T. Nishimura et al., GLIAL TAU-POSITIVE STRUCTURES LACK THE SEQUENCE ENCODED BY EXON-3 OF THE TAU-PROTEIN GENE, Neuroscience letters, 224(3), 1997, pp. 169-172
Tau protein comprises six distinct isoforms defined by the presence or
absence of sequences encoded by alternatively spliced exon 2, 3 and 1
0. We have investigated immunohistochemically the expression of exon 3
-derived fragment (E-3) of tau protein in brains of patients with Alzh
eimer'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 s
enile plaques were stained positively with an anti-E-3 antibody. In sh
arp contrast, glial tau-positive structures, such as astrocytic plaque
s and oligodendroglial coiled bodies, were negative for E3 in all case
s examined in this study. This is the first report to discriminate tau
-positive inclusions in glial cells from those in neurons at the molec
ular level. (C) 1997 Elsevier Science Ireland Ltd.