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Physiology and Pathophysiology of Heat Shock Protein 60

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The eukaryotic heat shock protein 60 (Hsp60), a Group I chaperonin and crucial member of the chaperoning system, is an intramitochondrial chaperone that assists, together with its co-chaperonin Hsp10, the folding of other mitochondrial proteins. This essential function signifies that an absence of Hsp60 is ...

The eukaryotic heat shock protein 60 (Hsp60), a Group I chaperonin and crucial member of the chaperoning system, is an intramitochondrial chaperone that assists, together with its co-chaperonin Hsp10, the folding of other mitochondrial proteins. This essential function signifies that an absence of Hsp60 is incompatible with life.

The Escherichia coli orthologs Hsp60 (GroEL) and Hsp10 (GroES) are the most studied of Group I chaperonins, and information regarding their structure and function has been instrumental in understanding the human counterparts. Biophysical methods have demonstrated that the human Hsp60 in solution occurs as ring-shaped homo-oligomers of seven subunits, in equilibrium with smaller populations of monomers and double-ring tetradecamers. Hsp60 is constitutively expressed under normal conditions, and it can be induced by different kinds of stressors as a mechanism of cellular defence. Hsp60 can be found not only in its canonical location, i.e., inside mitochondria, but also in extra-mitochondrial sites such as cytosol, cell membrane, extracellular milieu, blood, lymph, and microvesicles (e.g., exosomes). Hsp60 displays a variety of roles and interactions depending on its location, intracellular or extracellular, and the tissue or anatomic region considered. This diversity in distribution and function endows Hsp60 with a multifaceted capacity at the centre of the delicate balance between health and disease, for example in chaperonopathies.

Chaperonopathies are diseases recently organized in a coherent nosological group in which the determinant etiologic-pathogenic factor is a molecular chaperone. Genetic and acquired chaperonopathies caused by Hsp60 are relatively common, particularly the latter. Hereditary spastic paraplegia SPG13, and MitCHAP-60 disease are genetic Hsp60 chaperonopathies by defect, while various types of cancer, and chronic and autoimmune disorders associated with abnormal Hsp60 are acquired chaperonopathies by mistake. In chronic inflammation and autoimmunity, Hsp60 can play a pathogenic role as autoantigen, or as inducer of inflammatory cytokines, while in some cancers the chaperonin participates in pathways that favour cancer cell growth, multiplication, and metastasization.

The goal of this Research Topic is to compile current knowledge on Hsp60 in cellular physiology and pathology, with particular focus on the role of Hsp60 in the pathogenic mechanisms of human Hsp60 chaperonopathies. The topic will disseminate knowledge regarding the intricate molecular network around Hsp60 that influences its functions and drives disease. Thus, it aims to shed light on the mechanisms that cause the tissue and organ lesions observed in patients with Hsp60 chaperonopathies. It is likely that detection and quantitative and qualitative determinations of Hsp60 will become standard components of clinical laboratory research and practice. Consequently, studies targeted at developing therapeutic approaches centered on Hsp60 are welcomed. For example, strategies based on chemical chaperones, Hsp-inducers or inhibitors, manufactured chaperones, and the introduction of CRISPR methodology for gene therapy. This Research Topic should facilitate the introduction of Hsp60 into Clinical Medicine with diagnostic and therapeutic applications, for the benefit of a considerable population of patients suffering from acquired or genetic chaperonopathies.

We ask authors to contribute original research papers (including case reports), reviews, or mini reviews.


Keywords: Heat shock protein 60, Human diseases, Cancer, Immune system, Neurodegeneration


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