alexa Disruption Of Proteostatic Networks In Alzheimer?s Disease
ISSN: 2161-0460

Journal of Alzheimers Disease & Parkinsonism
Open Access

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2nd International Conference on Alzheimers Disease and Dementia
September 23-25, 2014 Valencia Convention Centre, Spain

David R Borchelt and Guilian Xu
ScientificTracks Abstracts: J Alzheimers Dis Parkinsonism
DOI: 10.4172/2161-0460.S1.006
Abstract
The extracellular accumulation of ?-amyloid peptide is a key trigger in the pathogenesis of Alzheimer?s disease (AD) that precedes the appearance of intracellular protein aggregate pathology formed by proteins such as Tau, ?-synuclein, and TDP-43. These latter pathologies are potentially a consequence of diminished function of protein homeostatic machinery. We developed a sequential detergent extraction method, followed by SDS-PAGE separation of the various fractions, in-gel trypsin digestions, and LC-MS/MS proteomic approaches to identify proteins that lose solubility in the brains of APPswe/PS1dE9 (line 85) mice with high amyloid burden. This protocol was initially used in a study of two neural cell lines, SH-SY5Y neuroblastoma and STTG-1 glioblastoma, that were exposed to mild heat-shock, leading to the identification of a number of cytosolic proteins that rapidly lost solubility and could be viewed as being sensitive to disturbances in proteostasis. Using the same approach on our APPswe/PS1dE9 model of Alzheimer amyloidosis, we identified numerous cytosolic proteins involved in glycolysis as well as 14-3-3 proteins and other chaperones that show specific losses in solubility as amyloid accumulates. These data provide in vivo evidence that the accumulation of extracellular amyloid can lead to diminished function of the intracellular protein homeostasis network. Ongoing studies in culture cell models may provide additional insight into the mechanisms by which amyloid disrupts proteostasis.
Biography
David R Borchelt has been with the University of Florida since April of 2005 after 13 years on the faculty of Johns Hopkins University School of Medicine. He has authored, or co-authored, more than 100 research papers focusing on human neurodegenerative disorders. He gained his PhD from the University of Kentucky in 1986, where he studied the viruses that are similar to the virus that causes AIDS. After receiving his doctorate, he worked as a post-doctoral fellow with Dr. Stanley Prusiner at the University of California in San Francisco. In 1999, he won the Nobel Prize in Medicine for his work on infectious proteins that cause Mad Cow disease, Cruetzfeldt-Jakob disease, and other neurodegenerative diseases of animals and humans. During his time with Dr. Prusiner, he produced some of the seminal work on prion protein that supported this hypothesis. From this work, he began to realize that most human neurodegenerative diseases, including amyotrophic lateral sclerosis, Huntington?s disease, and Alzheimer?s disease, share similarities with prion disease in that the symptoms and pathology are caused by the accumulation of proteins in altered conformations.
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