Prognostic Impact of Heat Shock Protein 90 Expression in Women Diagnosed with Cervical Cancer

Int J Mol Sci. 2024 Jan 26;25(3):1571. doi: 10.3390/ijms25031571.

Abstract

Heat Shock Protein 90 (HSP90), a major molecular chaperone, plays a crucial role in cell function by folding and stabilizing proteins and maintaining proteostasis. This study aimed to elucidate the prognostic impact of HSP90 in cervical cancer. We analyzed HSP90 expression using immunohistochemistry in cervical cancer tissue microarrays from 250 patients. This study investigated correlations between HSP90 expression levels and key clinical outcomes, including overall survival (OS), progression-free survival (PFS), and FIGO classification. The statistical analyses employed included the Kruskal-Wallis-H test, log-rank (Mantel-Cox), and Cox regression. Our findings indicate that high nuclear HSP90 expression is associated with improved OS, while high cytoplasmic HSP90 expression correlates with better PFS and a lower FIGO classification in cervical squamous cell carcinoma patients. These results suggest that HSP90 could serve as a positive prognostic factor in patients diagnosed with cervical squamous cell carcinoma, underlining its potential as a biomarker for patient prognosis and as a target for therapeutic strategies.

Keywords: HSP90; cervical cancer; chaperone; human papillomavirus; necroptosis; programmed cell death.

MeSH terms

  • Carcinoma, Squamous Cell* / pathology
  • Female
  • HSP90 Heat-Shock Proteins / metabolism
  • Humans
  • Molecular Chaperones
  • Prognosis
  • Uterine Cervical Neoplasms* / pathology

Substances

  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones

Grants and funding

T.L.R.V. and A.V. have received funds for this study from the structured promotion program of Ludwig-Maximilians University of Munich, “Molecular and clinically translational Medicine” (Reg.-Nr. 27/2017).