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Heat Shock Protein 90 in Human Diseases and Disorders pp 387–410Cite as

Hsp90: A Target for Susceptibilities and Substitutions in Biotechnological and Medicinal Application

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Part of the book series: Heat Shock Proteins ((HESP,volume 19))

Abstract

A main influencer of the chaperome is the environmental stress eliciting continuously degraded proteins. To avoid proteotoxic stress, which hinders the protein homeostasis and cell survival, most proteins are accompanied from the early existence on by heat shock proteins (HSP) and sequestrated into different routes of renaturation, de novo folding or denaturation. Therefore, the regulation of Hsp90 presence and activity is relevant for most cells and their function. In this position, Hsp90 can decide the fate between health and disease by selective refolding of denatured proteins and is a player in the evolution. From the last century on, Hsp90 was validated as a target due to its susceptibility for natural products and to make them perfect with the aim to hinder refolding and enhance the proteotoxic stress. In this review, the links between natural producer, chemical synthesis with Hsp90 as a target as well as alternative chaperoning routes by chemical compounds are illuminated.

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Abbreviations

CFTR:

Cystic fibrosis transmembrane conductance regulator

HSP:

Heat shock proteins

NBD:

Nucleotide binding domain

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Authors and Affiliations

  1. Clinic for Otorhinolaryngology – Head and Neck Surgery, Hannover Medical School (MHH), Hannover, Germany

    Athanasia Warnecke

  2. Leibniz University Hannover, Institute of Organic Chemistry and Biomolecular Drug Research Center (BMWZ), Hannover, Germany

    Andreas Kirschning

  3. Leibniz University Hannover, Center of Biomolecular Drug Research Center (BMWZ), Hannover, Germany

    Daniel Landsberg & Carsten Zeilinger

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  1. Athanasia Warnecke
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  2. Andreas Kirschning
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  3. Daniel Landsberg
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  4. Carsten Zeilinger
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Correspondence to Carsten Zeilinger .

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Editors and Affiliations

  1. Department of Medicine and Director, Precision Therapeutics Proteogenomics Diagnostic Center, Eleanor N. Dana Cancer Center, University of Toledo, College of Medicine and Life Sciences, Toledo, OH, USA

    Alexzander A. A. Asea

  2. Department of Experimental Radiation Oncology, MD Anderson Cancer Center, Houston, TX, USA

    Punit Kaur

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Warnecke, A., Kirschning, A., Landsberg, D., Zeilinger, C. (2019). Hsp90: A Target for Susceptibilities and Substitutions in Biotechnological and Medicinal Application. In: Asea, A., Kaur, P. (eds) Heat Shock Protein 90 in Human Diseases and Disorders. Heat Shock Proteins, vol 19. Springer, Cham. https://doi.org/10.1007/978-3-030-23158-3_18

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