Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets

Maxim Shevtsov1,2,3,4,5,6, Zsolt Balogi7, William Khachatryan4

  • 1Center for Translational Cancer Research Technische Universität München (TranslaTUM), Radiation Immuno-Oncology Group, Klinikum rechts der Isar, Einstein Str. 25; 81675 Munich, Germany.

Cells
|May 24, 2020
PubMed

Insights

Heat shock proteins (HSPs) are crucial for cell survival under stress. Membrane-associated HSPs in tumor cells offer potential for novel cancer therapies and diagnostics.

Area of Science:

  • Molecular biology
  • Cellular stress response
  • Oncology

Background:

  • Heat shock proteins (HSPs) are vital molecular chaperones maintaining protein homeostasis and cellular defense against stress.
  • HSPs are primarily intracellular but are also found on the plasma membrane of cancer cells.

Purpose of the Study:

  • To review the role of membrane-associated molecular chaperones in normal and tumor cells.
  • To explore the therapeutic and diagnostic potential of these proteins in cancer.

Main Methods:

  • Comprehensive literature review of studies on HSPs in normal and malignant cells.
  • Analysis of HSP localization and function in various cancer types.
  • Evaluation of HSPs as targets for cancer therapy and diagnostics.

Main Results:

  • Members of HSP families (HSP40, HSP60, HSP70, HSP90, small HSPs) are present on the plasma membrane of tumor cells.
  • Membrane-associated HSPs play roles in cancer cell survival, proliferation, and immune evasion.
  • These proteins show promise as biomarkers for cancer detection and as targets for drug development.

Conclusions:

  • Membrane-associated HSPs represent a significant area of research in cancer biology.
  • Targeting these chaperones could lead to innovative cancer treatment strategies.
  • Further investigation is warranted to fully elucidate their clinical utility in diagnostics and therapeutics.

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