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TRAFFICKING AND ENDOCYTOSIS OF ALZHEIMER AMYLOID PRECURSOR PROTEIN pp. 1-38 $100.00
Authors:  Ritva Tikkanen, Antje Banning, Melanie Meister, Institute of Biochemistry, Medical Faculty, University of Giessen, Giessen, Germany
Abstract:
Alzheimer Amyloid Precursor Protein (APP) is a ubiquitously expressed transmembrane protein that is involved in the pathogenesis of Alzheimer's disease. Cellular trafficking of APP is mediated by several targeting signals in its cytoplasmic tail, which are responsible for the interaction with the targeting machineries. APP undergoes several proteolytic processing steps which are carried out by different enzymes. The pathological amyloid β-peptide is generated as a result of the sequential action of two proteases termed β- and γ- secretases. For the processing of APP by the β-secretase, endocytosis of APP from the plasma membrane is necessary, and the processing takes place in endosomal compartments. Recent findings have suggested that the cholesterol and sphingolipid rich membrane microdomains known as rafts would be important players in the regulation of the pathological processing of APP. In this chapter, we will focus on describing the targeting signals in APP that mediate its transport into different cellular organelles and domains by means of interaction with the targeting machineries. In addition, we will especially summarize the recent findings implicating the role of rafts in the proteolytic processing of APP and in the pathogenesis of Alzheimer's disease. 


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TRAFFICKING AND ENDOCYTOSIS OF ALZHEIMER AMYLOID PRECURSOR PROTEIN pp. 1-38