G.M. Nagaraja, P. Kaur and A. Asea Pages 1142 - 1150 ( 9 )
Heat shock proteins (HSP) are a group of physiologically-essential, highly-conserved proteins that are induced by heat shock, as well as by other environmental and pathophysiological stressors. The twentyseven kDa heat shock protein (Hsp27; HspB1) is highly expressed in tumor tissues of patients diagnosed with cancer and expression levels correlate with poor prognosis. HspB1 plays a dual role in cancer and promotes both cancer development by suppressing host anti-cancer response, such as apoptosis and senescence, and facilitates the enhanced expression of metastastic genes. HspB1-mediated protection from tumor cell apoptosis induced by chemotherapeutic drugs occurs through several mechanisms, including decreased production of reactive oxygen species, restoration of protein homeostasis and promotion of cell survival by protein folding, stabilization of actin-cytoskeleton, delayed release of cytochrome c from mitochondria and inhibition of activation of caspase-3. High levels of HSP expression affect tumor susceptibility to adjuvant cancer treatments, including chemotherapy, hyperthermia, and radiation. This review highlights the most recent findings and role of HspB1 in metastasis.
Cancer, CD8+ CTL, heat shock proteins, lentivirus, metastasis, siRNA, tumor, connective tissue, intravasation, lymphatic system, extravasation, ocular melanoma, polymerization, acto-myosin contraction, phenotype
Division of Investigative Pathology, Scott & White Healthcare and the Texas A&M Health Science Center, College of Medicine, Temple, TX 76504, USA.