Andrea Pace, Giampaolo Barone, Antonino Lauria, Annamaria Martorana, Antonio Palumbo Piccionello, Paola Pierro, Alessio Terenzi, Anna Maria Almerico, Silvestre Buscemi, Claudia Campanella, Francesca Angileri, Francesco Carini, Giovanni Zummo, Everly Conway de Macario, Francesco Cappello and Alberto J.L. Macario Pages 2757 - 2764 ( 8 )
Heat shock protein 60kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential. Despite the plethora of studies devoted to the mechanism of Hsp60’s function, especially in prokaryotes, fundamental issues still remain unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article we discuss these differences in sequence, structure, and roles of Hsp60, focusing on the human ortholog with the view of devising compounds to block its ability to favour tumor-cell growth and survival. Compounds currently known to directly or indirectly affect Hsp60 functions, such as protein folding, HIF-1α accumulation, or Hsp60-induced cell proliferation, are discussed along with strategies that might prove effective for developing Hsp60-targeting drugs for anticancer therapy.
Hsp60, chaperonin, functional domains, binding pocket, compound docking, epolactaene, drug design, cancer treatment
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