Interaction between Proteasomal and Lysosomal Systems Can Be Modulated to Reduce Aß42 Effects in Hippocampal Slice Cultures
- UNCP Author/Contributor (non-UNCP co-authors, if there are any, appear on document)
- Heather Romine, Lab Manager and Research Specialist (Creator)
- Institution
- The University of North Carolina at Pembroke (UNCP )
- Web Site: http://www.uncp.edu/academics/library
Abstract: Intracellular protein clearance decreases with age, thus altering the vital balance between protein synthesis vs. degradation. Accumulating toxic proteins lead to the activation of proteasomal and lysosomal pathways for clearing such species. However, many studies indicate that the two pathways exhibit stress during AD-type protein accumulations. Surprisingly, instead of a decrease PADK appeared to cause a small increase in proteasome activity (control = 98.7±1.7, PADK = 115.3±12.4, N.S.). In slices with Aß42-mediated proteasomal compromise (34.7±5.2), PADK indeed enhanced the proteasome activity (73.0±10.0, p=0.027), to levels comparable to control slices. Such efficiency may involve cross-talk between proteasomes and lysosomes. Together, the results suggest a distinct interaction between proteasomal and lysosomal systems, and they point to potential dual modulation against protein accumulation pathology linked to Alzheimer’s disease and other dementias.
Interaction between Proteasomal and Lysosomal Systems Can Be Modulated to Reduce Aß42 Effects in Hippocampal Slice Cultures
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Created on 9/19/2017
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Additional Information
- Publication
- UNCP Research and Creativity Showcase
- Language: English
- Date: 2017
- Keywords
- Proteasomal and Lysosomal Systems, Aß42 Effects, Hippocampal Slice Cultures, Protein Accumulation Pathology, Z-Phe-Ala-diazomethylketone (PADK), Alzheimer’s Disease, Faculty Research, Poster Presentations, University of North Carolina at Pembroke