Preferential recruitment of ataxin-3 independent of expanded polyglutamine: an immunohistochemical study on Marinesco bodies
- H Fujigasakia,
- T Uchiharaa,
- J Takahashib,
- H Matsushitac,
- A Nakamuraa,
- S Koyanoa,d,
- K Iwabuchie,
- S Hiraif,
- H Mizusawag
- aDepartment of Neuropathology, Tokyo Metropolitan Institute for Neuroscience, 2–6 Musashidai, Fuchu-shi, Tokyo, Japan, bDepartment of Neuropathology, The Jikei University, Japan, cDepartment of Pathology, Toranomon Hospital, Japan, dDepartment of Neurology, Yokohama City University, Japan, eDepartment of Psychiatry and Neurology, Kanagawa Rehabilitation Center, Japan, fDepartment of Neurology, Tokyo Metropolitan Neurological Hospital, Japan, gDepartment of Neurology and Neurological Science, Tokyo Medical and Dental University, Graduate School of Medicine, Japan
- Dr T Uchiharauchihara{at}tmin.ac.jp
- Received 19 February 2001
- Revised 2 May 2001
- Accepted 16 May 2001
Abstract
In an immunohistochemical study of Marinesco bodies—a neuronal intranuclear inclusion often seen in neurons of the substantia nigra of patients with hepatic encephalopathy—it was shown that one of the polyglutamine proteins, ataxin-3, is preferentially recruited into this inclusion, whereas other polyglutamine proteins (ataxin-2 and TATA box-binding protein) are not. This suggests that recruitment of each of the polyglutamine proteins may be differently regulated. Because this nuclear inclusion is thought to be formed in response to cellular stress, as occurs in hepatic encephalopathy, even in the absence of an expanded CAG/polyglutamine repeat, recruitment of ataxin-3 and ubiquitin into Marinesco bodies may represent a cellular response to noxious external stimuli unrelated to expanded CAG/polyglutamine.
