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Oligodendroglial lesions and white matter pathology have long been underestimated and are specifically prominent in frontotemporal dementias (FTDs), such as Pick's disease (PiD), progressive supranuclear palsy (PSP), corticobasal degeneration (CBD) and frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP\u201017). Oligodendrocytes contain an extensive microtubule network and express the microtubule\u2010associated protein tau. Tau\u2010positive inclusion bodies in oligodendrocytes are postively stained with antibodies against ubiquitin and heat shock proteins (HSPs). Specifically the small HSP \u03b1B\u2010crystallin has been identified in oligodendroglial lesions. HSPs act as molecular chaperones and prevent the accumulation of abnormal proteins, and support proteolytic degradation by targeting non\u2010reparable proteins to the ubiquitin proteasomal pathway. HSPs and the proteasomal system closely work together. The present report summarizes recent data on HSP induction and aggregate formation in oligodendroglia cell culture systems, indicating that posttranslational modification of tau, HSP induction and alterations of the proteasomal system, which might occur during aging and disease processes, are involved in the neuropathological events leading to aggregate formation and degeneration.<\/jats:p><\/jats:sec>","DOI":"10.1016\/j.ijdevneu.2004.07.003","type":"journal-article","created":{"date-parts":[[2004,8,27]],"date-time":"2004-08-27T20:59:33Z","timestamp":1093640373000},"page":"443-451","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Tau\u2010inclusion body formation in oligodendroglia: the role of stress proteins and proteasome inhibition"],"prefix":"10.1002","volume":"22","author":[{"given":"Christiane","family":"Richter\u2010Landsberg","sequence":"first","affiliation":[{"name":"Department of Biology, Molecular Neurobiology University of Oldenburg P.O. 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