Work

A calcium-activated protease from Alzheimer's disease brain cleaves at the N-terminus of the amyloid β-protein

Year: 1991

Type: article

Abstract: Alzheimer's disease, Down's syndrome, and to a far lesser extent, normal aged brains exhibit abnormal extracellular deposits of amyloid. The major component of brain amyloid is the beta-protein, a 4Kd fragment of the larger beta-protein precursor. The finding of the abnormally processed beta-protein and a protease inhibitor (alpha 1-antichymotrypsin) in the amyloid deposits prompted us to search for proteases which may generate the beta-protein from its precursor. We now report on the presence and partial purification of one such proteolytic activity from Alzheimer's brain. Normal physiologic C-terminal cleavage of the secreted form of the beta-protein precursor occurs in the middle of the beta-protein suggesting that the beta-protein accumulates due to an alternative degradation pathway. We propose here that the protease activity we describe participates in this abnormal pathway.

Source: Biochemical and Biophysical Research Communications

DOI: 10.1016/0006-291x(91)91487-w

Authors: Carmela R. Abraham, James Driscoll, Huntington Potter, William E. Van Nostrand, Paul Tempst

Institutions: Boston University, Harvard University, University of California, Irvine, Howard Hughes Medical Institute

Language: English

Topic: Alzheimer's disease research and treatments

Subfield: Cellular and Molecular Neuroscience

Field: Neuroscience

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,110