PMID: 8584202Aug 11, 1995Paper

A serine protease in Alzheimer's disease cells cleaves a 16K-peptide with flanking residues upstream to beta-amyloid-N-terminus as natural substrate

Neuroscience Letters
A MatsumotoY Fujiwara

Abstract

A serine protease which cleaves an oligopeptide at the beta-amyloid (beta A4) N-terminus was identified and purified from extracellular fluid of familial Alzheimer's disease (FAD) lymphoblastoid cells. In order to search for a natural substrate that stands for a direct precursor of beta A4, C-terminal fragments of beta-amyloid precursor protein (APP) were prepared by immunoprecipitation of cytosol proteins with beta A4-specific antibody. The 16 kDa peptide with N-terminus 30 amino acids upstream from the beta A4-N-terminus, also existing in other hematopoietic cells, was proved to be a natural substrate for the protease in human lymphoid cells. Its cleaved fragment with beta A4-N-terminus was thought to be less amyloidogenic on the basis of its property of self-aggregation in acidic pH. The results suggest the significance of the unique cleavage site at beta A4-upstreams in generation and accumulation of beta A4.

References

Feb 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·A TamaokaD J Selkoe
Dec 31, 1990·Biochemical and Biophysical Research Communications·J E GardellaP D Gorevic
Mar 15, 1991·Biochemical and Biophysical Research Communications·A Matsumoto, Y Fujiwara

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