PROTEÍNAS DE CHOQUE TÉRMICO, MUERTE CELULAR Y RESPUESTA ANTITUMORAL

• Main Authors: S. Fiorentino, A. Barreto, A. Asea
• Format: Article
• Language: English
• Published: Pontificia Universidad Javeriana 2007-12-01
• Series: Universitas Scientiarum
• Subjects: antitumoral therapy; apoptosis; cancer; exosomes; heat shock proteins; immunostimulation
• Online Access: https://docs.google.com/folder/d/0B_IdlsctkRrxS29vWmptMzBJRWM/edit?usp=sharing#docId=0B_IdlsctkRrxTzhjSUY0U2ZxLTg

Heat shock proteins (HSP), particularly inducible HSP72 protein, have an important role generating aneffective antitumoral response as immunogenic peptide carriers or as immunostimulants, when induceactivation and maturation of dendritic cells (DC). These proteins, as molecular chaperones ATP dependant,increase cell survival under any kind of stress. Chaperone function is intrinsic of protein family HSP70structure, having a C-terminal domain that binds unfolded proteins and peptides and a N-terminal ATPasedomain that controls peptide binding pocket opening and closing. Their immunostimulant role mayantagonize with their protective activity against cell death induced by stress or cytotoxic agents. InducibleHSP70 protein is involved in carrying out these two functions, which is the purpose of this review.Furthermore, other members of HSP70 protein family could be implicated, but in different ways: inducingimmune response or promoting tumoral growth inhibiting apoptosis. Comprehension of mechanisms thatregulate both activities is crucial in developing an effective antitumoral therapy through searchingsubstances, which preserving their immunogenic potential, do not increase tumor resistance to classicalantitumoral therapy.