).

Highlights

The small heat shock proteins, HSP25/27 and alpha B-crystallin, are more prominent in glia than in neurons, act as molecular chaperones and interact with cytoskeletal elements. They represent prominent constituents in inclusion bodies originating in astrocytes and oligodendrocytes, and have been described to be involved in Alexander's disease, a human neurodegenerative disorder with astrocytic inclusions called Rosenthal fibres (RF)
We have examined if defects in the ubiquitin proteasome pathway (UPS) system contribute to the protein aggregation process in astrocytes
Treatment with MG-132 for 24 h caused the upregulation of HSP25 and alpha B-crystallin, which both were increasingly found in the detergent insoluble fraction

Summary

Introduction

The small heat shock proteins (sHSPs), HSP25/27 and alpha B-crystallin, are more prominent in glia than in neurons, act as molecular chaperones and interact with cytoskeletal elements. Effect of proteasomal inhibition by MG-132 on inclusion body formation in astrocytes Birte Meyer-Helms*, Thomas Stahnke, Olaf Goldbaum and Christiane Richter-Landsberg Address: University of Oldenburg, Department of Biology, Molecular Neurobiology, 26111 Oldenburg, Germany * Corresponding author from Annual Meeting of the Study Group Neurochemistry.

Results

Conclusion