Abstract
Benign prostatic hyperplasia (BPH) is one of the most common causes of lower urinary tract symptoms (LUTS) in men, which is characterized by a noncancerous enlargement of the prostate. BPH troubles the vast majority of aging men worldwide; however, the pathogenetic factors of BPH have not been completely identified. The heat shock protein 70 (HSP70) subfamily, which mainly includes HSP70, glucose-regulated protein 78 (GRP78) and GRP75, plays a crucial role in maintaining cellular homeostasis. HSP70s are overexpressed in the course of BPH and involved in a variety of biological processes, such as cell survival and proliferation, cell apoptosis, epithelial/mesenchymal transition (EMT) and fibrosis, contributing to the development and progress of prostate diseases. These chaperone proteins also participate in oxidative stress, a cellular stress response that takes place under stress conditions. In addition, HSP70s can bind to the androgen receptor (AR) and act as a regulator of AR activity. This interaction of HSP70s with AR provides insight into the importance of the HSP70 chaperone family in BPH pathogenesis. In this review, we discuss the function of the HSP70 family in prostate glands and the role of HSP70s in the course of BPH. We also review the potential applications of HSP70s as biomarkers of prostate diseases for targeted therapies.