Journal article

Presenilin I expression in yeast lowers secretion of the amyloid precursor protein

G Evin, D Le Brocque, JG Culvenor, D Galatis, A Weidemann, K Beyreuther, CL Masters, R Cappai

NEUROREPORT | LIPPINCOTT WILLIAMS & WILKINS | Published : 2000

Abstract

Presenilin (PS) mutations are associated with early-onset Alzheimer's disease and PS proteins are involved with gamma-secretase cleavage of the amyloid precursor protein, APP. We have shown previously that alpha-, beta- and gamma-secretase cleavages of APP are conserved in Pichia pastoris. Here, we report co-expression of APP and PSI in P. pastoris and show by immunoelectron microscopy colocalization of these two proteins in expanded endoplasmic reticulum. Western blot analysis indicates a drastic reduction of both alpha- and beta-secretase products. A relative increase in beta-secretase product derived from immature APP is also observed, pointing to a beta-secretase activity of P. pastoris ..

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