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The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

The Lipoprotein Receptor LR11 Regulates Amyloid β Production and Amyloid Precursor Protein Traffic in Endosomal Compartments

Offe, Katrin, Dodson, Sara E., Shoemaker, James T., Fritz, Jason J., Gearing, Marla, Levey, Allan I., Lah, James J.·2006·The Journal of Neuroscience
DOI 10.1523/jneurosci.4946-05.2006
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Abstract

Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by progressive cognitive decline and neuropathological changes, including the deposition of amyloid β (Aβ) in senile plaques. The mechanisms causing the disease and Aβ accumulation are not well understood, but important genetic associations with apolipoprotein E genotype and involvement of lipoprotein receptors have become apparent. LR11 (also known as SorLA), a member of the low-density lipoprotein receptor family, has been identified previously as an altered transcript in microarray analyses of samples from human AD cases. Here, we show neuronal expression of the lipoprotein receptor LR11 in control brain in regions vulnerable to AD neuropathology and marked reduction of LR11 expression in these regions in AD brains before cell death. Overexpression of LR11 drastically reduces levels of extracellular Aβ and also lowers levels of total cellular amyloid precursor protein (APP). LR11 colocalizes with APP and regulates its trafficking in endocytic compartments, which are important intracellular sites for APP processing and Aβ generation. Endogenous LR11 localizes to neuronal multivesicular bodies in both rat and human brain. The robust correlation between reduced LR11 expression and AD neuropathology and its potent effects on extracellular Aβ levels suggest that this neuronal lipoprotein receptor could play an important role in AD pathogenesis.

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  • Overexpression of SORL1 in neuronal and non-neuronal cell lines limits APP processing and decreases Aβ production.

    “On the other hand, overexpression of SORL1 in neuronal and non-neuronal cell lines limits the processing of APP, the Aβ precursor protein, and decreases Aβ production [5, 15, 18, 19].”

    From Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease (2021) · cites this paper as [18]

    The Results report that LR11 (SORL1) overexpression in HEK293 cells reduced full-length APP and extracellular Aβ, while the Discussion attributes the Aβ reduction to altered APP processing. The copy does not show these effects in an overexpressing neuronal cell line, and it reports increased APP fragments rather than an overall limit on APP processing. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • LR11/SorLA interacts with APP and affects its subcellular localization and proteolytic processing.

    “It was demonstrated that LR11/SorLA interacts with APP and affects its subcellular localization and proteolytic processing (Andersen et al., 2006;Offe et al., 2006;Spoelgen et al., 2006).”

    From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as Offe et al., 2006

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Metadata

Authors
Offe, K., Dodson, S. E., Shoemaker, J. T., Fritz, J. J., Gearing, M., Levey, A. I., & Lah, J. J.
Venue
The Journal of Neuroscience
Publisher
Society for Neuroscience
Published
2006-02-01
Volume
26
Issue
5
Pages
1596-1603
ISSN
  • 0270-6474
  • 1529-2401
DOI
10.1523/jneurosci.4946-05.2006
Cited by
245
References
6
Language
en
Licence
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 181 d)

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