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The role of HSP90 molecular chaperones in hepatocellular carcinoma

Masoud Nouri-Vaskeh1,2, Leila Alizadeh3, Khalil Hajiasgharzadeh1

  • 1Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.

Journal of Cellular Physiology
|May 27, 2020
PubMed

Insights

Heat shock protein 90 (HSP90) aids cancer cell survival and proliferation. Targeting HSP90 may offer new diagnostic and therapeutic strategies for hepatocellular carcinoma (HCC).

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • Misfolded proteins can form toxic aggregates, promoting disease.
  • Heat shock protein 90 (HSP90) is a crucial molecular chaperone regulating protein folding and cellular functions.
  • HSP90 plays a role in cell proliferation, motility, angiogenesis, signal transduction, and stress adaptation.

Purpose of the Study:

  • To review the multifaceted functions of HSP90 in cellular processes.
  • To assess the potential of HSP90 as a diagnostic biomarker for hepatocellular carcinoma (HCC).
  • To explore HSP90 as a therapeutic target for HCC.

Main Methods:

  • Comprehensive literature review of HSP90 functions.
  • Analysis of HSP90's role in cancer signaling pathways.
  • Evaluation of clinical data linking HSP90 expression to HCC progression and survival.

Main Results:

  • HSP90 facilitates malignant transformation by stabilizing mutated oncoproteins.
  • Upregulated HSP90 expression in HCC correlates with advanced disease stages.
  • HSP90 is implicated in tumorigenicity, therapy resistance, and apoptosis inhibition.

Conclusions:

  • HSP90 is a key regulator in pathways driving HCC.
  • HSP90 expression levels may serve as a prognostic indicator for HCC patients.
  • Targeting HSP90 presents a promising therapeutic avenue for hepatocellular carcinoma.
Keywords:
chaperone proteinsheat shock protein 90hepatocellular carcinomaliver cancer

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