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Down-regulation of the amyloid protein precursor of Alzheimer's disease by antisense oligonucleotides reduces neuronal adhesion to specific substrata |
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| Authors: | Elizabeth J. Coulson Graham L. Barrett Elsdon Storey Perry F. Bartlett Konrad Beyreuther Colin L. Masters |
| Affiliation: | a Department of Pathology, The University of Melbourne, Parkville, Victoria 3052, Australia b The Mental Health Research Institute, Parkville, Victoria 3052, Australia c The Walter and Eliza Hall Institute, Royal Parade, Parkville, Victoria 3050, Australia d The Co-operative Research Centre for Cellular Growth Factors, Parkville, Victoria 3050, Australia e Center for Molecular Biology (ZMBH), INF 282, The University of Heidelberg, 69120 Heidelberg, Germany |
| 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--lysine. It remains to be determined whether this effect is the direct result of APP-matrix interactions, or whether an intermediary pathway is involved. |
| Keywords: | Heparan sulphate proteoglycan Collagen Laminin Fibronectin Murine |
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