Hsp70: a chaperokine.
Chaperokine is a term recently coined to better describe the dual role of extracellular heat shock protein as both chaperone and cytokine. The augmentation of intracellular Hsp72 expression has clearly been demonstrated to be cytoprotective; with the ability to activate anti-apoptotic and anti-inflammatory pathways, exerting inhibitory effects on cell cycle progression and suppressing genes important in proliferation and differentiation. On the other hand, the role of extracellular Hsp72 is only now being elucidated and has been demonstrated to play a cytostimulatory role by enhancing proinflammatory cytokine and chemokine synthesis, up-regulate co-stimulatory molecule expression, enhance the maturation of dendritic cells and promote antitumour surveillance. This paper covers the most recent advances in elucidation of the mechanism by which the chaperokine activity of Hsp72 is transduced, addresses its biological significance and, finally, covers how it is being harnessed to produce novel therapeutic agents.
Asea
Alexzander
A
Division of Investigative Pathology, Scott & White Clinic and Texas A & M University System Health Science Center, College of Medicine, 1901 South 1st Street, Temple, TX 76508, USA.
D000818:Animals; D016207:Cytokines / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D050884:HSP72 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D051379:Mice
D016207:Cytokines; D018840:HSP70 Heat-Shock Proteins; D050884:HSP72 Heat-Shock Proteins