SelK is a novel ER stress-regulated protein and protects HepG2 cells from ER stress agent-induced apoptosis.
Selenoprotein K (SelK), an endoplasmic reticulum (ER) resident protein, its biological function has been less-well studied. To investigate the role of SelK in the ER stress response, effects of SelK gene silence and ER stress agents on expression of SelK and cell apoptosis in HepG2 cells were studied. The results showed that SelK was regulated by ER stress agents, Tunicamycin (Tm) and beta-Mercaptoethanol (beta-ME), in HepG2 cells. Moreover, the SelK gene silence by RNA interference could significantly aggravate HepG2 cell death and apoptosis induced by the ER stress agents. These results suggest that SelK is an ER stress-regulated protein and plays an important role in protecting HepG2 cells from ER stress agent-induced apoptosis.
Du
Shaoqing
S
Huazhong University of Science and Technology, Wuhan, People's Republic of China.
Zhou
Jun
J
Jia
Yi
Y
Huang
Kaixun
K
D017209:Apoptosis / Q000187:drug effects / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000378:metabolism / Q000494:pharmacology; D056945:Hep G2 Cells; D006801:Humans; D011506:Proteins / Q000378:metabolism / Q000494:pharmacology; D051140:Selenoproteins / Q000378:metabolism* / Q000494:pharmacology; D014415:Tunicamycin / Q000378:metabolism / Q000494:pharmacology
D006360:Heat-Shock Proteins; D011506:Proteins; D051140:Selenoproteins; D014415:Tunicamycin