Factors Influencing HSP20 Turnover (360G-Wellcome-202415_Z_16_Z)

HSP20, a chaperone protein which has been shown to have extensive cardio-protective properties, is upregulated in a variety of tissues in response to stressful stimuli. Research has demonstrated the anti-apoptotic, anti-ischaemic and anti-hypertrophic effects of HSP20. Little is known about the turnover of HSP20 in cells; recent research has highlighted the possible involvement of the Ubiquitin proteasome system in degradation of HSP20. This project will determine the involvement of this system by firstly, measuring HSP20 half-life by cycloheximide chase, secondly, inhibiting of the suspected proteasome component and studying the ubiquitination of HSP20 and finally, determining binding of the proteasome to HSP20 by immunopurification and peptide array. This project will uncover important details about HSP20 and its turnover and the research gathered will aid progress in development of therapeutic strategies to inhibit the turnover of HSP20 in order to utilise its protective properties.