Glial tau-positive structures lack the sequence encoded by exon 3 of the tau protein gene.
Tau protein comprises six distinct isoforms defined by the presence or absence of sequences encoded by alternatively spliced exon 2, 3 and 10. We have investigated immunohistochemically the expression of exon 3-derived fragment (E-3) of tau protein in brains of patients with Alzheimer's disease (AD) and other neurodegenerative diseases in which the abnormal accumulation of tau protein takes place. In AD, a subset of neurofibrillary tangles, neuropil threads and dystrophic neurites in senile plaques were stained positively with an anti-E-3 antibody. In sharp contrast, glial tau-positive structures, such as astrocytic plaques and oligodendroglial coiled bodies, were negative for E-3 in all cases examined in this study. This is the first report to discriminate tau-positive inclusions in glial cells from those in neurons at the molecular level.
Nishimura
T
T
Tokyo Institute of Psychiatry, Japan.
Ikeda
K
K
Akiyama
H
H
Arai
T
T
Kondo
H
H
Okochi
M
M
Furiya
Y
Y
Mori
H
H
Oda
T
T
Kato
M
M
Iseki
E
E
D000368:Aged; D001921:Brain / Q000276:immunology*; D005091:Exons / Q000235:genetics*; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008875:Middle Aged; D009457:Neuroglia / Q000378:metabolism*; D016875:tau Proteins / Q000235:genetics* / Q000378:metabolism
D016875:tau Proteins