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Part of the book series: Heat Shock Proteins ((HESP,volume 1))

Abstract

Cytosolic heat shock proteins and endoplasmic reticulum resident chaperones (collectively referred as to Heat Shock Proteins or HSPs) control the folding and prevent the aggregation of proteins. Tumor-derived HSPs, released by dying cells or purified from tumor cells, induce protective anti-tumoral immune responses. This property of HSPs is related to their ability to chaperone tumor-derived peptides and to be internalized, in a receptor-dependent manner, by antigen-presenting cells. Studies were thus focused on identifying HSP-binding elements. Several members of the scavenger receptor family, including CD91, LOX-1, SREC-I, SR-A and CD36, were shown to bind different HSPs and to mediate their internalization. Among these receptors, CD91 and LOX-1 were also demonstrated involved in antigen-processing and MHC I presentation. HSPs activate immune cells but SR do not appear involved in this process. In conclusion, due to their ability to target APC and to cross-present exogenous antigens and to their adjuvant properties, HSPs are considered as ideal vaccine vehicles to generate anti-tumor and anti-viral protective immune responses

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Delneste, Y., Jaillon, S., Jeannin, P. (2007). Heat Shock Proteins and Scavenger Receptors. In: Asea, A.A., Maio, A.D. (eds) Heat Shock Proteins: Potent Mediators of Inflammation and Immunity. Heat Shock Proteins, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-5585-0_6

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