Potential use of heat shock protein 90 as a biomarker for the diagnosis of human diseases

ABSTRACT

Introduction

The heat shock protein 90 (Hsp90) is a protein involved in many different biological processes and especially in cell survival. Some of these functions require the participation of other biological molecules, so Hsp90 is a chaperone that takes part in many protein–protein interactions working as a critical signaling hub protein. As a member of the heat shock protein family, Hsp90 expression is regulated under certain environmental and/or stressful situations, therefore Hsp90 concentration can be monitored and linked to these effects.

Areas covered

This review discusses the Hsp90 expression in samples from individuals affected by different diseases (from infectious to cancer origin), and the biological consequences of these disorders, including the potential use of Hsp90 as a biomarker for the diagnosis of human diseases.

Expert opinion

The potential of Hsp90 as a biomarker disease has been demonstrated in several studies in relation to infectious diseases and especially cancer. However, further research in this field is still needed, mainly to validate in statistically significant clinical studies that the detection of Hsp90 protein allows the diagnosis of some cancers at an early stage and also that it can act as a biomarker for monitoring the efficacy of their therapies.

KEYWORDS:

• Heat shock protein
• cancer
• infectious diseases
• biomarker
• diagnosis

Article highlights

• The monitoring of Hsp90 levels provides promising results as biomarker for infectious diseases at early stages.

• Hsp90 levels have been associated with diabetes type 1 or biliary atresia.

• Hsp90 levels have been studied as biomarker for the diagnosis of some cancer types with very promising results.

• Hsp90 has been studied for therapy effectiveness in different cancer types.

Declaration of interest

M.V.R., J.B.G., A.L.C., and F.G.dC acknowledge support by the Basque Government (Elkartek KK-2017/00008). A.L.C. acknowledges support by the European Research Council ERC-CoG-648071-ProNANO and ERC-PoC-841063-NIMM; Agencia Estatal de Investigación, Spain (PID2019–111649RB-I00); Basque Government (RIS3–2019222005). This work was performed under the Maria de Maeztu Units of Excellence Program from the Spanish State Research Agency – Grant No. MDM-2017–0720 (CIC biomaGUNE). The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.

Reviewers Disclosure

Peer reviewers on this manuscript have no relevant financial relationships or otherwise to disclose.

Additional information

Funding

This research was funded by the Basque Government (Elkartek KK-2017/00008).