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Originally published In Press as doi:10.1074/mcp.M700077-MCP200 on October 13, 2007.
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Molecular & Cellular Proteomics 7:15-34, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

The in Vivo Brain Interactome of the Amyloid Precursor Protein*,S

Yu Baia,b,c, Kelly Markhama,b, Fusheng Chena, Rasanjala Weerasekeraa,d,e, Joel Wattsa,d, Patrick Hornea, Yosuke Wakutania, Rick Bagshawa,d,f, Paul M. Mathewsg, Paul E. Frasera,h,i, David Westawayj, Peter St. George-Hyslopa,k,l and Gerold Schmitt-Ulmsa,d,m

From the a Centre for Research in Neurodegenerative Diseases and Departments of d Laboratory Medicine and Pathobiology, h Medical Biophysics, k Medicine (Neurology), University of Toronto, Ontario M5S 3H2, Canada, g New York University School of Medicine, Orangeburg, New York 10962, j Alberta Centre for Prions and Protein Folding Diseases, University of Alberta, Alberta T6G 2M8, Canada, and l Toronto Western Hospital Research Institute, Toronto Western Hospital, Toronto, Ontario M5S 3H2, Canada

Despite intense research efforts, the physiological function and molecular environment of the amyloid precursor protein has remained enigmatic. Here we describe the application of time-controlled transcardiac perfusion cross-linking, a method for the in vivo mapping of protein interactions in intact tissue, to study the interactome of the amyloid precursor protein (APP). To gain insights into the specificity of reported protein interactions the study was extended to the mammalian amyloid precursor-like proteins (APLP1 and APLP2). To rule out sampling bias as an explanation for differences in the individual datasets, a small scale quantitative iTRAQ (isobaric tags for relative and absolute quantitation)-based comparison of APP, APLP1, and APLP2 interactomes was carried out. An interactome map was derived that confirmed eight previously reported interactions of APP and revealed the identity of more than 30 additional proteins that reside in spatial proximity to APP in the brain. Subsequent validation studies confirmed a physiological interaction between APP and leucine-rich repeat and Ig domain-containing protein 1, demonstrated a strong influence of Ig domain-containing protein 1 on the proteolytic processing of APP, and consolidated similarities in the biology of APP and p75.


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