A novel way found to prevent protein plaques implicated in A...(the on-line November 18 2007 edition of ...)

The first study was performed by Dr. Levy in collaboration with other investigators at the Nathan S. Kline Institute for Psychiatric Research and New York University School of Medicine. The second study was performed by Dr. Levy and colleagues in the laboratory of Dr. Mathias Jucker at the Hertie-Institute for Clinical Brain Research in Tubingen, Germany.

Both studies used mice that were genetically engineered to produce human cystatin C as well as abundant amounts of amyloid beta plaques in their brains. The cystatin C bound to the soluble, non-pathological form of amyloid beta in these mice and inhibited the aggregation and deposition of amyloid beta plaques in the brain.

The research shows that cystatin C binds soluble amyloid beta also in the human brain, and suggests that this binding inhibits its aggregation into insoluble plaques in humans, says Dr. Levy. Cystatin C production and body fluid levels vary among healthy individuals and can be influenced by certain hormones, aging, and certain pathological conditions, she says. Furthermore, it was recently demonstrated that a genetic variation in the cystatin C gene in human populations is linked to a greater risk of developing Alzheimers disease during aging.

These findings suggest, says Dr .Levy, that even subtle modifications of cystatin C protein levels could affect amyloid beta accumulation and deposition in the brain, thereby modifying disease progression.

Cystatin C is found in all body fluids and tissues of mammals. It is a jack-of-all-trades, playing a broad role in many functions, including cell proliferation and growth, modulation of the inflammatory response, and bone resorption. The protein also has been implicated in neuronal degeneration and repair of the nervous system.

The work of Dr. Levy and colleagues offers important
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