Literature DB >> 21318518

Posttranslational modifications of the amyloid precursor protein : glycosylation.

C Liu1, T Rozmyslowicz, M Stwora-Wojczyk, B Wojczyk, S L Spitalnik.   

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.

Entities:  

Year:  2000        PMID: 21318518     DOI: 10.1385/1-59259-195-7:169

Source DB:  PubMed          Journal:  Methods Mol Med        ISSN: 1543-1894


  1 in total

1.  N-Glycosylation Regulates the Trafficking and Surface Mobility of GluN3A-Containing NMDA Receptors.

Authors:  Kristyna Skrenkova; Sanghyeon Lee; Katarina Lichnerova; Martina Kaniakova; Hana Hansikova; Martin Zapotocky; Young Ho Suh; Martin Horak
Journal:  Front Mol Neurosci       Date:  2018-06-04       Impact factor: 5.639

  1 in total

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