Parkinson's disease (PD) is a neurodegenerative movement disorder characterized by degeneration of dopaminergic neurons in the midbrain and formation of Lewy bodies. The molecular mechanism of the selectivity to dopamine-containing neurons is yet unclear. Recently we investigated the biochemical characteristics and degradation pathway of tyrosine hydroxylase, which is expressed selectively in catecholaminergic neurons, and found that phosphorylated tyrosine hydroxylase at Ser40 (p40-TH) formed insoluble intracellular inclusions tightly co-localized with ubiquitin by inhibition of a proteasome system in NGF-differentiated PC12D cells. Here we examined the immunoreactivity against anti-TH and anti-p40-TH antibodies in post-mortem brains from PD patients. We found that brainstem-type Lewy bodies were immunoreactive to anti-TH antibody and that the cytosol of some neurons were immunopositive to anti-p40-TH antibody.
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