Abstract
Beta-amyloid is released into the brains of Alzheimer's patients, where it aggregates and causes damage to neurons. It is cleaved proteolytically from a large transmembrane glycoprotein amyloid precursor protein by a membrane-bound protease, known as beta-secretase identified previously as the acid protease, Asp-2. We have shown previously that beta-secretase is up-regulated by increased intracellular cholesterol, and down-regulated by cholesterol biosynthesis inhibition. Here we show using mass spectrometry that discrete changes in the glycosylation and palmitoylation of beta-secretase occur when cells expressing it are treated with statins.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alzheimer Disease / enzymology*
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Alzheimer Disease / genetics
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Amyloid Precursor Protein Secretases
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Amyloid beta-Protein Precursor / metabolism
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Anticholesteremic Agents / pharmacology
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Aspartic Acid Endopeptidases
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Cell Line
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Cholesterol / pharmacology
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Endopeptidases / chemistry
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Endopeptidases / metabolism*
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Glycoside Hydrolases / metabolism
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Glycosylation
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Humans
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Lovastatin / pharmacology
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Mass Spectrometry
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Membrane Microdomains / enzymology
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Mutation
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Palmitates / metabolism
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Protein Processing, Post-Translational
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Recombinant Proteins / chemistry
Substances
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Amyloid beta-Protein Precursor
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Anticholesteremic Agents
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Palmitates
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Recombinant Proteins
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Cholesterol
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Lovastatin
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Glycoside Hydrolases
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Amyloid Precursor Protein Secretases
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Endopeptidases
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Aspartic Acid Endopeptidases
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BACE1 protein, human