The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
α2‐Macroglobulin Enhances the Clearance of Endogenous Soluble β‐Amyloid Peptide via Low‐Density Lipoprotein Receptor‐Related Protein in Cortical Neuron
Abstract
Abstract : Apolipoprotein E and α 2‐macroglobulin (α2M) are genetic risk factors for late‐onset Alzheimer's disease, and both bind a cell surface receptor, the lowdensity lipoprotein receptor‐related protein (LRP). To investigate the role of LRP on preventing the accumulation of β‐amyloid peptide (Aβ), we examined the effects of α2M on the clearance of endogenous Aβ. Studies were performed in primary Tg2576 transgenic mouse cortical neuronal cultures expressing human mutant amyloid precursor protein (APP) 695. This system allowed us to follow endogenous Aβ using immunoblots to detect monomeric forms of the peptide. Aβ and APP levels were measured in conditioned media. We found that activated α2M (α2M*) substantially decreased soluble Aβ levels and had no effect on secreted or full‐length APP levels. Native α2M, which is not a ligand for LRP, did not affect Aβ levels. The receptor‐associated protein, which inhibits interaction of all ligands with LRP in vitro, prevented α2M*‐induced decreases of soluble Aβ levels. These data suggest that α2M* affects soluble Aβ clearance rather than Aβ production. Further studies showed that similar Aβ clearance via an LRP‐mediated pathway was observed after treatment with another LRP ligand, lactoferrin. Taken together, these data demonstrate that α2M* enhances the clearance of soluble Aβ via LRP in cortical neurons.
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In the citing paper
“they promote A b clearance in smooth muscle cells (35), neurons (36, 38), and fibroblasts (37)”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [38]
In the citing paper
“A role for LRP-1 in promoting A b clearance in vitro in smooth muscle cells, neurons, and fibroblasts via a 2M and apoE has been suggested (35-38), although at significantly slower rates than the A b transport across the BBB demonstrated in this study.”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [38]
In the citing paper
“Neuronal cells in vitro metabolize A b via an LRP-1-dependent mechanism that may require apoE or a 2M (38).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [38]
In the citing paper
“binding of A to LRP ligands, such as ␣2M or apoE, contributes to reduced A levels”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Qiu et al., 1999
In the citing paper
“In addition, LRP appears to be the main lipoprotein receptor responsible for A clearance (Narita et al., 1997b;Qiu et al., 1999)”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Qiu et al., 1999
In the citing paper
“although binding of Kunitz protease inhibitor (KPI) containing isoforms of APP (APP751 and APP770) to LRP results in increased A production”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Qiu et al., 1999
In the citing paper
“and blocking LRP with RAP significantly decreased ␣2M-dependent A clearance in primary neuronal cultures and glial cells (Narita et al., 1997a;Fabrizi et al., 1999;Qiu et al., 1999).”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Qiu et al., 1999
In the citing paper
“LRP also appears to mediate the clearance of Aβ that is bound to α2M or ApoE[19], [21]–[23].”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [21]
In the citing paper
“LRP also functions in the catabolism of Aβ peptides”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [21]
Citations
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Cited by
Sorted by citations
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Self-citationLRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms
Deane, R., Wu, Z., Sagare, A., Davis, J., Du Yan, S., Hamm, K., Xu, F., Parisi, M., LaRue, B., Hu, H. W., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.017 · Cited by 828
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Shinohara, M., Tachibana, M., Kanekiyo, T., & Bu, G. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075796 · Cited by 297
Kanekiyo, T., & Bu, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00093 · Cited by 281
Metadata
- Authors
- Qiu, Z., Strickland, D. K., Hyman, B. T., & Rebeck, G. W.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1999-10
- Volume
- 73
- Issue
- 4
- Pages
- 1393-1398
- ISSN
- 0022-3042
- 1471-4159
- Cited by
- 107
- References
- 2
- Language
- en
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