HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine

By A. Asea, S. Kraeft, E. Kurt-Jones, M. Stevenson, L. Chen, R. Finberg, G. Koo, Stuart K. Calderwood. Nature Medicine, 2000

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How researchers see this paper

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Pathogen Recognition and Inflammatory Signaling in Innate Immune Defenses (2009, background): “Indeed, endogenous HSPs are upregulated and released by stressed, infected, necrotic, or malignant cells and mediate activation of APCs through TLR2 and TLR4/CD14 either directly or in association with PAMPs (22, 110, 279).”
Age-related inflammatory cytokines and disease. (2003, background): “It has been demonstrated that the 70-kDa heat shock protein (HSP70) acts as a cytokine [164].”
Invited review: Effects of heat and cold stress on mammalian gene expression. (2002, background): “This suggests that HSP70 can function as a proinflammatory cytokine when released from injured cells or when secreted by activated immune cells (4).”
Medical application of functionalized magnetic nanoparticles. (2005, neutral): “through CD14 and/or CD91 receptors (62).”