Soluble derivatives of the beta amyloid protein precursor of Alzheimer's disease are labeled by antisera to the beta amyloid protein
| Autor: | Marcia B. Podlisny, Sandra L. Siedlak, Steven G. Younkin, Dennis J. Selkbe, Earl R. Shelton, Barry D. Greenberg, Hardy W. Chan, M. F. Usiak, Mark R. Palmert, George Perry |
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| Rok vydání: | 1989 |
| Předmět: |
Amyloid
Molecular Sequence Data Biophysics Biochemistry Residue (chemistry) Amyloid beta-Protein Precursor Epitopes Cytosol Alzheimer Disease Amyloid precursor protein medicine Humans Protease Inhibitors Amino Acid Sequence Protein Precursors Molecular Biology Antiserum Gel electrophoresis biology Chemistry Immune Sera P3 peptide Brain Membrane Proteins Cell Biology medicine.disease Membrane protein biology.protein Alzheimer's disease Oligopeptides |
| Zdroj: | Biochemical and biophysical research communications. 165(1) |
| ISSN: | 0006-291X |
| Popis: | The amyloid deposited in Alzheimer's disease (AD) is composed primarily of a 39-42 residue polypeptide (beta AP) that is derived from a larger beta amyloid protein precursor (beta APP). In previous studies, we and others identified full-length, membrane-associated forms of the beta APP and showed that these forms are processed into soluble derivatives that lack the carboxyl-terminus of the full-length forms. In this report, we demonstrate that the soluble approximately 125 and approximately 105 kDa forms of the beta APP found in human cerebrospinal fluid are specifically labeled by several different antisera to the beta AP. This finding indicates that both soluble derivatives contain all or part of the beta AP sequence, and it suggests that one or both of these forms may be the immediate precursor of the amyloid deposited in AD. |
| Databáze: | OpenAIRE |
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