TITLE

Immunotherapeutic Strategies for Prevention and Treatment of Alzheimer's Disease

AUTHOR(S)
Solomon, Beka
PUB. DATE
November 2001
SOURCE
DNA & Cell Biology;Nov2001, Vol. 20 Issue 11, p697
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Pathologic examination in Alzheimer's disease (AD) shows a significant correlation between �-amyloid peptide (A�P) deposition and the clinical severity of dementia. Formation of �-amyloid (A�) is a complex kinetic and thermodynamic process, dependent on peptide�peptide interactions that may be modulated by other proteins. We found that site-directed antibodies toward peptide EFRH sequences 3�6 of the N-terminal region of A�P suppress in vitro formation of A� and dissolve already-formed fibrillar amyloid. These so-called chaperone-like properties of monoclonal antibodies led to the development of a new immunologic approach to AD treatment. The immunization procedure, based on phages displaying the EFRH epitope as antigen, induced anti-A�P antibodies that recognized the whole A�P and exhibited antiaggregating properties similar to those of antibodies obtained by injection of A� fibrils. Production and performance of anti-�-amyloid antibodies in the transgenic mouse model of AD showed that these antibodies may be delivered from the periphery to the central nervous system, preventing the formation of A� and dissolving already-present aggregates. Moreover, immunization with A� protected transgenic mice from the learning and age-related memory deficits that occur in AD. These data support the hypotheses that A� plays a central role in AD and that site-directed antibodies that modulate A� conformation may provide immunotherapy of the disease.
ACCESSION #
5849366

 

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