Mechanism of formation and stability of macromolecular complexes of Hsp70 and Hsp90 in endothelial cells

• Grant number: 19/25503-1
• Support Opportunities: Scholarships in Brazil - Scientific Initiation
• Effective date (Start): January 01, 2020
• Effective date (End): December 31, 2020
• Field of knowledge: Biological Sciences - Biophysics - Cellular Biophysics
• Principal Investigator: Thaís Larissa Araujo de Oliveira Silva
• Grantee: Everton Gonzaga de Melo
• Host Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil
• Associated research grant: 18/13739-8 - Molecular chaperone HSP70 mediates proteostasis in endothelial cells response to hemodynamic force, AP.JP

Abstract

Proteostasis or homeostasis of proteins including synthesis, folding and protein degradation. The chaperone is defined by several chaperones, co-chaperones and enzymes of protein folding and scaffold proteins that regulate one of proteostasis arm. The network hyperconnectivity chaperone know as epichaperome, which hubs are HSP70 and HSP90 is found in a half of teste cancer cells and its disruption with HSP90 inhibitor PU-H71, nowadays in a clinical trial. Further, the presence of HSP90 isoelectric point, pI >5 was proposed as personalized therapy. The macromolecular complexes are also found in bacteria, virus, yeast and plant are modulated by stress. Our hypothesis is that HSP70 and HSP90 macromolecular complexes are also found in endothelial cells after exposure to chronic shear stress and hypoxia. (AU)