Double calcein-labeled bone cross section from a six-month-old female Hrpt2 cKO mouse. Bones were labeled ten days apart to measure the bone formation rate. The large cortical pits outlined in green stain are due to mature osteoblasts and osteocytes lacking the Hrpt2 gene, which is required for proper regulation of transcription. Image by Casey Droscha of the Williams lab. 56 Van Andel Research Institute | <strong>Scientific</strong> <strong>Report</strong>
JIYAN MA, PH.D. Dr. Ma earned his Ph.D. in biochemistry and molecular biology from the University of Illinois at Chicago. He was at Ohio State University from 2002 until he joined VARI in November 2013 as a Professor. STAFF ROMANY ABSKHARON, PH.D. AUDREY ANDERSON, B.S. KATELYN BECKER, M.S. AMANDINE ROUX, PH.D. JUXIN RUAN, PH.D. FEI WANG, PH.D. XINHE WANG, PH.D. RESEARCH INTERESTS Protein aggregation is a key pathological feature of a large group of late-onset neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. Our overall goals are to elucidate the molecular events leading to protein misfolding in the aging central nervous system; to understand the relationship between misfolded protein aggregates and neurodegeneration; and, to develop approaches to prevent, stop, or reverse protein aggregation and neurodegeneration in these devastating diseases. We study protein aggregates in prion diseases (transmissible spongiform encephalopathies). These are true infectious diseases that can spread from individual to individual and cause outbreaks. We have established an in vitro system to reconstitute prion infectivity with bacterially expressed prion protein plus defined cofactors. We use this system to dissect the essential components and the structural features of an infectious prion and to uncover the molecular mechanisms responsible for the prion strain and species barrier. Recently, the concept of prions has expanded to Parkinson’s and Alzheimer’s diseases. α-Synuclein has been suggested to spread the disease pathology in a prionlike manner from a sick cell to healthy ones. We want to understand the similarities and differences between prions and amyloidogenic proteins. We are investigating cellular factors that affect α-synuclein aggregation and the connections between various α-synuclein aggregated forms, their prion-like spread, and dopaminergic neuron degeneration. RECENT PUBLICATIONS Yu, Guohua, Ajun Deng, Wanbin Tang, Junzhi Ma, Chonggang Yuan, and Jiyan Ma. In press. Hydroxytyrosol induces phase II detoxifying enzyme expression and effectively protects dopaminergic cells against dopamine- and 6-hydroxydopamine induced cytotoxicity. Neurochemistry International. Yu, Guohua, Huiyan Liu, Wei Zhou, Xuewei Zhu, Chao Yu, Na Wang, Yi Zhang, Ji Ma, Yulan Zhao, et al. 2015. In vivo protein targets for increased quinoprotein adduct formation in aged substantia nigra. Experimental Neurology 271: 13–24. CENTER FOR NEURODEGENERATIVE SCIENCE 57
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PETER A. JONES, Ph.D., D.SC. CHIEF
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EVENTS AND AWARDS FUNDING Research!
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