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Uptake of Aβ 1–40- and Aβ 1–42-coated yeast by microglial cells: a role for LRP

Laporte, Vincent, Lombard, Yves, Levy-Benezra, Rachel, Tranchant, Christine, Poindron, Philippe, Warter, Jean-Marie·2004·Journal of Leukocyte Biology
DOI 10.1189/jlb.1203620
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Abstract

Artificial diffuse and amyloid core of neuritic plaques [β-amyloid peptide (Aβ) deposits] could be prepared using heat-killed yeast particles opsonized with Aβ 1–40 or Aβ 1–42 peptides. Interaction and fate of these artificial deposits with microglial cells could be followed using a method of staining that allows discrimination of adherent and internalized, heat-killed yeast particles. Using this system, it was possible to show that nonfibrillar or fibrillar (f)Aβ peptides, formed in solution upon heating (aggregates), could not impair the internalization of heat-killed yeast particles opsonized with fAβ 1–40 or fAβ 1–42. This indicated that depending on their physical state, Aβ peptide(s) do not recognize the same receptors and probably do not follow the same internalization pathway. Using competitive ligands of class A scavenger receptors (SR-A) or low-density lipoprotein-related receptor protein (LRP), it has been shown that SR-A were not involved in the recognition of amyloid peptide deposits, whereas LRP specifically recognized deposits of fAβ 1–42 (but not fAβ 1–40) and mediated their phagocytosis.

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Metadata

Authors
Laporte, V., Lombard, Y., Levy-Benezra, R., Tranchant, C., Poindron, P., & Warter, J.-M.
Affiliations
Laboratoire de Pathologie des Communications entre Cellules Nerveuses et Musculaires, EA 3429, Faculté de Pharmacie , Cedex, France
Venue
Journal of Leukocyte Biology
Publisher
Oxford University Press (OUP)
Published
2004-05-10
Volume
76
Issue
2
Pages
451-461
ISSN
  • 0741-5400
  • 1938-3673
DOI
10.1189/jlb.1203620
Cited by
27
References
8
Language
en
Licence
academic.oup.com/pages/standard-publication-reuse-rights (vor)

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