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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
Published on: October 17, 2015
Posttranslational modifications of the amyloid precursor protein : glycosylation
C Liu1, T Rozmyslowicz, M Stwora-Wojczyk
1Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA.
Abstract:
Many studies have demonstrated the importance of amyloid precurser protein (APP) in the pathogenesis of Alzheimer's disease. Nonetheless, the exact mechanism by which APP contributes to the pathogenesis of Alzheimer's disease is still not clear. Because APP is a glycoprotein, and because glycosylation can be important in the cell biology of individual glycoproteins (for review, see refs. 1 and 2), it is possible that changes in APP glycosylation during development and aging are important in APP biosynthesis, proteolysis, and degradation. However, few studies have addressed this issue (3 -8). This chapter provides methods for analyzing the glycosylation of APP that is actively synthesized by living cells in tissue culture. These methods can be applied to primary cultures, continuous cell lines, and transfected cell lines expressing recombinant APP.
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