TAILIEUCHUNG - Báo cáo khoa học: In vitro gamma-secretase cleavage of the Alzheimer’s amyloid precursor protein correlates to a subset of presenilin complexes and is inhibited by zinc

Thec-secretase complex mediates the final proteolytic event in Alzheimer’s disease amyloid-bbiogenesis. This membrane complex of presenilin, ante-rior pharynx defective, nicastrin, and presenilin enhancer-2 cleaves the C-terminal 99-amino acid fragment of the amyloid precursor protein intra-membranously atc-sites to form C-terminally heterogeneous amyloid-b and cleaves at ane-site to release the intracellular domain or e-C-terminal fragment. | iFEBS Journal In vitro gamma-secretase cleavage of the Alzheimer s amyloid precursor protein correlates to a subset of presenilin complexes and is inhibited by zinc David E. Hoke Jiang-Li Tan Nancy T. Ilaya Janetta G. Culvenor Stephanie J. Smith Anthony R. White Colin L. Masters and Genevieve M. Evin Department of Pathology The University of Melbourne and the MentalHealth Research Institute Parkville Victoria Australia Keywords Alzheimer s disease amyloid precursor protein gamma-secretase amyloid beta Correspondence D. E. Hoke Department of Microbiology Monash University Clayton Vic 3800 Australia Fax 61 39905 4811 Tel 61 39905 4807 E-mail G. M. Evin Department of Pathology The University of Melbourne Parkville Vic 3010 Australia Fax 61 38344 4004 Tel 61 38344 4205 E-mail gmevin@ Received 20 May 2005 revised 4 August 2005 accepted 30 August 2005 doi The y-secretase complex mediates the final proteolytic event in Alzheimer s disease amyloid-b biogenesis. This membrane complex of presenilin anterior pharynx defective nicastrin and presenilin enhancer-2 cleaves the C-terminal 99-amino acid fragment of the amyloid precursor protein intra-membranously at y-sites to form C-terminally heterogeneous amyloid-b and cleaves at an e-site to release the intracellular domain or e-C-terminal fragment. In this work two novel in vitro y-secretase assays are developed to further explore the biochemical characteristics of y-secretase activity. During development of a bacterial expression system for a substrate based on the amyloid precursor protein C-terminal 99-amino acid sequence fragments similar to amyloid-b and an e-C-terminal fragment were observed. Upon purification this substrate was used in parallel with a transfected source of substrate to measure y-secretase activity from detergent extracted membranes. With these systems it was determined that recovery of size-fractionated cellular and .

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