Down-regulation of the amyloid protein precursor of Alzheimer's disease by antisense oligonucleotides reduces neuronal adhesion to specific substrata
- Author(s)
- Coulson, EJ; Barrett, GL; Storey, E; Bartlett, PF; Beyreuther, K; Masters, CL;
- Details
- Publication Year 1997-10-03,Volume 770,Issue #1-2,Page 72-80
- Journal Title
- BRAIN RESEARCH
- Publication Type
- Journal Article
- Abstract
- The hallmark of Alzheimer's disease is the cerebral deposition of amyloid which is derived from the amyloid precursor protein (APP). The function of APP is unknown but there is increasing evidence for the role of APP in cell-cell and/or cell-matrix interactions. Primary cultures of murine neurons were treated with antisense oligonucleotides to down-regulate APP. This paper presents evidence that APP mediates a substrate-specific interaction between neurons and extracellular matrix components collagen type I, laminin and heparan sulphate proteoglycan but not fibronectin or poly-L-lysine. It remains to be determined whether this effect is the direct result of APP-matrix interactions, or whether an intermediary pathway is involved. (C) 1997 Elsevier Science B.V.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- NERVE GROWTH-FACTOR; HEPARAN-SULFATE PROTEOGLYCAN; MESSENGER-RNA; NEURITE OUTGROWTH; CELL-SURFACE; BETA-PROTEIN; EXTRACELLULAR-MATRIX; DIFFERENTIAL EXPRESSION; HIPPOCAMPAL-NEURONS; CORTICAL-NEURONS
- Publisher's Version
- https://doi.org/10.1016/S0006-8993(97)00757-9
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1997-10-03 12:00:00