Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P62988 (Ubiquitin)
 4,326 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ubiquitin immunocytochemistry with an antiserum which reacts with ubiquitin-protein conjugates demonstrates the presence of ubiquitinated proteins in filamentous inclusions found in neurones in the major human neurodegenerative diseases, i.e. Alzheimer's disease, diffuse Lewy body disease, motor neurone disease. Ubiquitin immunohistochemistry has revolutionized the neuropathological diagnosis of dementia showing that diffuse Lewy body disease is not, as previously supposed, a rare cause of dementia. The filamentous inclusions in neurones in the human neurodegenerative diseases can be divided into at least two types based on recent immunocytochemical studies. We have shown that a ubiquitin-carboxyl terminal hydrolase is present in Lewy bodies but not in neurofibrillary tangles in Alzheimer's disease. This observation is significant since it indicates that molecular pathological mechanisms in neurones in diffuse Lewy body disease are fundamentally different to Alzheimer's disease. Ubiquitin-protein conjugates are also found in vacuoles in areas of granulovacuolar degeneration in hippocampal neurones in Alzheimer's disease and in granulovacuoles in neurones of scrapie infected mouse brain. These locations suggest that ubiquitinated protein are present in the lysosome-related system of neurones. We have recently shown that ubiquitin-protein conjugates are indeed enriched some 12-fold in the lysosomes of normal fibroblasts and lymphocytes.
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PMID:The role of protein ubiquitination in neurodegenerative disease. 166 96

We have shown by northern analyses that the expression of the mouse polyubiquitin C gene is increased severalfold in the brains of mice infected with both the ME7 and 87V strains of scrapie. Expression of the polyubiquitin gene does not change significantly, compared with controls, until the later stages of disease progression when there is a 2.5-fold increase in ME7-infected brains and a 1.8-fold increase in 87V-infected brains. The patterns of changes of expression of the polyubiquitin genes in brains infected with the two strains of scrapie resemble those of accumulation of ubiquitin-conjugate-positive structures in the brain that are detected immunohistochemically. A similar increase in the expression of a heat-shock protein 70 gene also occurs.
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PMID:Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain. 751 19