Abstract
To explore whether extracellular matrix components in human brain affect the deposition and aggregation of beta-amyloid containing peptides, human brain samples from patients with sporadic Alzheimer's disease and normal aged were analyzed by Western blot analysis. All major beta-amyloid-containing peptides contained epitope(s) which is recognized by anti heparan sulfate antibody. Incubation of brain beta-amyloid-containing peptides with human collagen type IV in neutral pH efficiently generated a high molecular weight aggregated band, approximately 5-fold that of the control sample. We have previously found a serine protease which is capable of cleaving an oligopeptide at the N-terminus of beta-amyloid. In this study, the protease, which also contains heparan sulfate glycoconjugates, degraded the above brain peptides as natural substrates, although with different efficiency. These findings suggest that extra-cellular matrix components affect the processing and aggregation of beta-amyloid-containing peptides in human brain.
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