Bm. Riederer et al., Differential phosphorylation of tau proteins during kitten brain development and Alzheimer's disease, J NEUROCYT, 30(2), 2001, pp. 145-158
Differential distribution and phosphorylation of tau proteins were studied
in developing kitten brain by using several antibodies, and was compared to
phosphorylation in Alzheimer's disease. Several antibodies demonstrated th
e presence of phosphorylated tau proteins during kitten brain development a
nd identified pathological structures in human brain tissue. Antibody AD2,
recognized tau in kittens and adult cats, but reacted in Alzheimer's tissue
only with a pathological tau form. Antibody AT8 was prominent in developin
g kitten neurons and was found in axons and dendrites. After the first post
natal month this phosphorylation type disappeared from axons. Furthermore,
dephosphorylation of kitten tau with alkaline phosphatase abolished immunor
eactivity of AT8, but not that of AD2, pointing to a protection of the AD2
epitope in cats. Tau proteins during early cat brain development are phosph
orylated at several sites that are also phosphorylated in paired helical fi
laments during Alzheimer's disease. In either event, phosphorylation of tau
may play a crucial role to modulate microtubule dynamics, contributing to
increased microtubule instability and promoting growth of processes during
neuronal development or changing dynamic properties of the cytoskeleton and
contributing to the formation of pathological structures in neurodegenerat
ive diseases.