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Membrane‐associated heat shock proteins in oncology: From basic research to new theranostic targets

  • Maxim Shevtsov
  • , Zsolt Balogi
  • , William Khachatryan
  • , Huile Gao
  • , László Vígh
  • , Gabriele Multhoff
  • Technical University of Munich
  • Institute of Cytology of the Russian Academy of Sciences
  • St. Petersburg State Medical Pavlov University
  • Almazov National Medical Research Centre
  • National Center for Neurosurgery
  • Far Eastern Federal University
  • University of Pecs Medical School
  • Sichuan University
  • Biological Research Centre

Research output: Contribution to journalReview articlepeer-review

78 Scopus citations

Abstract

Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane‐associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics.

Original languageEnglish
Article number1263
JournalCells
Volume9
Issue number5
DOIs
StatePublished - May 2020

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • Calreticulin
  • GRP78
  • GRP96
  • HSP27
  • HSP40
  • HSP60
  • HSP70
  • HSP90
  • Heat shock proteins
  • Targeted diagnostics and therapy

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