| Literature DB >> 33860088 |
Naoyuki Iwahashi1, Midori Ikezaki2, Hiroyuki Saito3, Kenji Uchimura4, Kazuchika Nishitsuji2.
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.Entities:
Keywords: glycosaminoglycan; heparan sulfate; p53; prion; protein aggregates
Year: 2021 PMID: 33860088 PMCID: PMC8018399 DOI: 10.1080/23723556.2021.1892444
Source DB: PubMed Journal: Mol Cell Oncol ISSN: 2372-3556