Alpha-synuclein differentially reduces surface expression of N-methyl-d-aspartate receptors in the aging human brain.

The aging brain is associated with reduced cell surface expression of N-methyl-d-aspartate receptors (NMDARs), but the mechanism remains poorly understood. In the present study, we showed that in the striatum and hippocampus but not the cerebellum and parietal cortex, levels of α-synuclein monomers and oligomers increased with age, which correlated negatively with the expression of GluN1, and positively with the expression of total Rab5B. The oligomer-α-synuclein exhibited a stronger correlation with the expression of surface GluN1 and total Rab5B.

Alpha-synuclein oligomerization increases its effect on promoting NMDA receptor internalization.

The internalization of NMDA receptors (NMDARs) is promoted by monomeric α-synuclein (α-syn). Because of the pathogenic role of oligomeric α-syn, the effect of aggregated α-syn on this regulation deserves investigation. Several α-syn oligomers were prepared by incubating recombinant human α-syn in phosphate-buffered saline (PBS), plasma of normal controls (NC) and patients with Parkinson's disease (PD).

Identifying distinct candidate genes for early Parkinson's disease by analysis of gene expression in whole blood.

Objective: Parkinson disease (PD) is a degenerative disorder of the central nervous system, and in the majority of cases, the causes of PD are unknown. Coupled with impressive advances in statistical tools for analyzing large, complex data sets, well-designed microarray experiments are poised to make a big impact in the field of diseases. So we set the study to identify distinct PD-associated candidates.