HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Published online before print May 10, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: jlb.1203620v1 76/2/451    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Laporte, V. Articles by Warter, J.-M. Search for Related Content PubMed PubMed Citation Articles by Laporte, V. Articles by Warter, J.-M.

(Journal of Leukocyte Biology. 2004;76:451-461.)
© 2004 by Society for Leukocyte Biology

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

Vincent Laporte^*, Yves Lombard^*, Rachel Levy-Benezra^*, Christine Tranchant^*,, Philippe Poindron^*,1 and Jean-Marie Warter^*,

^* Laboratoire de Pathologie des Communications entre Cellules Nerveuses et Musculaires, EA 3429, Faculté de Pharmacie, and
Clinique Neurologique 2, Service des maladies du Nerf et du Muscle, Hôpitaux Universitaires, Faculté de Médecine, Université Louis Pasteur de Strasbourg, Cedex, France

¹Correspondence: Laboratoire de Pathologie des Communications entre Cellules Nerveuses et Musculaires, EA 3429, Faculté de Pharmacie, Université Louis Pasteur, 74, route du Rhin-BP 24, F-67401 Illkirch, Cedex, France. E-mail: poindron{at}pharma.u-strasbg.fr

Artificial diffuse and amyloid core of neuritic plaques [ß-amyloid peptide (Aß) deposits] could be prepared using heat-killed yeast particles opsonized with Aß 1–40 or Aß 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)Aß peptides, formed in solution upon heating (aggregates), could not impair the internalization of heat-killed yeast particles opsonized with fAß 1–40 or fAß 1–42. This indicated that depending on their physical state, Aß 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 fAß 1–42 (but not fAß 1–40) and mediated their phagocytosis.

Key Words: amyloid ß-protein • senile plaque • Alzheimer’s disease • scavenger receptor A • phagocytosis • endocytosis