Cell-to-cell transmission of p53 aggregates: a novel player in oncology?

Abstract

The mutants of the tumor suppressor protein p53 form protein aggregates. It has been proposed that these aggregates propagate like prions, albeit the detailed mechanism of the propagation is unclear. Our recent study revealed that sulfated glycosaminoglycans, especially highly sulfated domains of heparan sulfate (heparan sulfate S-domains), participate in cancer pathology by mediating transcellular propagation of p53 aggregates.

Keywords

• p53
• protein aggregates
• prion
• glycosaminoglycan
• heparan sulfate