[Frontiers in Bioscience E5, 768-778, January 1, 2013]

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

Sabrina David,1 Fabio Bucchieri,1,2 Simona Corrao,1,2 Anna M. Czarnecka,3 Claudia Campanella,1,2 Felicia Farina,1 Giovanni Peri,1 Giovanni Tomasello,4 Carmelo Sciumè,4 Giuseppe Modica,4 Giampiero La Rocca,1,2 Rita Anzalone,1 Mario Giuffrè,5 Everly Conway De Macario,6 Alberto J.L. Macario,2,6 Francesco Cappello,1,2 Giovanni Zummo1

1Department of Experimental Biomedicine and Clinical Neuroscience, Section of Human Anatomy, University of Palermo, Italy, 2Istituto Euro-Mediterraneo di Scienza e Tecnologia (IEMEST), Palermo, Italy,3Laboratory of Molecular Oncology, Department of Oncology, Military Institute of Medicine, Warsaw, Poland, 4Department of Surgical and Oncological Sciences, University of Palermo, Palermo, Italy, 5Department of Neonatology and Neonatal Intensive Care, University of Palermo , Italy, 6Department of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore, and IMET, Baltimore, MD, USA.


1. Abstract
2. Molecular chaperones, heat shock proteins and chaperonopathies
3. Hsp10 molecular anatomy and functions
4. Hsp10 and cancer
5. Hsp10 and autoimmune diseases
6. Hsp10 and chronic inflammatory diseases
7. Hsp10 and aging
8. Conclusion
9. Acknowledgements
10. References


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.