Heat-shock proteins (HSPs) induce protective cytotoxic immune responses against tumour antigens. This property is related to their ability to bind to and to be internalized by DC (dendritic cells) before gaining access to the MHC class I processing pathway, a process called antigen cross-presentation. This process requires internalization of the antigen by DC via endocytic receptors. Owing to their particular immune properties, several studies were focused on the identification of HSP-binding elements on DC. We and others have reported that scavenger receptors are the main HSP-binding structures on human DC and have identified LOX-1 as one of these molecules. The binding of human Hsp70 to DC and the in vitro Hsp70-mediated antigen cross-presentation are inhibited by an anti-LOX-1 monoclonal antibody. In vivo, targeting LOX-1 with a tumour antigen using an anti-LOX-1 monoclonal antibody induces antitumour immunity. Thus scavenger receptors are certainly new promising targets for cancer immunotherapy.
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August 2004
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Conference Article|
August 01 2004
Scavenger receptors and heat-shock protein-mediated antigen cross-presentation
Y. Delneste
Y. Delneste
1
1Unité INSERM U564, University Hospital of Angers, 4, rue Larrey, F-49933 Angers, France
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Publisher: Portland Press Ltd
Received:
April 16 2004
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2004 The Biochemical Society
2004
Biochem Soc Trans (2004) 32 (4): 633–635.
Article history
Received:
April 16 2004
Citation
Y. Delneste; Scavenger receptors and heat-shock protein-mediated antigen cross-presentation. Biochem Soc Trans 1 August 2004; 32 (4): 633–635. doi: https://doi.org/10.1042/BST0320633
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