Abstract
The most deadly gynecological cancer is ovarian cancer. The endoplasmic reticulum (ER), a vital cell organelle, is involved in the folding, synthesis, and modification of a wide range of soluble and insoluble proteins. ER stress initiates the unfolded protein response (UPR), an evolutionary conserved cell stress mechanism. The UPR is mediated by three ER transmembrane sensors: IRE1, ATF6, and PERK. An inhibitor of ERAD is a small VCP/p97-interacting protein (SVIP). The study aimed to investigate the relationship between SVIP and the ER stress protein markers in the ovarian cancer cell line OVCAR-3. This study used human ovarian cancer cell line OVCAR-3. The SVIP and GRP78, PERK, ATF4 immunoexpression levels were analyzed. Furthermore, employing immunofluorescence, the co-localization of three ER sensors and SVIP was ascertained. The immunoexpression of SVIP and GRP78, ATF4, and PERK were shown in the OVCAR-3 cell line. Additionally, immunofluorescence results showed the co-localization of SVIP and UPR-related proteins in the cytoplasm of OVCAR-3 cells.In conclusion, we demonstrated the cellular localization of SVIP and the proteins involved in the UPR pathway however further studies are needed to determine the relation between SVIP and these proteins in cancer cells.
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