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Consequences of Intracellular Amyloid in Alzheimer's Disease addresses one of the more currently unresolved aspects confounding Alzheimer's research, the significance of intraneuronal amyloid. It seeks to explain some of the unresolved questions concerning intracellular amyloid and its origin, entry, and toxicity. Following up on Dr. D'Andrea's first book, Bursting Neurons and Fading Memories: An Alternative Hypothesis for the Pathogenesis of Alzheimer's Disease, this book further examines the Inside-Out or Bursting alternative hypothesis of how amyloid escapes the circulatory system to ultimately enter neurons, also examining whether there is a relationship between intracellular amyloid, amyloid plaques, and cognitive impairment. Through a comprehensive explanation of the currently relevant scientific research on intracellular amyloid compiled in this handy reference, readers will better understand the mechanisms that lead to neuron death. - Presents the latest research on the significance of intracellular amyloid as it relates to Alzheimer's - Addresses crucial questions about intracellular amyloid, including how if forms and enters neurons, its toxicity, if it triggers cell death, and how amyloid plaques are formed - Examines the potential relationship between intracellular amyloid, plaques, and cognitive impairment in an effort to answer whether Alzheimer's is initially a problem of amyloid, the neuron, or of the blood-brain barrier - Seeks to help researchers generate additional alternative therapeutic opportunities to cure Alzheimer's

Amyloid-forming proteins are implicated in over 30 human diseases. The proteins involved in each disease have unrelated sequences and dissimilar native structures, but they all undergo conformational alterations to form fibrillar polymers. The fibrillar assemblies accumulate progressively into disease-specific lesions in vivo. Substantial evidence suggests these lesions are the end state of aberrant protein folding whereas the actual disease-causing culprits likely are soluble, non-fibrillar assemblies preceding the aggregates. The non-fibrillar protein assemblies range from small, low-order oligomers to spherical, annular, and protofibrillar species. Oligomeric species are believed to mediate various pathogenic mechanisms that lead to cellular dysfunction, cytotoxicity, and cell loss, eventuating in disease-specific degeneration and systemic morbidity. The particular pathologies thus are determined by the afflicted cell types, organs, systems, and the proteins involved. Evidence suggests that the oligomeric species may share structural features and possibly common mechanisms of action. In many cases, the structure–function interrelationships amongst the various protein assemblies described in vitro are still elusive. Deciphering these intricate structure–function correlations will help understanding a complex array of pathogenic mechanisms, some of which may be common across different diseases albeit affecting different cell types and systems.

This authoritative volume contains 179 chapters by international experts on recent developments in our understanding of amyloid proteins, protein folding disorders, and new and proposed clinical trials in amyloidosis. Topics include detection and characterization techniques; biological functions; genetics; disorders, diagnosis, and treatments, incl