Molecular chaperones and cancer immunotherapy.
As one of the most abundant and evolutionally conserved intracellular proteins, heat shock proteins, also known as stress proteins or molecular chaperones, perform critical functions in maintaining cell homeostasis under physiological as well as stress conditions. Certain chaperones in extracellular milieu are also capable of modulating innate and adaptive immunity due to their ability to chaperone polypeptides and to interact with the host's immune system, particularly professional antigen-presenting cells. The immunomodulating properties of chaperones have been exploited for cancer immunotherapy. Clinical trials using chaperone-based vaccines to treat various malignancies are ongoing.
Wang
X Y
XY
Department of Cellular Stress Biology and Urologic Oncology, Roswell Park Cancer Institute, Buffalo, NY 14263, USA. xiang-yang.wang@roswellpark.org
Facciponte
J G
JG
Subjeck
J R
JR
D000818:Animals; D000951:Antigens, Neoplasm / Q000276:immunology / Q000502:physiology; D019496:Cancer Vaccines / Q000276:immunology*; D003713:Dendritic Cells / Q000276:immunology; D006360:Heat-Shock Proteins / Q000276:immunology* / Q000502:physiology; D006801:Humans; D007167:Immunotherapy; D018832:Molecular Chaperones / Q000276:immunology* / Q000502:physiology; D009369:Neoplasms / Q000628:therapy*; D011993:Recombinant Fusion Proteins / Q000276:immunology; D014614:Vaccines, Synthetic / Q000276:immunology
D000951:Antigens, Neoplasm; D019496:Cancer Vaccines; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011993:Recombinant Fusion Proteins; D014614:Vaccines, Synthetic