Abstract
The first genetic lesions associated with Alzheimer’s disease were in the coding sequence of the β amyloid precursor protein (βAPP) [1]. Although these mutations account for a small proportion of familial Alzheimer (FAD) cases, they conceptually solidified the link between this protein and the pathology of the disease. As the source of the amyloid β peptide (Aβ) that accumulates in plaques, βAPP had garnered attention for several years. The mutations were immediately presumed to contribute to disease by modifying Aβ production, but increased understanding of the bioactivities of βAPP itself have led to models that do not depend on Aβ for Alzheimer pathogenesis. Both Aβ and non-amyloidogenic derivatives of βAPP can have an impact on proinflammatory glial activation. Indeed, the role of inflammatory reactions in Alzheimer’s has been lent additional credence by indications of such reactions in mice transgenic for βAPP. These interactions will be reviewed and discussed here in the context of cell biology; protein-protein interactions between Aβ and α2-macroglobulin or components of the complement cascade are addressed in accompanying chapters of this volume.
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Barger, S.W. (2001). Proinflammatory actions of derivatives of the β amyloid precursor protein. In: Rogers, J. (eds) Neuroinflammatory Mechanisms in Alzheimer’s Disease Basic and Clinical Research. Progress in Inflammation Research. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8350-4_8
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