Altered trafficking of abnormal @entity27465 in XXXX : @entity27465 accumulation in oligodendroglial inner mesaxons.

@entity1 @entity742 @entity19 @entity1579 @entity281 @entity27465 @entity11506
AIMS: Prion diseases exist in classical and atypical disease forms. Both forms are characterised by disease-associated accumulation of a host membrane sialoglycoprotein known as @entity27465 (PrP(d) ). In classical forms of @entity1579 , PrP(d) can accumulate in the extracellular space as fibrillar amyloid, intracellularly within lysosomes, but mainly on membranes in association with unique and characteristic membrane pathology. These membrane changes are found in all species and strains of classical @entity1579 and consist of spiral, branched and clathrin coated membrane invaginations on dendrites. Atypical @entity1579 have been described in ruminants and @entity1 and have distinct biological, biochemical and pathological properties when compared to classical disease. The purpose of this study was to determine whether the sub-cellular pattern of PrP(d) accumulation and membrane changes in @entity11506 were the same as those found in classical @entity1579 METHODS: Immunogold electron microscopy was used to examine brains of @entity11506 affected @entity742 and Tg338 @entity19 RESULTS: Classical prion disease-associated membrane lesions were not found in @entity11506 affected @entity742 , however, white matter PrP(d) accumulation was localised mainly to the inner mesaxon and paranodal cytoplasm of oligodendroglia. Similar lesions were found in myelinated axons of @entity11506 Tg338-infected @entity19 . However, Tg338 @entity19 also showed the unique grey matter membrane changes seen in classical forms of disease CONCLUSIONS: These data show that atypical @entity281 directs a change in trafficking of abnormal PrP to axons and oligodendroglia and that the resulting pathology is an interaction between the agent strain and host genotype. This article is protected by copyright. All rights reserved.
