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Abstract
The ubiquitin-dependent protein degradation system plays a major role in the removal
of abnormal and denatured proteins which may form insoluble aggregates in pathological
conditions or during other cellular stress. Neuritic plaques and neurofibrillary tangles
in sections of Alzheimer's cortex contain insoluble aggregates of proteins and are
shown here to specifically immunostain with an antiserum to ubiquitin-protein conjugates.
Plaque core amyloid and normal neurons do not immunostain and sodium dodecyl sulphate
(SDS)-insoluble tangle preparations are not ubiquitin-positive on slot blots. The
possible role and consequences of ubiquitination in tangle and plaque production in
Alzheimer's disease are discussed.