A Chemical Biology Approach to the Chaperome in Cancer-HSP90 and Beyond.
Animals
Antineoplastic Agents
/ pharmacology
Biology
Decision Making
Drug Design
Gene Expression Regulation, Neoplastic
HEK293 Cells
HSP70 Heat-Shock Proteins
/ metabolism
HSP90 Heat-Shock Proteins
/ metabolism
Humans
K562 Cells
Kinetics
Mice
Molecular Chaperones
/ metabolism
NIH 3T3 Cells
Neoplasms
/ drug therapy
Protein Binding
Journal
Cold Spring Harbor perspectives in biology
ISSN: 1943-0264
Titre abrégé: Cold Spring Harb Perspect Biol
Pays: United States
ID NLM: 101513680
Informations de publication
Date de publication:
01 04 2020
01 04 2020
Historique:
pubmed:
3
4
2019
medline:
3
8
2021
entrez:
3
4
2019
Statut:
epublish
Résumé
Cancer is often associated with alterations in the chaperome, a collection of chaperones, cochaperones, and other cofactors. Changes in the expression levels of components of the chaperome, in the interaction strength among chaperome components, alterations in chaperome constituency, and in the cellular location of chaperome members, are all hallmarks of cancer. Here we aim to provide an overview on how chemical biology has played a role in deciphering such complexity in the biology of the chaperome in cancer and in other diseases. The focus here is narrow and on pathologic changes in the chaperome executed by enhancing the interaction strength between components of distinct chaperome pathways, specifically between those of HSP90 and HSP70 pathways. We will review chemical tools and chemical probe-based assays, with a focus on HSP90. We will discuss how kinetic binding, not classical equilibrium binding, is most appropriate in the development of drugs and probes for the chaperome in disease. We will then present our view on how chaperome inhibitors may become potential drugs and diagnostics in cancer.
Identifiants
pubmed: 30936118
pii: cshperspect.a034116
doi: 10.1101/cshperspect.a034116
pmc: PMC6773535
mid: NIHMS1039026
pii:
doi:
Substances chimiques
Antineoplastic Agents
0
HSP70 Heat-Shock Proteins
0
HSP90 Heat-Shock Proteins
0
Molecular Chaperones
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIA NIH HHS
ID : R56 AG061869
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA155226
Pays : United States
Organisme : NCI NIH HHS
ID : R21 CA158609
Pays : United States
Organisme : NCI NIH HHS
ID : P50 CA192937
Pays : United States
Organisme : NIA NIH HHS
ID : U01 AG032969
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA172546
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA119001
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NCI NIH HHS
ID : P01 CA186866
Pays : United States
Informations de copyright
Copyright © 2020 Cold Spring Harbor Laboratory Press; all rights reserved.
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