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Poly(ADP-ribose) drives pathologic α-synuclein neurodegeneration in Parkinson’s disease.

I have corresponded with James Clement about the possibility that elevated PARP-1 activity may a primary cause of the decline of NAD+ during aging, because PARP-1 consumes NAD+ as a cofactor in its activity. This group reports that PARP-1 also apparently accelerates the formation of toxic alpha-synuclein, and in at least one model, PARP-1 inhibition or deletion could prevent alpha-synuclein toxicity. PARP-1 inhibition or deletion does not seem like an enduring solution, as it leaves us tinkering with metabolism instead of cleaning up damage. I do wonder why PARP-1 is upregulated during aging; perhaps if we address the cause of this upregulation, we could prevent these negative downstream effects.
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α-Synuclein Aggregated with Tau and β-Amyloid in Human Platelets from Healthy Subjects: Correlation with Physical Exercise.

This group reports that (1) alpha-synuclein forms aggregates with Abeta or tau in red blood cells of healthy people, (2) all three of these aggregation-prone proteins were found in human platelets, and (3) tau was found to correlate inversely with physical activity (more activity was associated with lower tau). If I understand them correctly, they conclude that platelet content of these proteins might be used as a surrogate marker for their concentration in other compartments in aging humans.
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α-Synuclein impairs ferritinophagy in the retinal pigment epithelium: Implications for retinal iron dyshomeostasis in Parkinson’s disease.

I'm skeptical that an in vitro model of this situation would accurately represent what happens in humans with Parkinson's disease, but I'll leave it up to readers to decide. Here, these researchers report that alpha-synuclein appears to disrupt trafficking of lysosomal hydrolases, which could be the cause of accumulated alpha-synuclein and ferritin in the eyes of people with Parkinson's.
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