Prognostic Impact of Heat Shock Protein 90 Expression in Women Diagnosed with Cervical Cancer
Open Access
- 26 January 2024
- journal article
- research article
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 25 (3) , 1571
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
Funding Information
- Ludwig-Maximilians University of Munich, “Molecular and clinically translational Medicine” (27/2017)
This publication has 40 references indexed in Scilit:
- Hsp90, an unlikely ally in the war on cancerThe FEBS Journal, 2013
- Amplification and high-level expression of heat shock protein 90 marks aggressive phenotypes of human epidermal growth factor receptor 2 negative breast cancerBreast Cancer Research, 2012
- Molecular chaperones in protein folding and proteostasisNature, 2011
- Functional Inactivation of Endogenous MDM2 and CHIP by HSP90 Causes Aberrant Stabilization of Mutant p53 in Human Cancer CellsMolecular Cancer Research, 2011
- Human papillomavirus oncoproteins: pathways to transformationNature Reviews Cancer, 2010
- Converging concepts of protein folding in vitro and in vivoNature Structural & Molecular Biology, 2009
- Cytoplasmic functions of the tumour suppressor p53Nature, 2009
- Drugging the Cancer Chaperone HSP90Annals of the New York Academy of Sciences, 2007
- Hsp90 Chaperones Wild-type p53 Tumor Suppressor ProteinJournal of Biological Chemistry, 2004
- Disruption of Hsp90 Function Results in Degradation of the Death Domain Kinase, Receptor-interacting Protein (RIP), and Blockage of Tumor Necrosis Factor-induced Nuclear Factor-κB ActivationJournal of Biological Chemistry, 2000