Cell surface APP751 forms complexes with protease nexin 2 ligands and is internalized via the low density lipoprotein receptor-related protein (LRP)
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Cited by (105)
Full-length amyloid precursor protein regulates lipoprotein metabolism and amyloid- clearance in human astrocytes
2018, Journal of Biological ChemistryRole of LRP1 in the pathogenesis of Alzheimer's disease: Evidence from clinical and preclinical studies
2017, Journal of Lipid ResearchCitation Excerpt :Accordingly, many interesting observations have been reported using cellular or animal models where LRP1 amount or function was biologically or genetically manipulated. Initial efforts were devoted to addressing the effects of LRP1 on APP trafficking and processing to Aβ by using cellular models, as it was known that LRP1 catabolizes tissue factor pathway inhibitor, and this protein shares the Kunitz protease inhibitor domain with the longer forms of APP (67–70). Blocking LRP1 function by RAP increased cell surface APP and reduced Aβ production in H4 cells stably expressing human APP (69).
The Amyloid β Precursor Protein and Cognitive Function in Alzheimer's Disease
2016, Genes, Environment and Alzheimer's DiseaseSorLA complement-type repeat domains protect the amyloid precursor protein against processing
2015, Journal of Biological ChemistryThe role of choroid plexus in IVIG-induced beta-amyloid clearance
2014, NeuroscienceCitation Excerpt :LRP1 serves as a receptor for these two proteins, and LRP1-mediated clearance of A2M and apoE contributes to a reduction in Aβ levels (Herz and Strickland, 2001). LRP1 may play a role in the BBB to transfer Aβ from the brain to the blood (Kounnas et al., 1995; Knauer et al., 1996; Goto and Tanzi, 2002; Moir and Tanzi, 2005; Yamada et al., 2009). Recently, LRP1 was identified in the CP.
Association of ApoE and LRP mRNA levels with dementia and AD neuropathology
2012, Neurobiology of AgingCitation Excerpt :Later studies with APP transgenic mice carrying human ApoE isoforms show an isoform-specific effect on Aβ accumulation (murine apoE > ApoE4 > ApoE3 > ApoE2), and supported the hypothesis that ApoE is critical for the development of fibrillar, compact amyloid plaques. LRP has also been shown to interact directly with the extracellular domain of APP through its Kunitz-type serine protease inhibitor (KPI) domain and also indirectly with the cytoplasmic tail of APP through a common adapter protein FE65 (Kinoshita et al., 2001; Knauer et al., 1996; Kounnas et al., 1995; Pietrzik et al., 2004; Trommsdorff et al., 1998). Interestingly, an increase in Kunitz-type serine protease inhibitor (KPI) containing isoforms of APP protein levels has been reported in AD (Harrison et al., 1996; Moir et al., 1998; Preece et al., 2004).