Heat-shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell-cycle control and signaling, and protection of cells against stress/apoptosis.

Heat shock proteins (HSPs) are small polypeptide groups that are classified into families based on molecular weight. HSPs have been classified into several families including small HSPs, HSP40, HSP47, calreticulin, HSP60, HSP70, disease, immunology, oncology, and autoimmunity, heat shock proteins are relatively unstudied in the field of endodontics.

Immunological function of HSPs

The immunological function of HSPs was first observed by Srivastava et al. in the study of HSPs in anti-tumor immunity. Mice immunized with tumor derived HSPs rejected the subsequent challenge with the same tumor. Whereas normal tissue derived HSPs did not protect mice from tumor challenge. This has been verified in a series of studies using gp96, HSP70, HSP90, calreticulin, HSP110 and GRP 170 (21-25). HSP-mediated tumor specific immunogenicity is dependent on CD8+ T cells and macrophages in the priming phase, and on CD4+, CD8+ T cells and macrophages in the effector phase. Preparation of HSPs from a tumor was associated with peptides derived from the tumor specific antigens (Ags). Thus it has been proposed that HSPs function as Ag chaperones to channel peptides into APCs and induce T cell activation. Consistent with this proposition, HSP peptide complexes reconstituted in vitro can elicit Ag-specific CD8+ T cell responses.

Another line of evidence supporting the immunogenicity of HSPs comes from the study of the effects of fever-range hyperthermia on immune responses. Hyperthermia increases trafficking of effector cells to the site of inflammation, accelerates migration of Langerhans’ cells to the draining lymph nodes and promotes an Ag-specific T cell response. Given the fact that hyperthermia induces expression of HSPs, the up-regulation of immune response by hyperthermia highly indicates the immunological functions of HSPs.


Zheng, Hong. "Heat shock proteins in dendritic cell activation and antigen cross-presentation." (2003).

Goodman, Steven Chad.The role of heat shock proteins in periapical disease. Diss. The University of Texas School of Dentistry at Houston, 2013.

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