Medical chaperone blog9/12/2023 ![]() ![]() “We’re excited about using this new model of tauopathy in finding ways to restore chaperone protein balance to delay or stop the progression of Alzheimer’s and other neurodegenerative diseases.”ĭr. “The chaperone protein network is your cell’s natural defense to maintain homeostasis throughout life, and this study emphasizes the importance of protecting that balance in the aging brain,” said principal investigator Laura Blair, PhD, an assistant professor of molecular medicine at the USF Health Byrd Alzheimer’s Center, Morsani College of Medicine. Normally, co-chaperone proteins assist chaperone proteins in monitoring and sustaining the balance (homeostasis) of proteins critical to cell health. Hsp90 is a chaperone protein abundant in neurons and other cells in the brain. ![]() The findings, highlighted below, were reported April 8 in Acta Neuropathologica Communications. They modeled molecular chaperone imbalance by overexpressing production of Aha1 and FKBP52 in these old, wide-type mice. In this study the USF Health Morsani College of Medicine researchers used mice that were not genetically modified (wild-type mice) to examine the effects of Aha1 and FKBP52, two co-chaperone proteins of heat shock protein Hsp90, in the aging brain. In humans, misfolding of the protein tau leads to its toxic accumulation inside brain cells, the formation of these tau aggregates into hallmark neurofibrillary tangles, neuron death, and eventually symptoms of cognitive decline such as memory loss and diminished thinking skills. ![]() Laura Blair, PhD, assistant professor of molecular medicine at the USF Health Byrd Alzheimer’s Center, was principal investigator for the NIH-funded study published in Acta Neuropathologica Communications | Photo by Allison Long, USF Health Communications ![]()
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