Editing GroEL (section)

== Immunological role ==
As discussed above, HSP60 has generally been known as a chaperonin which assists in protein folding in mitochondria.  However, some new research has indicated that HSP60 possibly plays a role in a “danger signal cascade” [[immune response]].<ref name=fourteen>{{cite journal  |vauthors=Hansen JJ, Bross P, Westergaard M, etal |title=Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter |journal=Hum. Genet. |volume=112 |issue=1 |pages=71–7 |date=January 2003 |pmid=12483302 |doi=10.1007/s00439-002-0837-9|s2cid=25856774 }}</ref>  There is also mounting evidence that it plays a role in [[autoimmune]] disease.

[[Infection]] and [[disease]] are extremely stressful on the cell.  When a cell is under stress, it naturally increases the production of stress proteins, including [[heat shock proteins]] such as HSP60.  In order for HSP60 to act as a signal it must be present in the [[extracellular]] environment.  In recent research “it has emerged that…chaperonin 60 can be found on the surface of various [[prokaryotic]] and [[eukaryotic]] cells, and can even be released from cells”.<ref name=six/> According to recent research, many different types of [[heat shock proteins]] are used in [[immune]] response signaling, but it appears that different proteins act and respond differently to other signaling molecules.  HSP60 has been shown to be released from specific cells like [[peripheral blood mononuclear cell]]s (PBMCs) when there are [[lipopolysaccharides]] (LPS) or GroEL present.  This suggests that the cell has different [[Receptor (biochemistry)|receptors]] and responses to human and bacterial HSP60.<ref name=fourteen/>  In addition, it has been shown that HSP60 has the capability “of activating [[monocytes]], [[macrophages]] and [[Dendrite (non-neuronal)|dendritic]] cells…and also of inducing secretion of a wide range of [[cytokines]].” <ref name=fourteen/>  The fact that HSP60 responds to other signal molecules like LPS or GroEL and has the ability to activate certain types of cells supports the idea that HSP60 is part of a danger signal cascade which is involved in activating an immune response.

There is however, a twist in the immunological role of HSP60.  As mentioned above, there are two different types of HSP60 proteins, bacterial as well as mammalian.  Since they are very similar in sequence, bacterial HSP60 wouldn’t be expected to cause a large immune response in humans.  The immune system is “designed to ignore ‘self’, that is, host constituents; however, paradoxically, this is not the case with chaperonins”.<ref name=six/> It has been found that many anti-chaperonin antibodies exist and are associated with many autoimmune diseases.  According to Ranford, et al. experiments have been performed which have shown that [[antibodies]] which are “generated by a human host after exposure to bacterial chaperonin 60 proteins” can cross-react with human chaperonin 60 proteins.<ref name=six/>  Bacterial HSP60 is causing the immune system to create anti-chaperonin antibodies, even though bacterial and human HSP60 have similar protein sequences.  These new antibodies are then recognizing and attacking human HSP60 which causes an autoimmune disease.  This suggests that HSP60 may play a role in [[autoimmunity]], however more research needs to be done in order to discover more completely its role in this disease.