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The microtubule-associated protein tau is required for microtubule assembly, axonal transport, neurite outgrowth, and stability of microtubules (Binder et al. 1985). Tau selfassembly, aggregation, and accumulation in neurofibrillary tangles (NFTs) are major pathological hallmarks of Alzheimer disease (AD) and other neurodegenerative diseases (Lee et al. 2001, Alonso et al. 2008). Although the importance of tau in AD and other tauopathies is well established (Iqbal et al. 2009, Ballatore et al. 2007, Haroutunian et al. 2007) still unanswered is whether NFTs are the primary neurotoxic factor (Brunden et al. 2008, Marx 2007, Kayed & Jackson 2009). Despite the poor correlation between NFTs and disease progression, and evidence showing, that neuronal loss in AD actually precedes NFTs formation research until recently focused on them and other large meta-stable inclusions composed of aggregated hyperphosphorylated tau protein. Lately, the significance and toxicity of NFTs have been challenged and new aggregated tau entity has emerged as the true pathogenic species in tauopathies and a possible mediator of A┚ toxicity in AD. Tau intermediate aggregate (tau oligomers; aggregates of an intermediate that is between monomers and NFTs in size) can cause neurodegeneration and memory impairment in the absence of A┚. This exciting body of evidence includes results from human brain samples, transgenic mouse and cell-based studies, thus tau oligomers present a new and novel drug target for AD treatment. In this chapter, we summarize the characterization and toxicity of tau oligomers; discuss the evidence supporting their critical role in AD pathogenesis, and the potential and challenges for targeting them by immunotherapy and drug discovery as a novel approach for AD treatment

Tau Oligomers as Potential Drug Target for Alzheimer Disease (AD) Treatment