SHetA2 Attack on Mortalin and Colleagues in Cancer Therapy and Prevention.

ABSTRACT: Heat Shock Proteins of the 70-kDa family (HSP70s) do not cause cancer by themselves, but instead protect cells as they transform into cancer. These molecular chaperones bind numerous client proteins and utilize ATP hydrolysis to facilitate proper protein folding, formation of functional complexes and cellular localizations, or degradation of irreparably damaged proteins. Their transient upregulation by stressful situations avoids induction of programmed cell death. Continued upregulation of the mortalin, heat shock cognate (hsc70) and glucose regulated protein 78 (Grp78) support cancer development and progression by supporting pro-proliferative and metabolic functions and repressing pro-death functions of oncoproteins and tumor suppressor proteins. This review describes the discovery and d

SUBMITTER: Benbrook DM 

PROVIDER: S-EPMC8906462 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature