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CD91 Is a Common Receptor for Heat Shock Proteins gp96, hsp90, hsp70, and Calreticulin
Abstract
Complexes of the heat shock protein gp96 and antigenic peptides are taken up by antigen-presenting cells and presented by MHC class I molecules. In order to explain the unusual efficiency of this process, the uptake of gp96 had been postulated to occur through a receptor, identified recently as CD91. We show here that complexes of peptides with heat shock proteins hsp90, calreticulin, and hsp70 are also taken up by macrophages and dendritic cells and re-presented by MHC class I molecules. All heat shock proteins utilize the CD91 receptor, even though some of the proteins have no homology with each other. Postuptake processing of gp96-chaperoned peptides requires proteasomes and the transporters associated with antigen processing, utilizing the classical endogenous antigen presentation pathway.
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LRP1 is a plasma membrane receptor mediating endocytosis, phagocytosis, chemotaxis and signaling for extracellular ligands including ApoE, lipoproteins, α2-macroglobulin, proteases, extracellular matrix proteins, growth factors, complement factors, heat shock proteins and dozens of other natural ligands.
“Low density lipoprotein (LDL) receptor related protein 1 (LRP1) is a plasma membrane receptor mediating endocytosis, phagocytosis, chemotaxis and signaling for extracellular ligands, including apolipoprotein E (ApoE), lipoproteins, α2-macroglobulin, proteases, extracellular matrix proteins, growth factors, complement factors, heat shock proteins and dozens of other natural ligands (1–5).”
From LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation (2023) · cites this paper as [2]
LRP1 and related LDL family receptors regulate a wide range of cellular processes, including endocytosis, phagocytosis, chemotaxis and signaling in response to dozens of ligands.
“Outside the brain, LRP1 and related LDL family receptors regulate a wide range of cellular processes, including endocytosis, phagocytosis, chemotaxis and signaling in response to dozens of ligands (1–4).”
From LRPAP1 is released from activated microglia and inhibits microglial phagocytosis and amyloid beta aggregation (2023) · cites this paper as [2]
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Metadata
- Authors
- Basu, S., Binder, R. J., Ramalingam, T., & Srivastava, P. K.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 14
- Issue
- 3
- Pages
- 303-313
- ISSN
- 1074-7613
- Cited by
- 900
- References
- 0
- Language
- en
- Licence
- Funders
- National Institutes of Health (CA64394)
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