Hsp60, a novel target for antitumor therapy: Structure-function features and prospective drugs design

Anna Maria Almerico, Francesco Cappello, Giovanni Zummo, Andrea Pace, Antonino Lauria, Silvestre Buscemi, Annamaria Martorana, Alessio Terenzi, Claudia Campanella, Francesco Carini, Giampaolo Barone, Claudia Campanella, Andrea Pace, Francesca Angileri, Giampaolo Barone, Everly Conway De Macario, Francesco Cappello, Everly Conway De Macario, Alberto J.L. Macario, Francesca AngileriPaola Pierro

Risultato della ricerca: Articlepeer review

40 Citazioni (Scopus)


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.
Lingua originaleEnglish
pagine (da-a)2757-2764
Numero di pagine8
Stato di pubblicazionePublished - 2013

All Science Journal Classification (ASJC) codes

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