**Therapy**

**Chapter 11**

**Potential Therapeutic Strategies to**

Additional information is available at the end of the chapter

Ester Aso and Isidre Ferrer

http://dx.doi.org/10.5772/54783

**1. Introduction**

most the telencephalon.

in the formation of neuropil threads.

**Prevent the Progression of Alzheimer to Disease States**

Alzheimer is an age-dependent neurodegenerative process distinct from normal aging and characterized morphologically by the presence of senile plaques and neurofibrillary tangles, which progress from the brain stem and inner parts of the temporal lobes to

Senile plaques are mainly composed of different species of fibrillar β-amyloid (Aβ), a product of the cleavage of the β-amyloid precursor protein (APP), and they are surrounded by dystrophic neurites, reactive astrocytes and microglia. Aβ fibrillar deposits also occur in diffuse plaques, subpial deposits and in the wall of the cerebral and meningeal blood vessels in the form of amyloid angiopathy. A substantial part of β-amyloid is not fibrillar but soluble

Neurofibrillary tangles are mainly composed of various isoforms of tau protein, which is hyper-phosphorylated and nitrated. It has an altered conformation and is truncated at different sites through the action of a combination of several proteolytic enzymes giving rise to species of low molecular weight which are toxic to nerve cells. Abnormal tau deposition also occurs in the dystrophic neurites of senile plaques and within the small neuronal processes, resulting

The mechanisms of disease progression are not completely understood but Aβ initiates the pathological process in the small percentage of familial cases due to mutations in genes encoding APP, presenilin 1 and presenilin 2, the latter involved in the cleavage of APP, and potentiates tau phosphorylation in sporadic cases that represent the majority of affected individuals (β-amyloid cascade hypothesis). Moreover, Aβ act as a seed of new β-amyloid production and deposition under appropriate settings, and abnormal tau promotes the

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© 2013 Aso and Ferrer; licensee InTech. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

© 2013 The Author(s). Licensee InTech. This chapter is distributed under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution,

and forms oligomers of differing complexity which are toxic to nerve cells.

**Chapter 11**
