A mycobacterial heat shock protein 70-based fusion protein targeting mesothelin induces dendritic cell maturation and cross-presentation in a murine model of ovarian carcinoma

2014 ◽  
Vol 133 ◽  
pp. 90
Author(s):  
N. Hashim Arrifin ◽  
J. Yuan ◽  
S. Kashiwagi ◽  
M. Nguyen ◽  
G. Jean-Mary ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Fusion Protein ◽  
Murine Model ◽  
Heat Shock Protein 70 ◽  
Protein Targeting ◽  
Dendritic Cell Maturation ◽  
Cell Maturation ◽  
Cross Presentation

scholarly journals Control of cross-presentation during dendritic cell maturation

2004 ◽  
Vol 34 (2) ◽  
pp. 398-407 ◽  
Author(s):  
Beatriz C. Gil-Torregrosa ◽  
Ana Maria Lennon-Duménil ◽  
Benedikt Kessler ◽  
Pierre Guermonprez ◽  
Hidde L. Ploegh ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Dendritic Cell Maturation ◽  
Cell Maturation ◽  
Cross Presentation

Human platelets express heat shock protein receptors and regulate dendritic cell maturation

Blood ◽  
2002 ◽  
Vol 99 (10) ◽  
pp. 3676-3682 ◽  
Author(s):  
Norbert Hilf ◽  
Harpreet Singh-Jasuja ◽  
Petra Schwarzmaier ◽  
Cécile Gouttefangeas ◽  
Hans-Georg Rammensee ◽  
...  
Keyword(s):  
Heat Shock ◽  
Immune Responses ◽  
Heat Shock Protein ◽  
Chronic Inflammation ◽  
Proinflammatory Cytokines ◽  
Human Platelets ◽  
Dendritic Cell Maturation ◽  
Cell Contact ◽  
Cross Presentation ◽  
Endogenous Proteins

Immunizations using the endoplasmic reticulum–resident heat shock protein Gp96 induce specific immune responses. Specificity is based on the major histocompatibility complex class I–restricted cross-presentation of Gp96-associated peptides derived from endogenous proteins. Initiation of the immune response depends on the ability of Gp96 to induce the production of proinflammatory cytokines by macrophages and dendritic cells (DCs) and of their maturation in a fashion presumably independent of associated peptide. Both events are mediated by Gp96 receptors on antigen-presenting cells. It is known that Gp96 is released from cells at necrosis induced, for example, by virus infection. Although this event supports the efficient induction of immune responses, it might also interfere with processes that are susceptible to chronic inflammation, such as wound healing after tissue damage. Therefore, Gp96-mediated stimulation of the immune system requires tight regulation. Here we show that human thrombocytes specifically interact with Gp96 and that binding of Gp96 to platelets is enhanced more than 10-fold on activation by thrombin. Gp96 interferes with neither thrombin-induced platelet activation nor platelet aggregation. However, the presence of platelets during Gp96-mediated DC activation reduces the secretion of proinflammatory cytokines and the activation of DCs. This effect is independent of soluble platelet factors and cell-to-cell contact between DCs and thrombocytes. Thus, we provide evidence for a regulatory mechanism that neutralizes Gp96 molecules systemically, especially in the blood. This effect might be of significance in wounds in which chronic inflammation and immune responses against autoantigens have to be prevented.

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