AbstractBeta‐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.