The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis

The chaperone system (CS) is emerging as a key multistage participant in carcinogenesis. The CS chief components are the molecular chaperones (some of which are named heat shock proteins or Hsp), which are typically cytoprotective but if abnormal in structure, location, or quantity, can become etiop...

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Main Authors: Charbel A. Basset, Inaya Hajj Hussein, Abdo R. Jurjus, Francesco Cappello, Everly Conway de Macario, Alberto J. L. Macario, Angelo Leone
Format: Article
Language:English
Published: MDPI AG 2023-11-01
Series:Applied Biosciences
Subjects:
Online Access:https://www.mdpi.com/2813-0464/2/4/38
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author Charbel A. Basset
Inaya Hajj Hussein
Abdo R. Jurjus
Francesco Cappello
Everly Conway de Macario
Alberto J. L. Macario
Angelo Leone
author_facet Charbel A. Basset
Inaya Hajj Hussein
Abdo R. Jurjus
Francesco Cappello
Everly Conway de Macario
Alberto J. L. Macario
Angelo Leone
author_sort Charbel A. Basset
collection DOAJ
description The chaperone system (CS) is emerging as a key multistage participant in carcinogenesis. The CS chief components are the molecular chaperones (some of which are named heat shock proteins or Hsp), which are typically cytoprotective but if abnormal in structure, location, or quantity, can become etiopathogenic and cause diseases, known as chaperonopathies, including some cancers. For example, abnormal Hsp90 expression is associated with tumorigenesis and poor prognosis. Hsp90 is positioned at the center of several key oncogenic pathways by stabilizing and activating oncogenic kinases responsible for driving cell proliferation and survival. Consequently, inhibition of Hsp90 is being investigated as a possible anti-cancer strategy and some results are encouraging. However, the 5-year survival rate for patients suffering from salivary gland carcinomas is still unsatisfactory. Because of the rarity of these malignancies, they may have been overlooked and understudied and, thus, novel therapies (e.g., inhibition of CS components like Hsp90 and others) are urgently needed. In this review, we also summarize the histopathological quantitative patterns and the intra- and extra-cellular location characteristics of Hsp90 in tumors of salivary glands, pointing to their potential for differential diagnosis, prognostication, and patient monitoring.
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spelling doaj.art-90adff64b78b468a8aa2dff30115eb3a2023-12-22T13:48:42ZengMDPI AGApplied Biosciences2813-04642023-11-012460761610.3390/applbiosci2040038The Chaperone Hsp90, a Key Player in Salivary Gland TumorigenesisCharbel A. Basset0Inaya Hajj Hussein1Abdo R. Jurjus2Francesco Cappello3Everly Conway de Macario4Alberto J. L. Macario5Angelo Leone6Department of Biomedicine, Neuroscience and Advanced Diagnostics, Institute of Human Anatomy and Histology, University of Palermo, 90127 Palermo, ItalyDepartment of Foundational Medical Studies, Oakland University William Beaumont School of Medicine, Rochester, MI 48309, USADepartment of Anatomy, Cell Biology and Physiological Sciences, Faculty of Medicine, American University of Beirut (AUB), Beirut 1107 2020, LebanonDepartment of Biomedicine, Neuroscience and Advanced Diagnostics, Institute of Human Anatomy and Histology, University of Palermo, 90127 Palermo, ItalyEuro-Mediterranean Institute of Science and Technology (IEMEST), 90139 Palermo, ItalyEuro-Mediterranean Institute of Science and Technology (IEMEST), 90139 Palermo, ItalyDepartment of Biomedicine, Neuroscience and Advanced Diagnostics, Institute of Human Anatomy and Histology, University of Palermo, 90127 Palermo, ItalyThe chaperone system (CS) is emerging as a key multistage participant in carcinogenesis. The CS chief components are the molecular chaperones (some of which are named heat shock proteins or Hsp), which are typically cytoprotective but if abnormal in structure, location, or quantity, can become etiopathogenic and cause diseases, known as chaperonopathies, including some cancers. For example, abnormal Hsp90 expression is associated with tumorigenesis and poor prognosis. Hsp90 is positioned at the center of several key oncogenic pathways by stabilizing and activating oncogenic kinases responsible for driving cell proliferation and survival. Consequently, inhibition of Hsp90 is being investigated as a possible anti-cancer strategy and some results are encouraging. However, the 5-year survival rate for patients suffering from salivary gland carcinomas is still unsatisfactory. Because of the rarity of these malignancies, they may have been overlooked and understudied and, thus, novel therapies (e.g., inhibition of CS components like Hsp90 and others) are urgently needed. In this review, we also summarize the histopathological quantitative patterns and the intra- and extra-cellular location characteristics of Hsp90 in tumors of salivary glands, pointing to their potential for differential diagnosis, prognostication, and patient monitoring.https://www.mdpi.com/2813-0464/2/4/38molecular chaperonesHsp90chaperone systemsalivary gland tumorscarcinomadiagnosis
spellingShingle Charbel A. Basset
Inaya Hajj Hussein
Abdo R. Jurjus
Francesco Cappello
Everly Conway de Macario
Alberto J. L. Macario
Angelo Leone
The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis
Applied Biosciences
molecular chaperones
Hsp90
chaperone system
salivary gland tumors
carcinoma
diagnosis
title The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis
title_full The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis
title_fullStr The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis
title_full_unstemmed The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis
title_short The Chaperone Hsp90, a Key Player in Salivary Gland Tumorigenesis
title_sort chaperone hsp90 a key player in salivary gland tumorigenesis
topic molecular chaperones
Hsp90
chaperone system
salivary gland tumors
carcinoma
diagnosis
url https://www.mdpi.com/2813-0464/2/4/38
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