Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-1-7
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid Precursor Protein Secretases, http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor, http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, http://linkedlifedata.com/resource/pubmed/chemical/Aplp1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Aplp2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/LINGO1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1535-9476
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-34
pubmed:dateRevised
2011-8-4
pubmed:meshHeading
pubmed-meshheading:17934213-Amino Acid Sequence, pubmed-meshheading:17934213-Amyloid Precursor Protein Secretases, pubmed-meshheading:17934213-Amyloid beta-Protein Precursor, pubmed-meshheading:17934213-Animals, pubmed-meshheading:17934213-Antibodies, pubmed-meshheading:17934213-Brain, pubmed-meshheading:17934213-Cross-Linking Reagents, pubmed-meshheading:17934213-Heat-Shock Proteins, pubmed-meshheading:17934213-Mass Spectrometry, pubmed-meshheading:17934213-Membrane Proteins, pubmed-meshheading:17934213-Mice, pubmed-meshheading:17934213-Molecular Chaperones, pubmed-meshheading:17934213-Molecular Sequence Data, pubmed-meshheading:17934213-Nerve Tissue Proteins, pubmed-meshheading:17934213-Peptides, pubmed-meshheading:17934213-Perfusion, pubmed-meshheading:17934213-Protein Binding, pubmed-meshheading:17934213-Protein Interaction Mapping, pubmed-meshheading:17934213-Protein Structure, Tertiary, pubmed-meshheading:17934213-Reproducibility of Results, pubmed-meshheading:17934213-Time Factors
pubmed:year
2008
pubmed:articleTitle
The in vivo brain interactome of the amyloid precursor protein.
pubmed:affiliation
Centre for Research in Neurodegenerative Diseases and Departments of Laboratory Medicine and Pathobiology, University of Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural