AntiTumor Response and Heat Shock Proteins (HSP): A friend or Foe relationship (original) (raw)

Heat shock proteins (HSP), particularly inducible HSP72 have a role in generating an effective antitumoral response as immunogenic peptide carriers or as immunostimulants; inducing activation and maturation of dendritic cells (DC). Their basic function is as molecular chaperones, ATP dependant; increasing cell survival under any type of stress. Chaperone function is natural to protein family HSP70 structure, having a C-terminal domain that binds unfolded proteins and peptides and a N-terminal ATPase domain that controls peptide binding pocket opening and closing. Their immunostimulant role might antagonized with their protective activity against cell death induced by stress or cytotoxic agents. Inducible HSP70 is implicated in carrying out these two functions; purpose of the present review. Furthermore, is possible other members of HSP70 protein family to be implicated, but in different ways; by inducing immune response or as tumoral growth promoters inhibiting apoptosis. Comprehension of mechanisms that regulate both activities, is crucial in developing an effective antitumoral therapy through the search of substances that preserving their immunogenic potential do not increase tumor resistance to classical antitumoral therapy