Comparative analysis of Hsp10 and Hsp90 in large bowel healthy mucosa and adenocarcinomas
- Authors: Rappa F.; Lo Bello M.; Caruso Bavisotto C.; Marino Gammazza A.; Campanella C.; David S.; Sciume C.; Zarcone F.; Geraci G.; Modica G.; Carini F.; Tomasello G.; Bellavia M.; Uzzo M.L.; Spatola G.; Bonaventura G.; Leone A.; Damiani P.; Buccheri F.; Gerbino A.; Farina F.; Cappello F.
- Publication year: 2015
- Type: Articolo in rivista
- OA Link: http://hdl.handle.net/10447/436737
Abstract
Heat shock proteins (Hsps) are an important class of molecules with various functions. Their classic role is to assist other proteins in folding and re-folding and, when proteins are defective or irreversibly misfolded, to drive their degradation. For this reason, some Hsps are also named molecular chaperones. During evolution, this class of proteins has also acquired extrachaperoning roles such as participation in immune system regulation, cell differentiation, programmed cell death and carcinogenesis. Hsp10 is a partner of Hsp60 in the Hsp60/10 folding machine, but numerous scientific studies have shown that Hsp10 may also play other roles. In fact, Hsp10 seems to have an immunomodulatory activity and a role in tumor progression. Hsp90 regulates late-stage maturation, activation and stability of a range of client proteins, such as HER2, EGFR and BRAF, some of which are involved in signal transduction and other key pathways important for malignancy in several cancers, including large bowel carcinomas. The aim of the present study was to evaluate levels and expression of Hsp10 and Hsp90 in a series of samples of large bowel mucosa obtained from healthy controls and patients with adenocarcinomas.