Peroxiredoxin-1 as a molecular chaperone that regulates glutathione S-transferase P1 activity and drives mutidrug resistance in ovarian cancer cells

  • Biochem Biophys Rep. 2024 Jan 14:37:101639. doi: 10.1016/j.bbrep.2024.101639.
Chengling Fan  1 ,  Shubin Yuan  2 ,  Yuemei Zhang  1 ,  Yinmei Nie  1 ,  Li Xiang  1 ,  Tianchao Luo  1 ,  Qi Xi  2 ,  Yaqin Zhang  2 ,  Zixiang Gu  2 ,  Peng Wang  2 ,  Hongxia Zhou  1
Affiliations
  • 1. Baoying Maternity and Child Health Care Hospital, 118 Anyi East Road, Baoying County, Yangzhou, China.
  • 2. Jiangsu Yinfeng Science and Technology Association, No. 7, Yongfeng Avenue, Qinhuai District, Nanjing, China.
PMID: 38288281 DOI: 10.1016/j.bbrep.2024.101639
Abstract

Ovarian Cancer is among the most prevalent gynecological malignancies around the globe. Nonetheless, chemoresistance continues to be one of the greatest obstacles in the treatment of ovarian Cancer. Therefore, understanding the mechanisms of chemoresistance and identifying new treatment options for ovarian Cancer patients is urgently required. In this study, we found that the mRNA and protein expression levels of PRDX1 were significantly increased in cisplatin resistant A2780/CDDP cells. Cell survival assays revealed that PRDX1 depletion substantially increased ovarian Cancer cell sensitivity to cisplatin, docetaxel, and doxorubicin. Additionally, PRDX1 significantly increased GSTP1 activity, resulting in multidrug resistance. Biochemical experiments showed that PRDX1 interacted with GSTP1 through Cysteine 83, which regulated GSTP1 activity as well as chemotherapy resistance in ovarian Cancer cells. Our findings indicate that the molecular chaperone activity of PRDX1 is a promising new therapeutic target for ovarian Cancer.

Keywords
GSTP1; Molecular chaperone; Mutidrug resistance; Ovarian cancer; PRDX1.
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