Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 20, Pages 11039-11041Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.211352598
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Elucidation of the proteolytic processing of the amyloid beta -protein precursor (APP) has revealed that one of the two proteases (gamma -secretase) that cleave APP to release amyloid beta -protein (A beta) is likely to be presenilin. Presenilin also mediates the gamma -secretase-like cleavage of Notch receptors to enable signaling by their cytoplasmic domains. Therefore, APP and Notch may be the first identified substrates of a unique intramembranous aspartyl protease that has presenilin as its active-site component. In view of the evidence for a central role of cerebral build-up of A beta in the pathogenesis of Alzheimer's disease, this disorder appears to have arisen in the human population as a late-life consequence of the conservation of a critical developmental pathway.
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