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Uptake of Aβ 1–40‐ and Aβ 1–42‐coated yeast by microglial cells: a role for LRP
Author(s) -
Laporte Vincent,
Lombard Yves,
LevyBenezra Rachel,
Tranchant Christine,
Poindron Philippe,
Warter JeanMarie
Publication year - 2004
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.1203620
Subject(s) - internalization , scavenger receptor , peptide , yeast , phagocytosis , biology , opsonin , receptor , amyloid (mycology) , senile plaques , microbiology and biotechnology , biochemistry , lipoprotein , biophysics , cholesterol , alzheimer's disease , pathology , medicine , botany , disease
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.