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Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
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Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
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Journal Article
Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
2000
Overview
The β-amyloid precursor protein (β-APP), which is involved in the pathogenesis of Alzheimer’s disease, and the Notch receptor, which is responsible for critical signalling events during development, both undergo unusual proteolysis within their transmembrane domains by unknown γ-secretases. Here we show that an affinity reagent designed to interact with the active site of γ-secretase binds directly and specifically to heterodimeric forms of presenilins, polytopic proteins that are mutated in hereditary Alzheimer’s and are known mediators of γ-secretase cleavage of both β-APP and Notch. These results provide evidence that heterodimeric presenilins contain the active site of γ-secretase, and validate presenilins as principal targets for the design of drugs to treat and prevent Alzheimer’s disease.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Alzheimer Disease - drug therapy
/ Alzheimer Disease - enzymology
/ Amyloid beta-Peptides - metabolism
/ Amyloid beta-Protein Precursor - genetics
/ Amyloid beta-Protein Precursor - metabolism
/ Amyloid Precursor Protein Secretases
/ Animals
/ Aspartic Acid Endopeptidases
/ Biomedical and Life Sciences
/ Humans
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Peptide Fragments - chemistry
/ Peptide Fragments - metabolism
/ Protease Inhibitors - chemistry
/ Protease Inhibitors - metabolism
/ Protease Inhibitors - pharmacology
/ Protease Inhibitors - therapeutic use
