Hsp10: anatomic distribution, functions, and involvement in human disease.

Felicia Farina, Giovanni Tomasello, Giovanni Zummo, Francesco Cappello, Sabrina David, Giuseppe Modica, Fabio Bucchieri, Mario Giuffre, Giampiero La Rocca, Rita Anzalone, Giovanni Peri, Carmelo Sciume', Claudia Campanella, Claudia Campanella, Simona Corrao, Giampiero La Rocca, Giovanni Tomasello, Anna M. Czarnecka, Fabio Bucchieri, Carmelo SciumèEverly Conway De Macario, Giuseppe Modica, Francesco Cappello, Everly Conway De Macario, Alberto J.L. Macario, Simona Corrao

Risultato della ricerca: Articlepeer review

28 Citazioni (Scopus)


There is growing evidence that molecular chaperones/heat shock proteins are involved in the pathogenesis of a number of human diseases, known as chaperonopathies. A better molecular understanding of the pathogenetic mechanisms is essential for addressing new strategies in diagnostics, therapeutics and clinical management of chaperonopathies, including those in which Hsp10 is involved. This chaperonin has been studied for a long time as a member of the mitochondrial protein-folding machine. However, although in normal cells Hsp10 is mainly localized in the mitochondrial matrix, it has also been found during and after stress in other subcellular compartments, such as cytosol, vesicles and secretory granules, alone or in combination with other proteins. In these extramitochondrial locales, Hsp10 plays an active role in cell signalling. For example, cancer cells often show altered levels of Hsp10, compared to normal cells. Hsp10 may also be found in the extracellular space and in the bloodstream, with a possible immunomodulatory activity. This minireview focuses on some studies to date on the involvement of Hsp10 in human disease pathogenesis.
Lingua originaleEnglish
pagine (da-a)768-778
Numero di pagine11
Stato di pubblicazionePublished - 2013

All Science Journal Classification (ASJC) codes

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