Journal of Clinical and Cellular Immunology
Open Access
ISSN: 2155-9899
ISSN: 2155-9899
Wen-Quan Zou
Department of Pathology and National Prion Disease
Pathology Surveillance Center
Case Western Reserve University
2085 Adelbert Road, Cleveland, Ohio 44106
USA
Dr. Wen-Quan Zou received his medical degree from Jiangxi Medical College, his M.Sc. from Tongji Medical University, and his Ph.D. from Shanghai Medical University. He has practiced Internal Medicine and Nephrology for six years in Nanchang and Shanghai, China, as both a physician and an attending physician, respectively. His post-doctoral work in neurodegenerative diseases, with a concentration in prion diseases, was done at the Institute of Pathology at Case Western Reserve University and at the Centre for Research in Neurodegenerative Diseases at University of Toronto. Currently, Dr. Zou is an Associate Professor of Pathology with tenure and Associate Director of the National Prion Disease Pathology Surveillance Center at Case Western Reserve University School of Medicine.
Dr. Zou's research focus is in the areas of protein aggregation in the conformational diseases especially on the physiological and pathologic prion proteins (PrPC and PrPSc) in prion diseases (PrD) as well as on neurotoxic amyloid β (Aβ) in Alzheimer disease (AD). The co-existence of PrPC and PrPSc in the central nervous system is a prerequisite for PrD, a group of fatal transmissible neurodegenerative diseases such as Creutzfeldt-Jakob disease (CJD) in humans, scrapie in sheep and goat, bovine spongiform encephalopathy in cattle, and chronic wasting disease in deer and elk. His laboratory is the first to demonstrate that small amounts of insoluble aggregates and protease-resistant conformers of PrP called insoluble PrPC(iPrPC) are present in normal human brains (Yuan et al., 2006). The discovery of this new isoform of PrPC may conceivably open a new frontier for investigating the pathogenesis of PrD. For instance, his laboratory also observed that a new protease-resistant PrPSc species with an immunoreactivity behavior and fragmentation similar to iPrPC is present in an atypical sporadic human prion disease termed variably protease-sensitive prionopathy and a familial prion disease (Zou et al., 2010; Zou et al., 2011; Xiao et al., 2013; Zou et al., 2013) and a relative early-stage of a subset sporadic prion disease (Yuan et al., 2008). Remarkably, the Zou laboratory revealed for the first time that iPrPC is the major PrP species that interacts with Aβ in AD and that human PrP exhibits two types of Aβ-binding sites on in terms of its specificity for Aβ42 (Zou et al., 2011). Currently, the Zou laboratory is studying the role of iPrPC in the pathogenesis of both PrD and AD using patient-specific iPSCs-derived neurons as well as in the ischemia reperfusion injury of tissues and organs.