Increased amyloid production from aberrant beta-amyloid precursor proteins
| Autor: | Diana Hom Quon, Ziyang Zhong, Jeffrey N. Higaki, L. S. Higgins, Barbara Cordell |
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| Rok vydání: | 1994 |
| Předmět: |
Gene isoform
Amyloid Immunoprecipitation Biology Sulfur Radioisotopes medicine.disease_cause Models Biological Biochemistry Cell Line Amyloid beta-Protein Precursor Neuroblastoma Methionine Chlorocebus aethiops mental disorders Tumor Cells Cultured medicine Amyloid precursor protein Animals Humans Secretion Cysteine Molecular Biology Secretory pathway chemistry.chemical_classification Mutation Amyloid beta-Peptides Cell Biology Recombinant Proteins Cell biology Molecular Weight Kinetics chemistry biology.protein Electrophoresis Polyacrylamide Gel Glycoprotein Protein Processing Post-Translational |
| Zdroj: | Journal of Biological Chemistry. 269:12179-12184 |
| ISSN: | 0021-9258 |
| Popis: | The 4-kDa beta-amyloid protein that forms fibrillar deposits in Alzheimer's diseased brains is derived from a large precursor, the beta-amyloid precursor protein (beta-APP). Recently, it has been reported that beta-amyloid is normally produced and secreted by cultured mammalian cells. In our studies involving recombinant expression of beta-APP, increased yields of beta-amyloid were associated with expression of aberrant beta-APP molecules. Deletion mutations within the beta-amyloid domain, incorrect beta-APP isoform expression in fibroblasts or neuronal cells, or excess amounts of beta-APP all led to increases in beta-amyloid production. Aberrant beta-APP appears to be diverted from the secretory pathway and then degraded to beta-amyloid. |
| Databáze: | OpenAIRE |
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