Switching on Endogenous Metal Binding Proteins in Parkinson's Disease.

The formation of cytotoxic intracellular protein aggregates is a pathological signature of multiple neurodegenerative diseases. The principle aggregating protein in Parkinson's disease (PD) and atypical Parkinson's diseases is α-synuclein (α-syn), which occurs in neural cytoplasmic inclusions. Several factors have been found to trigger α-syn aggregation, including raised calcium, iron, and copper.

Mechanisms underlying select chemotherapeutic-agent-induced neuroinflammation and subsequent neurodegeneration.

This review demonstrates the importance of uncovering the mechanisms that underlie chemotherapy-induced neuroinflammation. It builds upon the well-established connection between chemotherapeutic-agents and neurotoxicity along with widespread peripheral toxicities. This article summarises the major studies which have linked chemotherapy-induced neurodegeneration with direct evidence of neuroinflammation.

Dexamethasone Inhibits Copper-Induced Alpha-Synuclein Aggregation by a Metallothionein-Dependent Mechanism.

Intracellular aggregates of α-synuclein are the pathological hallmark of Parkinson's disease (PD) and dementia with Lewy bodies (DLB), being linked to neurotoxicity. Multiple triggers of α-synuclein aggregation have been implicated, including raised copper. The potential protective role of the endogenous copper-/zinc-binding proteins, metallothioneins (MT), has been explored in relation to copper-induced α-synuclein aggregation.