Gladstone/UCSF team discovers interaction of two brain proteins may be key factor in development of Alzheimer's disease

ous systems that affects some four million Americans and is the fourth leading cause of death among adults in the U.S. It causes progressive mental deterioration that culminates in dementia, robbing people of their ability to think and share thoughts with others. There is no cure, and current treatments offer only limited hope of alleviating the devastating effects of the disease.

The cells in this study were neurons, which are necessary for the processing and storage of information in the brain. They had been genetically altered to express wild-type human APP or a mutant APP found in a type of early-onset AD that runs in families. When the neurons were exposed to stimuli that induce cell death, wild-type APP--but not mutant APP--protected the cells by inhibiting the ability of p53 to switch on the cell suicide machinery. "The inability of mutant APP to control p53 activation may help to explain, at least in part, why Alzheimer's-linked APP mutations result in the early onset of neurodegenerative disease," Mucke said. "The next step will be to determine if the APP mutations directly impair the protective function of APP or rather counteract it by increasing a neurotoxic APP breakdown product."

The new research findings relate to an earlier study by Mucke, Roger Nicoll, MD, UCSF professor of pharmacology and physiology, and their colleagues in the UCSF neuroscience program. Published in the March 1999 issue of PNAS, it focused on the amyloid-beta peptide, or A-beta, a breakdown product of APP.

Production of A-beta is increased by AD-linked APP mutations. The peptide accumulates in the brains of Alzheimer's victims, forming roundish deposits, called plaques, which have long been suspected of causing the memory loss and disturbed thinking that characterize the disease.

A correlation between cognitive decline and accumulation of A-beta in brain plaques has been reported by some researchers, but many other scien

Contact: Corinna Kaarlela
University of California - San Francisco

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