Hsp90 inhibition promotes proteasome function in vascular endothelial cells
Konferenz: BIBE 2018 - International Conference on Biological Information and Biomedical Engineering
06.06.2018 - 08.06.2018 in Shanghai, China
Tagungsband: BIBE 2018
Seiten: 3Sprache: EnglischTyp: PDFPersönliche VDE-Mitglieder erhalten auf diesen Artikel 10% Rabatt
Peng, Min; Zhang, Fengxue (Sichuan Academy of Medical Sciences & Sichuan Provincial People’s Hospital, School of Medicine, University of Electronic Science and Technology of China, Chengdu, Sichuan, China)
Dysfunction of proteasome has been implicated in the development of many human diseases. Promoting proteasome function may have profound clinical interests. We have shown in our previous study that proteasome is inhibited by O-GlcNAc modification, which has been shown in another study to be decreased by Hsp90 inhibition as a result of the degradation of O-GlcNAc transferase (OGT). In this study we examined the effect of Hsp90 inhibition on proteasome function in vascular endothelial cells. We found that inhibition of Hsp90 promoted proteasome function, as indicated by proteasome chymotrypsin-like peptidase activity and the clearance of ubiquitinated proteins. Thus, Hsp90 inhibitors may be used to promote proteasome function pharmacologically.