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Liu C, Rozmyslowicz T, Stwora-Wojczyk M, et al. Posttranslational modifications of the amyloid precursor protein : glycosylation. Methods Mol Med. 2000;32:169-90doi: 10.1385/1-59259-195-7:169.
Liu, C., Rozmyslowicz, T., Stwora-Wojczyk, M., Wojczyk, B., & Spitalnik, S. L. (2000). Posttranslational modifications of the amyloid precursor protein : glycosylation. Methods in molecular medicine, 32169-90. https://doi.org/10.1385/1-59259-195-7:169
Liu, C, et al. "Posttranslational modifications of the amyloid precursor protein : glycosylation." Methods in molecular medicine vol. 32 (2000): 169-90. doi: https://doi.org/10.1385/1-59259-195-7:169
Liu C, Rozmyslowicz T, Stwora-Wojczyk M, Wojczyk B, Spitalnik SL. Posttranslational modifications of the amyloid precursor protein : glycosylation. Methods Mol Med. 2000;32:169-90. doi: 10.1385/1-59259-195-7:169. PMID: 21318518.
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Methods Mol Med. 2000;32:169-90. doi: 10.1385/1-59259-195-7:169.

Posttranslational modifications of the amyloid precursor protein : glycosylation.

Methods in molecular medicine

C Liu, T Rozmyslowicz, M Stwora-Wojczyk, B Wojczyk, S L Spitalnik

Affiliations

  1. Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA.

PMID: 21318518 DOI: 10.1385/1-59259-195-7:169

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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