Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-08

AUTHORS

T. Iwatsubo, M. Hasegawa, Y. Ihara

ABSTRACT

Tau accumulating as paired helical filaments (PHF) in Alzheimer's disease brain is considered to be abnormally phosphorylated on distinct sites. To compare the phosphorylation state of tau-positive neuronal inclusions among diverse neurologic diseases, we have probed these lesions with three well-defined PHF/tau monoclonals, C5, M4 and tau 1, that most likely recognize three proline-directed phosphorylation sites in PHF-tau. In Alzheimer's disease brain all three monoclonals intensely immunostained intracellular neurofibrillary tangles, neuropil threads, senile plaque neurites, and "pretangle neurons" in a phosphorylation-dependent manner. They also stained, in the same manner, Pick bodies in Pick's disease, and neurofibrillary tangles and neuropil threads in various tangle-forming neurologic diseases. In most of these diseases (including Pick's disease, progressive supranuclear palsy, subacute sclerosing panencephalitis, and Alzheimer's disease) astrocytes and oligodendrocytes were found to contain tau-positive inclusions which showed the same immunocytochemical characteristics. Thus, the widely occurring tau-positive inclusions share common phosphorylation characteristics irrespective of underlying diseases or cell types. More... »

PAGES

129-136

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00294505

DOI

http://dx.doi.org/10.1007/bf00294505

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052858985

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7985493


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