Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: Evidence for the participation of heparan sulfate proteoglycans

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dc.contributor.authorCaceres, J
dc.contributor.authorBrandan, E
dc.date.accessioned2025-01-21T01:33:21Z
dc.date.available2025-01-21T01:33:21Z
dc.date.issued1997
dc.description.abstractThe interaction between the Alzheimer amyloid precursor protein (APP) and an intact extracellular matrix (ECM), matrigel, obtained from Engelbreth-Holm-Swarm tumors was evaluated. Based on quantitative analyses of the binding data obtained from solid phase binding assays, two binding sites on the ECM were identified for [I-125]-APP (with apparent Kd(1) of 1.0 x 10(-11) M and Kd(2) of 1.6 x 10(-9) M respectively). Over 70% of [I-125]-APP was displaced by heparin and N-desulfated heparin but not by chondroitin sulfate. Pretreatment of matrigel with heparitinase decreased the binding of [I-125]-APP by 80%. beta-amyloid peptides (residues 1-40, 1-28, and 1-16) containing a heparin binding domain also displaced 80% of bound [I-125]-APP, which was totally displaced by intact APP. The binding of [I-125]-APP to matrigel increased by 210% with a decrease in the pH. These observations suggest that [I-125]-APP interacts mainly with heparan sulfate proteoglycan present in the ECM. The binding of [I-125]-APP to individual ECM components was also analyzed. [I-125]-APP was found to bind laminin and collagen type IV but not fibronectin. However, when these ECM constituents were combined, the extent of APP-binding decreased significantly, to levels comparable to those obtained with intact matrigel, suggesting that multiple interactions may occur between ECM constituents and [I-125]-APP. The results are discussed in terms of APP function and amyloidogenesis. (C) 1997 Wiley-Liss, Inc.
dc.fuente.origenWOS
dc.identifier.eissn1097-4644
dc.identifier.issn0730-2312
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97411
dc.identifier.wosidWOS:A1997WW58000002
dc.issue.numero2
dc.language.isoen
dc.pagina.final158
dc.pagina.inicio145
dc.revistaJournal of cellular biochemistry
dc.rightsacceso restringido
dc.subjectAlzheimer's disease
dc.subjectheparan sulfate proteoglycans
dc.subjectbeta-amyloid
dc.subjectextracellular matrix
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleInteraction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: Evidence for the participation of heparan sulfate proteoglycans
dc.typeartículo
dc.volumen65
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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