engleski

Heat shock proteins 70 induce pro-inflammatory maturation program in decidual CD1a+ dendritic cells

The aim of the study was to assess possible binding of a mixture of constitutive Hsc70 and inducible Hsp70 forms (HSP70) to Toll-like receptor (TLR) 4 and CD91 receptors on decidual CD1a+ dendritic cells (DCs) and their influence on DCs maturation status. Immunohistology and immunofluorescence of paraffin-embedded first trimester and term pregnancy decidua were performed together with flow cytometry detection of antigens in DCs after stimulation of decidual mononuclear cells with HSP70. Hsc70 and Hsp70 labeling revealed intracellular and nuclear staining in trophoblast cells. The numbers of Hsc70+ and Hsp70+ cells of decidual tissue were higher in early pregnancy decidua than in decidua at term. HSP70 binds CD91 and TLR4 receptors on CD1a+ DCs and increased the expression of CD83, HLA-DR, CD80, and CD86, but decreased CC receptor (CCR) 5. HSP70 increased CC ligand (CCL) 3 and CCL22. HSP70 in the concentration of 1 lg/mL increased the percentage of interferon-c and interleukin (IL)-15-expressing cells over the cells expressing IL-4. HSP70 binds CD91 and TLR4 on decidual CD1a+ DCs, causes their maturation, and increases IL-15 in the context of Th1 cytokine/chemokine domination, which could support immune response harmful for ongoing pregnancy.

Antigen-presenting cells ; chemokine ; cytokine ; HSP70 ; interleukin-15 ; pregnancy

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