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Originally published as JHC exPRESS on September 7, 2005.
doi:10.1369/jhc.5B6752.2005
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Journal of Histochemistry and Cytochemistry
Volume 54 (2): 263-267, 2006
Copyright ©The Histochemical Society, Inc.

BRIEF REPORT

Subcellular Distribution of Components of the Ubiquitin–Proteasome System in Non-diseased Human and Rat Brain

Csaba Ádori, Péter Low, Georgij Moszkovkin, György Bagdy, Lajos László and Gábor G. Kovács

Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University of Sciences, Budapest, Hungary (CA,PL,LL), and Department of Neuropathology (GM,GGK), Laboratory of Neurochemistry and Experimental Medicine (CA,GB), National Institute of Neurology and Psychiatry, Budapest, Hungary

Correspondence to: Lajos László, Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University of Sciences, Pázmány Péter Stny. 1/C, H-1117 Budapest, Hungary. E-mail: laszlo{at}cerberus.elte.hu

Our aim was to investigate and to compare the intracellular distribution of ubiquitin, 20S proteasome, and all six proteasomal regulatory ATPases in non-diseased human and rat brains. Ubiquitin and ATPases S4 and S7 show dominant nuclear immunostaining, whereas subunits S6a, S6b, and S10b show mainly cytoplasmic immunostaining in both species. However, S8 localization is inconsistent, prevailing nuclear in rat and cytoplasmic in human. In rat brain, small clastosome-like nuclear bodies demonstrate strong ubiquitin, 20S, and S6a immunoreactivity both in neurons and glial cells. Prominent nuclear immunolocalization of members of the ubiquitin–proteasome system provides morphological evidence for function of these proteins in transcription regulation and/or DNA repair. J Histochem Cytochem 54:263–267, 2006

Key Words: ubiquitin • proteasome • regulatory ATPase • clastosome • brain • immunohistochemistry


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