HSP60 participates in many interactions between the system integrated by all chaperones
and closely associated molecules (chaperoning system or CS) and the immune system (IS). These
interactions occur constantly to maintain normal cell physiology but, occasionally, they are perturbed
and become mediators of pathologic events that may lead to disease. This switch to pathology may be
initiated by various factors, genetic or acquired, which cause qualitative and/or quantitative
modifications of HSP60, or immune crossreactivity between the human and microbial chaperonin
orthologs, or a break in the balance between the pro- and anti-inflammatory actions of the chaperonin.
Thus, autoimmune and chronic inflammatory pathologies may occur. Likewise, a perturbation of the
CS-IS interactions, e.g., those that take place during ageing, may favor carcinogenesis. HSP60 may be
commandeered by tumor cells to assist its high-rate protein synthesis and, also, to be an emissary
among the devices tumor cells utilize to avoid anti-tumor immune reactions. Here, we briefly discuss
the canonical and non-canonical functions of HSP/chaperones; and HSP60 as a multifunctional
molecule, its migration itinerary, and its possible roles during carcinogenesis and in certain chronic
inflammatory and autoimmune diseases. We examine the potential of HSP60 as a biomarker useful for
diagnosing and monitoring the progression of the various conditions in which it actively participates.
Lastly, we discuss the use HSP60 as target for controlling its activity when it is an etiopathogenic
factor, or as a therapeutic agent to correct its deficiency.