TY - JOUR
T1 - A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease
AU - Cottrell, Barbara A.
AU - Galvan, Veronica
AU - Banwait, Surita
AU - Gorostiza, Olivia
AU - Lombardo, Christian R.
AU - Williams, Tristan
AU - Schilling, Birgit
AU - Peel, Alyson
AU - Gibson, Bradford
AU - Koo, Edward H.
AU - Link, Christopher D.
AU - Bredesen, Dale E.
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/8
Y1 - 2005/8
N2 - Several approaches have been used in an effort to identify proteins that interact with β-amyloid precursor protein (APP). However, few studies have addressed the identification of proteins associated with APP in brain tissue from patients with Alzheimer's disease. We report the results of a pilot proteomic study performed on complexes immunoprecipitated with APP in brain samples of patients with Alzheimer's disease and normal control subjects. The 21 proteins identified could be grouped into five functional classes: molecular chaperones, cytoskeletal and structural proteins, proteins involved in trafficking, adaptors, and enzymes. Among the proteins identified, six had been reported previously as direct, indirect, or genetically inferred APP interactors. The other 15 proteins immunoprecipitated with APP were novel potential partners. We confirmed the APP interaction by Western blotting and coimmunolocalization in brain tissues, for 5 of the 21 interactors. In agreement with previous studies, our results are compatible with an involvement of APP in axonal transport and vesicular trafficking, and with a potential association of APP with cellular protein folding/protein degradation systems.
AB - Several approaches have been used in an effort to identify proteins that interact with β-amyloid precursor protein (APP). However, few studies have addressed the identification of proteins associated with APP in brain tissue from patients with Alzheimer's disease. We report the results of a pilot proteomic study performed on complexes immunoprecipitated with APP in brain samples of patients with Alzheimer's disease and normal control subjects. The 21 proteins identified could be grouped into five functional classes: molecular chaperones, cytoskeletal and structural proteins, proteins involved in trafficking, adaptors, and enzymes. Among the proteins identified, six had been reported previously as direct, indirect, or genetically inferred APP interactors. The other 15 proteins immunoprecipitated with APP were novel potential partners. We confirmed the APP interaction by Western blotting and coimmunolocalization in brain tissues, for 5 of the 21 interactors. In agreement with previous studies, our results are compatible with an involvement of APP in axonal transport and vesicular trafficking, and with a potential association of APP with cellular protein folding/protein degradation systems.
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U2 - 10.1002/ana.20554
DO - 10.1002/ana.20554
M3 - Article
C2 - 16049941
AN - SCOPUS:23244456099
VL - 58
SP - 277
EP - 289
JO - Annals of Neurology
JF - Annals of Neurology
SN - 0364-5134
IS - 2
ER -