Biological Activity
He at shock protein 27 (HSP27) accumulates in cells exposed to a short period of hyperthermia and contributes to the development of a transient state of thermotolerance. HSP27 can inhibit actin polymerization, thus modulating actin dynamics during stress. It is known to guard against apoptotic cell death activated by several stimuli, such as Fas ligand hyperthermia, oxidative stress and cytotoxic drugs. It can hinder the mitochondrial pathway of caspase-induced cell death by acting as a negative regulator of cytochrome c-dependent activation of caspase-3. The synthesis of HSP27 is stimulated by various cytokines, growth factors, hormones and chemicals. HSP27 shows a rapid phosphorylation, following exposure to stress stimuli. HSP27 is expressed in the cytoplasm and colocalizes to the nucleus upon stress stimuli. Mutation on this HSP27 gene is associated with Charcot-Marie-Tooth disease.
