MedicalResearch.com Interview with: Wenquan Zou, MD/PhD, Professor Department of Pathology Associate Director National Prion Disease Pathology Surveillance Center Case Western Reserve University School of Medicine Cleveland, Ohio 44106 MedicalResearch.com: What is the background for this study? Response: Parkinson’s disease (PD) is the second most common age-related neurodegenerative disorder. It is characterized by the accumulation of pathologically misfolded α-synuclein (αSynP) aggregates in the brain. Currently, a definite diagnosis relies on the detection of αSynP-containing Lewy bodies in the brain of PD patients. Development of a reliable and sensitive assay for αSynP in easily accessible peripheral tissue specimens is critical for early or differential diagnosis, determination of disease severity, and evaluation of therapeutic efficacy in clinical trials. Previous studies have revealed that the pathologically phosphorylated α-synuclein is detectable with traditional immunohistochemistry (IHC) and immunofluorescence (IF) microscopy but the sensitivity with IHC/IF is highly variable and inconsistent. Also the prion-like aggregation seeding activity of αSynP is detected in cerebrospinal fluid (CSF) of Parkinson’s disease patients with highly sensitive real-time quaking-induced conversion (RT-QuIC) and protein misfolding cyclic amplification assays (PMCA). But the lumbar puncture to collect CSF is more invasive compared to skin punch biopsy. (more…)