Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-7-21
pubmed:abstractText
The amyloid beta peptide (A beta) is a central player in Alzheimer's disease (AD) pathology. A beta liberation depends on APP cleavage by beta- and gamma-secretases. The low density lipoprotein receptor related protein 1 (LRP1) was shown to mediate APP processing at multiple steps. Newly synthesized LRP1 can interact with APP, implying an interaction between these two proteins early in the secretory pathway. We wanted to investigate whether LRP1 mediates APP trafficking along the secretory pathway, and, if so, whether it affects APP processing. Indeed, the early trafficking of APP within the secretory pathway is strongly influenced by its interaction with the C-terminal domain of LRP1. The LRP1-construct expressing an ER-retention motif, LRP-CT KKAA, had the capacity to retard APP traffic to early secretory compartments. In addition, we provide evidence that APP metabolism occurs in close conjunction with LRP1 trafficking, highlighting a new role of lipoprotein receptors in neurodegenerative diseases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1095-953X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
188-97
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:18559293-Alzheimer Disease, pubmed-meshheading:18559293-Amino Acid Motifs, pubmed-meshheading:18559293-Amyloid beta-Peptides, pubmed-meshheading:18559293-Amyloid beta-Protein Precursor, pubmed-meshheading:18559293-Animals, pubmed-meshheading:18559293-Brain, pubmed-meshheading:18559293-CHO Cells, pubmed-meshheading:18559293-Cell Compartmentation, pubmed-meshheading:18559293-Cricetinae, pubmed-meshheading:18559293-Cricetulus, pubmed-meshheading:18559293-Glycosylation, pubmed-meshheading:18559293-Humans, pubmed-meshheading:18559293-Low Density Lipoprotein Receptor-Related Protein-1, pubmed-meshheading:18559293-Neurons, pubmed-meshheading:18559293-Plaque, Amyloid, pubmed-meshheading:18559293-Protein Processing, Post-Translational, pubmed-meshheading:18559293-Protein Structure, Tertiary, pubmed-meshheading:18559293-Protein Transport, pubmed-meshheading:18559293-Signal Transduction
pubmed:year
2008
pubmed:articleTitle
LRP1 modulates APP trafficking along early compartments of the secretory pathway.
pubmed:affiliation
Institute of Physiological Chemistry and Pathobiochemistry, Molecular Neurodegeneration, Johannes Gutenberg-University Mainz, 55099 Mainz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't