Abstract
The presynaptic protein alpha-synuclein has been implicated in the pathogenesis of Parkinson's disease. First, two missense mutations A30P and A53T cause inheritable early onset Parkinson's disease in some families. Secondly, alpha-synuclein is present in Lewy bodies of affected nerve cells in the predominant sporadic type of Parkinson's disease as well as in dementia with Lewy bodies. We demonstrate in the rat optic system that a portion of alpha-synuclein is carried by the vesicle-moving fast component of axonal transport and that it binds to rat brain vesicles through its amino-terminal repeat region. We find alpha-synuclein with the A30P mutation of familial Parkinson's disease devoid of vesicle-binding activity and propose that mutant alpha-synuclein may accumulate, leading to assembly into Lewy body filaments.
Highlights
Parkinson’s disease is a common neurodegenerative disorder that affects approximately 0.2% of the population
We show that ␣-synuclein binds to vesicles from rat brain through its amino-terminal repeat region. ␣-Synuclein with the A30P mutation of familial Parkinson’s disease is devoid of significant vesicle-binding activity
Comparison of the amounts of immunoprecipitated labeled synucleins at 4, 30, and 96 h showed that approximately 15% of the total pool of ␣-synuclein and -synuclein moves by fast axonal transport, with the remainder moving in slow component b of axonal transport (SCb)
Summary
Parkinson’s disease is a common neurodegenerative disorder that affects approximately 0.2% of the population. We report that in rat optic nerve a portion of ␣-synuclein is carried in the vesicle-moving fast component of axonal transport. We show that ␣-synuclein binds to vesicles from rat brain through its amino-terminal repeat region. ␣-Synuclein with the A30P mutation of familial Parkinson’s disease is devoid of significant vesicle-binding activity.
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