A high throughput substrate binding assay reveals hexachlorophene as an inhibitor of the ER-resident HSP70 chaperone GRP78.


Journal

Bioorganic & medicinal chemistry letters
ISSN: 1464-3405
Titre abrégé: Bioorg Med Chem Lett
Pays: England
ID NLM: 9107377

Informations de publication

Date de publication:
15 07 2019
Historique:
received: 14 03 2019
accepted: 19 05 2019
pubmed: 28 5 2019
medline: 10 9 2020
entrez: 27 5 2019
Statut: ppublish

Résumé

Glucose-regulated protein 78 (GRP78) is the ER resident 70 kDa heat shock protein 70 (HSP70) and has been hypothesized to be a therapeutic target for various forms of cancer due to its role in mitigating proteotoxic stress in the ER, its elevated expression in some cancers, and the correlation between high levels for GRP78 and a poor prognosis. Herein we report the development and use of a high throughput fluorescence polarization-based peptide binding assay as an initial step toward the discovery and development of GRP78 inhibitors. This assay was used in a pilot screen to discover the anti-infective agent, hexachlorophene, as an inhibitor of GRP78. Through biochemical characterization we show that hexachlorophene is a competitive inhibitor of the GRP78-peptide interaction. Biological investigations showed that this molecule induces the unfolded protein response, induces autophagy, and leads to apoptosis in a colon carcinoma cell model, which is known to be sensitive to GRP78 inhibition.

Identifiants

pubmed: 31129054
pii: S0960-894X(19)30338-5
doi: 10.1016/j.bmcl.2019.05.041
pmc: PMC6608569
mid: NIHMS1530304
pii:
doi:

Substances chimiques

Endoplasmic Reticulum Chaperone BiP 0
HSP70 Heat-Shock Proteins 0
HSPA5 protein, human 0
Hexachlorophene IWW5FV6NK2

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

1689-1693

Subventions

Organisme : NIEHS NIH HHS
ID : P30 ES006694
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM120350
Pays : United States
Organisme : NIEHS NIH HHS
ID : T32 ES007091
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008804
Pays : United States

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

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Auteurs

Andrew J Ambrose (AJ)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Christopher J Zerio (CJ)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Jared Sivinski (J)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Cody J Schmidlin (CJ)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Taoda Shi (T)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Alison B Ross (AB)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Kimberly J Widrick (KJ)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Steven M Johnson (SM)

Indiana University, School of Medicine, Department of Biochemistry and Molecular Biology, 635 Barnhill Dr., Indianapolis, IN 46202, USA.

Donna D Zhang (DD)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA.

Eli Chapman (E)

Department of Pharmacology and Toxicology, College of Pharmacy, University of Arizona, 1703 East Mabel Street, PO Box 210207, Tucson, AZ 85721, USA. Electronic address: chapman@pharmacy.arizona.edu.

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Classifications MeSH