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dc.contributor.authorVilasi, S.
dc.contributor.authorBulone, D.
dc.contributor.authorBavisotto, C.C.
dc.date.accessioned2019-06-05T18:28:17Z
dc.date.available2019-06-05T18:28:17Z
dc.date.issued2018
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85041341383&doi=10.3389%2ffmolb.2017.00099&partnerID=40&md5=0bf9b25f3c8a4a184e4d869cb0c0d9de
dc.identifier.urihttp://hdl.handle.net/10713/9436
dc.description.abstractChaperonins play various physiological roles and can also be pathogenic. Elucidation of their structure, e.g., oligomeric status and post-translational modifications (PTM), is necessary to understand their functions and mechanisms of action in health and disease. Group I chaperonins form tetradecamers with two stacked heptameric rings. The tetradecamer is considered the typical functional complex for folding of client polypeptides. However, other forms such as the monomer and oligomers with smaller number of subunits than the classical tetradecamer, also occur in cells. The properties and functions of the monomer and oligomers, and their roles in chaperonin-associated diseases are still incompletely understood. Chaperonin I in eukaryotes occurs in various locations, not just the mitochondrion, which is its canonical place of residence and function. Eukaryotic Chaperonin I, namely Hsp60 (designated HSP60 or HSPD1 in humans) has, indeed, been found in the cytosol; the plasma-cell membrane; on the outer surface of cells; in the intercellular space; in biological liquids such as lymph, blood, and cerebrospinal fluid; and in secretions, for instance saliva and urine. Hsp60 has also been found in cell-derived vesicles such as exosomes. The functions of Hsp60 in all these non-canonical locales are still poorly characterized and one of the questions not yet answered is in what form, i.e., monomer or oligomer, is the chaperonin present in these non-canonical locations. In view of the steady increase in interest on chaperonopathies over the last several years, we have studied human HSP60 to determine its role in various diseases, its locations in cells and tissues and migrations in the body, and its post-translational modifications that might have an impact on its location and function. We also carried out experiments to characterize the oligomeric status of extramitochondrial of HSP60 in solution. Here, we provide an overview of our results, focusing on the oligomeric equilibrium and stability of the various forms of HSP60 in comparison with GroEL. We also discuss post-translational modifications associated with anti-cancer drugs to indicate the potential of Hsp60 in Medicine, as a biomarker and etiopathogenic factor. Copyright 2018 Vilasi, Bulone, Caruso Bavisotto, Campanella, Marino Gammazza, San Biagio, Cappello, Conway de Macario and Macario.en_US
dc.description.urihttps://dx.doi.org/10.3389/fmolb.2017.00099en_US
dc.language.isoen-USen_US
dc.publisherFrontiers Media S.A.en_US
dc.relation.ispartofFrontiers in Molecular Biosciences
dc.subjectChaperonopathiesen_US
dc.subjectGroELen_US
dc.subjectHeptameren_US
dc.subjectHsp60en_US
dc.subjectMonomeren_US
dc.subjectNon-canonical localesen_US
dc.subjectPost-translation modificationen_US
dc.subjectTetradecameren_US
dc.titleChaperonin of Group I: Oligomeric spectrum and biochemical and biological implicationsen_US
dc.typeArticleen_US
dc.identifier.doi10.3389/fmolb.2017.00099


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