HSP70

Heat shock protein 70 (HSP70) is a highly conserved protein produced by the body after being stimulated by factors such as high temperature, infection, and damage. It can serve as a chaperone to assist in refolding and accelerating degradation of proteins, and initiate immune response by binding to antigenic peptides and activating immune cells. However, HSP70 is highly expressed in lung cancer, liver cancer, gastric cancer, colorectal cancer, prostate cancer, breast cancer, ovarian cancer and other tumors, which is closely related to the malignant development of tumors and the poor prognosis of patients. Some research found that HSP70 is an important negative regulator of cell apoptosis, which can inhibit Caspase-3 activation to hinder the intrinsic pathway, and interfere with the interaction between AIF and death receptors to hinder the extrinsic pathway. Meanwhile, HSP70 in pancreatic cancer can stimulate proliferation through the P13K/AKT pathway, promote epithelial-mesenchymal transition (EMT) through the NF-κB pathway, and reduce treatment reactivity through metabolic reprogramming and oxidative stress antagonism.