Biomarker Of Cancers

A molecular chaperone, heat shock protein 27 (HSP27, heat-shock 27-KD protein 1, HSPB1) is one of the small heat shock protein family. It modulates the ability of cells to respond to several types of injury, heat shock, oxidative stress and other stresses. HSP27 is expressed in almost all organisms from prokaryotes to mammals. It interacts with many proteins and can prevent a wide variety of apoptotic agents from causing cell death. HSP27 regulates apoptosis by interacting with key components of the apoptotic signaling pathway. It was reported that HSP27 inhibited cytochrome c and dATP triggered activation of procaspase-9 and prevented etoposide-induced apoptosis, and HSP27 altered the expression of topoisomerase II and inhibited doxorubicin-induced apoptosis. Furthermore, it was reported that over-expression of HSP27 in prostate cancer cells rendered cells resistant to etoposide-, diethylmaleate-, cycloheximide- or radiation induced apoptosis, which may be mediated by the production of survival factors. From recent studies, up-regulation of HSP27 in pancreatic cancer cells has been clarified to be linked to the resistance to gemcitabine (GEM), and the down-regulation of HSP27 by using HSP27 inhibitors; siRNA for HSP27, interferon γ or KNK437 in GEMresistant cells showed the increasing sensitivity for GEM

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Last date updated on September, 2024