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Small heat shock proteins, the cytoskeleton, and inclusion body formation
Author(s) -
Head M. W.,
Goldman J. E.
Publication year - 2000
Publication title -
neuropathology and applied neurobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.538
H-Index - 95
eISSN - 1365-2990
pISSN - 0305-1846
DOI - 10.1046/j.1365-2990.2000.00269.x
Subject(s) - intermediate filament , glial fibrillary acidic protein , microbiology and biotechnology , downregulation and upregulation , heat shock protein , cytoskeleton , inclusion bodies , biology , protein filament , chemistry , cell , biochemistry , immunology , immunohistochemistry , escherichia coli , gene
Since first being implicated in central nervous system disease 10 years ago, much has been learned concerning the regulation and function of the small heat shock protein αB‐crystallin. Neuropathological, cellular and molecular studies all now point to a functional relationship between αB‐crystallin and intermediate filaments. αB‐crystallin accumulation marks reactive astrocytes in general in a wide variety of disorders and specifically intermediate filament‐based glial inclusion bodies such as Rosenthal fibres found in astrocytes in Alexander's disease. In vitro , αB‐crystallin expression suppresses intermediate filament aggregation and can prevent or reverse experimentally induced glial inclusion body formation. Conversely, dysregulation of glial fibrillary acidic protein expression in vivo results in Rosenthal fibre formation and upregulation of endogenous αB‐crystallin expression. These data and those from studies recently carried out on other tissues strongly suggest that one function of this small heat shock protein is to modulate intermediate filament organization under conditions of physiological stress and neurodegenerative disease.