Affiliations: [a] Department of Neurology, Department of Laboratory Medicine, Donders Institute for Brain, Cognition and Behaviour, Alzheimer Centre Nijmegen, Radboud University Nijmegen Medical Centre, Nijmegen, the Netherlands | [b] Department of Pathology, Radboud University Nijmegen Medical Centre, Nijmegen, the Netherlands
Correspondence:
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Correspondence to: Nienke M. Timmer, Department of Neurology, 830 LGEM, Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. Tel.: +31 312 436 18786; Fax: +31 312 436 68754; E-mail: n.timmer@neuro.umcn.nl.
Note: [] Handling Associate Editor: Gary Arendash
Abstract: Senile plaques and cerebral amyloid angiopathy in Alzheimer's disease (AD) patients not only consist of the amyloid-β protein (Aβ), but also contain many different Aβ-associated factors, such as heparan sulfate proteoglycans, apolipoproteins, and complement factors. These factors may all influence Aβ deposition, aggregation, and clearance and therefore seem important in the development of human Aβ deposits. To study AD pathology and test new therapeutic agents, many different mouse models have been created. By transgenic expression of the amyloid-β protein precursor, frequently in combination with other transgenes, these animals develop Aβ deposits that morphologically resemble their human counterparts. Whether this resemblance also applies to the presence of Aβ-associated factors is largely unclear. In this review, the co-deposition of factors known to associate with human Aβ deposits is summarized for several different AD mouse models.
