Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins |
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Authors: | Keiko Akasaka-Manya Hiroshi Manya Yoko Sakurai Boguslaw S. Wojczyk Steven L. Spitalnik Tamao Endo |
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Affiliation: | (1) Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, 35-2 Sakaecho, Itabashi-ku, Tokyo 173-0015, Japan;(2) Department of Pathology and Cell Biology, Columbia University Medical Center, New York, NY 10032, USA |
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Abstract: | Alteration of glycoprotein glycans often changes various properties of the glycoprotein. To understand the significance of N-glycosylation in the pathogenesis of early-onset familial Alzheimer’s disease (AD) and in β-amyloid (Aβ) production, we examined whether the mutations in the amyloid precursor protein (APP) gene found in familial AD affect the N-glycans on APP. We purified the secreted forms of wild-type and mutant human APPs (both the Swedish type and the London type) produced by transfected C17 cells and determined the N-glycan structures of these three recombinant APPs. Although the major N-glycan species of the three APPs were similar, both mutant APPs contained higher contents of bisecting N-acetylglucosamine and core-fucose residues as compared to wild-type APP. These results demonstrate that familial AD mutations in the polypeptide backbone of APP can affect processing of the attached N-glycans; however, whether these changes in N-glycosylation affect Aβ production remains to be established. Keiko Akasaka-Manya and Hiroshi Manya contributed equally to this work. |
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Keywords: | Amyloid precursor protein N-glycan Alzheimer’ s disease Bisecting N-acetylglucosamine Core-fucose |
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