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S2–03–06: Functional and structural analysis of γ–secretase
Author(s) -
Steiner Harald,
Winkler Edith,
Yamasaki Aya,
Shirotani Keiro,
Revuelta Blanca Perez,
Tomioka Masanori,
Haass Christian
Publication year - 2006
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2006.05.093
Subject(s) - presenilin , nicastrin , protein subunit , biochemistry , chemistry , proteolysis , amyloid precursor protein , cleavage (geology) , amyloid precursor protein secretase , biology , microbiology and biotechnology , enzyme , alzheimer's disease , gene , disease , medicine , paleontology , pathology , fracture (geology)
not available. S2-03-06 FUNCTIONAL AND STRUCTURAL ANALYSIS OF -SECRETASE Harald Steiner, Edith Winkler, Aya Yamasaki, Keiro Shirotani, Blanca Perez Revuelta, Masanori Tomioka, Christian Haass, LudwigMaximilians-University, Adolf-Butenandt-Institute, Munich, Germany. Contact e-mail: hsteiner@med.uni-muenchen.de Background: -Secretase catalyzes the intramembrane cleavage of a large variety of type I membrane proteins including the Alzheimer s disease -amyloid precursor protein. Biochemical and genetic studies demonstrated that -secretase is a complex composed of presenilin (PS), nicastrin (NCT), APH-1 and PEN-2. In human cells, two PS homologues, PS1 and PS2, and two APH-1 homologues, APH-1a and APH-1b, were identified and shown to be part of distinct -secretase complexes demonstrating that -secretase represents a heterogeneous activity. Apart from the established role of PS as the catalytic subunit of -secretase and the recently proposed role of NCT as substrate receptor, knowledge about the function of the other subunits within the complex, in particular regarding the mechanism S27 Symposia S2-03: Disease Mechanisms (Presenilins/ -Secretase)