Abstract
Human heat shock protein 60 (Hsp60) elicits a pro-inflammatory response in innate immune cells. This response includes the release of inflammatory mediators like tumor necrosis factor α, interleukin (IL-)1β, IL-6 and nitric oxide. Hsp60 also has been found to induce the gene expression of the T helper (Th)1-phenotype promoting cytokines IL-12 and IL-15. Detailed studies identified specific receptor structures for the interaction of Hsp60 with innate immune cells. Accumulating evidence points to the presence of different receptor structures, which are involved in Hsp60-binding and in the Hsp60-mediated initiation of a pro-inflammatory response. These findings indicate that the interaction of Hsp60 with innate immune cells is a highly complex process. Recently, the epitopes of the Hsp60 molecule responsible for binding to innate immune cells and for the activation of these cells have been characterized. In a cell-type-specific manner, the region aa481–500 and the regions aa241–260, aa391–410 and aa461–480 were identified to account for Hsp60-binding to innate immune cells. A completely different region of Hsp60, aa354–365 was found to be involved in specific LPS-binding, thereby mediating the immunostimulatory effects of Hsp60 on innate immune cells. Because of the immunomodulatory properties of Hsp60 it has been proposed to act as an intercellular danger signal, regulating innate and adaptive immune reactions, thereby contributing to the induction and progression of inflammatory diseases
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Habich, C., Burkart, V. (2007). Interaction of Heat Shock Protein 60 with Innate Immune Cells. 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_8
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DOI: https://doi.org/10.1007/978-1-4020-5585-0_8
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