Ubiquitin conjugate immunoreactivity in the brains of scrapie infected mice

Lowe, James, McDermott, Helen, Kenward, Nigel, Landon, Michael, Mayer, R. John, Bruce, Moira, McBride, Patricia, Somerville, Robert A. and Hope, James (1990) Ubiquitin conjugate immunoreactivity in the brains of scrapie infected mice. The Journal of Pathology, 162 (1). pp. 61-66. ISSN 0022-3417

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Abstract

Sections of brain from normal mice or clinically‐ill mice infected with either the 87V or the ME7 strains of sheep scrapie were immunostained to show the localization of ubiquitin‐protein conjugates or a specific marker of disease, the scrapie‐associated fibril protein (PrP). In both scrapie models immunoreactive ubiquitin‐protein conjugates were seen in thread‐like structures found throughout the neuropil, in inclusion bodies within vacuolated neurones, and in areas surrounding anti‐PrP positive amyloid plaques. The PrP protein was visualized in diffuse deposits in highly vacuolated parts of the scrapie‐affected brain, and focally in amyloid plaques, microglia and neuronal processes. The ubiquitin‐protein conjugate staining of scrapie amyloid plaques is very similar to that seen in the plaques of Alzheimer's disease. The ubiquitinated intraneuronal inclusion bodies seen in scrapie resemble the granulovacuolar lesions also seen in Alzheimer's disease, but appear much larger and possibly correspond to material in giant autophagic vacuoles. We suggest that these inclusions may be the result of ubiquitinated abnormal proteins being directed to the lysosomal system, and that scrapie and Alzheimer's disease share at least some common processes of neurodegeneration.

Item Type: Article
Uncontrolled Keywords: amyloid plaques,neurodegeneration,scrapie,scrapie‐associated fibril protein,ubiquitin,pathology and forensic medicine ,/dk/atira/pure/subjectarea/asjc/2700/2734
Faculty \ School: Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 02 Dec 2025 15:30
Last Modified: 10 Dec 2025 14:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/101189
DOI: 10.1002/path.1711620112

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