Your browser doesn't support javascript.
loading
The deubiquitinase USP10 protects pancreatic cancer cells from endoplasmic reticulum stress.
Bhattacharya, Udayan; Thavathiru, Elangovan; Neizer-Ashun, Fiifi; Xu, Chao; Gatalica, Zoran; Dwivedi, Shailendra Kumar Dhar; Dey, Anindya; Mukherjee, Priyabrata; Bhattacharya, Resham.
Affiliation
  • Bhattacharya U; Department of Obstetrics and Gynecology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Thavathiru E; Department of Obstetrics and Gynecology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Neizer-Ashun F; Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Xu C; Department of Biostatistics and Epidemiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Gatalica Z; Department of Pathology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Dwivedi SKD; Department of Obstetrics and Gynecology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Dey A; Department of Obstetrics and Gynecology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Mukherjee P; Department of Pathology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
  • Bhattacharya R; Peggy and Charles Stephenson Cancer Center, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
NPJ Precis Oncol ; 6(1): 93, 2022 Dec 21.
Article in En | MEDLINE | ID: mdl-36543867
The ubiquitin-specific peptidase 10 (USP10) plays a context-specific, pro or anti-tumorigenic role in different malignancies. However, the role of USP10 in pancreatic cancer remains unclear. Our protein and RNA level analysis from archived specimens and public databases show that USP10 is overexpressed in pancreatic ductal adenocarcinoma (PDAC) and expression correlates with poor overall patient survival. Phenotypically, silencing USP10 decreased viability, clonal growth and invasive properties of pancreatic cancer cells. Mechanistically, silencing USP10 upregulated BiP and induced endoplasmic reticulum (ER) stress that led to an unfolded protein response (UPR) and upregulation of PERK, IRE1α. Decreased cell viability of USP10 silenced cells could be rescued by a chemical chaperone that promotes protein folding. Our studies suggest that USP10 by protecting pancreatic cancer cells from ER stress may support tumor progression.

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: NPJ Precis Oncol Year: 2022 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: NPJ Precis Oncol Year: 2022 Document type: Article Affiliation country: Country of publication: