PMID: 8994217Dec 20, 1996Paper

Enhanced aggregation of beta-amyloid-containing peptides by extracellular matrix and their degradation by the 68 kDa serine protease prepared from human brain

Neuroscience Letters
A MatsumotoR Matsumoto

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.

References

Jan 1, 1991·Annual Review of Biochemistry·L Kjellén, U Lindahl
Aug 18, 1995·Science·E Levy-LahadG D Schellenberg
May 15, 1993·Proceedings of the National Academy of Sciences of the United States of America·E H KooD J Selkoe
Jun 21, 1996·Neuroscience Letters·A MatsumotoH Baba

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Citations

Jan 1, 1998·The Neuroscientist : a Review Journal Bringing Neurobiology, Neurology and Psychiatry·R Douglas Fields
May 17, 2017·Current Cardiology Reports·Paco E Bravo, Sharmila Dorbala
Jun 22, 1999·The Journal of Biological Chemistry·R YaminC R Abraham
Feb 6, 2019·Scientific Reports·Tamás LetohaLászló Szilák

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