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The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Mechanism mediating oligomeric Aβ clearance by naïve primary microglia

Yang, Cheng-Ning, Shiao, Young-Ji, Shie, Feng-Shiun, Guo, Bo-Shen, Chen, Pei-Hao, Cho, Chi-Yuan, Chen, Yi-Jen, Huang, Fong-Lee, Tsay, Huey-Jen·2011·Neurobiology of Disease
DOI 10.1016/j.nbd.2011.01.005
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Abstract

The accumulation of soluble oligomeric amyloid-β peptide (oAβ) proceeds the formation of senile plaques and contributes to synaptic and memory deficits in Alzheimer's disease (AD). The mechanism of mediating microglial oAβ clearance remains unclear and thought to occur via scavenger receptors (SRs) in microglia. SRs respond to their ligands in a subtype-specific manner. Therefore, we sought to identify the specific subtypes of SRs that mediate oAβ internalization and proteases that degrade oAβ species in naïve primary microglia. The component of oAβ species were characterized by western blot analysis, analytical ultracentrifugation analysis, and atomic force microscopy. The oAβ species remained soluble in the medium and microglial lysates during incubation at 37 °C. SR-A, but not CD36, mediated oAβ internalization in microglia as suggested by the use of subtype-specific neutralizing antibodies and small interfering RNAs (siRNAs). Immunoprecipitation analysis showed that oAβ interacted with SR-A on the plasma membrane. After internalization, over 40% of oAβ vesicles were trafficked toward lysosomes and degraded by cysteine proteases, including cathepsin B. The inhibitors of proteasome, neprilysin, matrix metalloproteinases, and insulin degrading enzyme failed to protect internalized oAβ from degradation. Our study suggests that SR-A and lysosomal cathepsin B are critical in microglial oAβ clearance, providing insight into how microglia are involved in the clearance of oAβ and…

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Crossref · 10.1016/j.nbd.2011.01.005

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  • Both neurons and glia can clear extracellular Ab through endocytosis for subsequent lysosomal degradation or secretion of amyloid-degrading enzymes for extracellular clearance.

    “We and others have shown that both neurons and glia can clear extracellular Ab through endocytosis for subsequent lysosomal degradation or secretion of amyloiddegrading enzymes for extracellular clearance (4,7).”

    From Differential protective effects of connective tissue growth factor against Aβ neurotoxicity on neurons and glia (2017) · cites this paper as [7]

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Metadata

Authors
Yang, C.-N., Shiao, Y.-J., Shie, F.-S., Guo, B.-S., Chen, P.-H., Cho, C.-Y., Chen, Y.-J., Huang, F.-L., & Tsay, H.-J.
Venue
Neurobiology of Disease
Publisher
Elsevier BV
Published
2011-06
Volume
42
Issue
3
Pages
221-230
ISSN
0969-9961
DOI
10.1016/j.nbd.2011.01.005
Cited by
117
References
19
Language
en
Licence
Funders
  • NSC (94-2321-B-010-006, and NSC99-2320-B-010-012)
  • Brain Research Center ((99ACB6-2))
  • Ministry of Education-Aim for the Top University Plan (98A-C-D105)
  • Mackey memorial hospital (MMH-YM-9903)

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