Novel potent azetidine-based compounds irreversibly inhibit Stat3 activation and induce antitumor response against human breast tumor growth in vivo

Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies the Stat3-inhibitory activity of lead compounds to levels previously unseen. The azetidine-based compounds, including H172 (9f) and H182, irr...

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Published inCancer letters Vol. 534; p. 215613
Main Authors Yue, Peibin, Zhu, Yinsong, Brotherton-Pleiss, Christine, Fu, Wenzhen, Verma, Nagendra, Chen, Jasmine, Nakamura, Kayo, Chen, Weiliang, Chen, Yue, Alonso-Valenteen, Felix, Mikhael, Simoun, Medina-Kauwe, Lali, Kershaw, Kathleen M., Celeridad, Maria, Pan, Songqin, Limpert, Allison S., Sheffler, Douglas J., Cosford, Nicholas D.P., Shiao, Stephen L., Tius, Marcus A., Lopez-Tapia, Francisco, Turkson, James
Format Journal Article
LanguageEnglish
Published Ireland Elsevier B.V 28.05.2022
Elsevier Limited
Subjects
Animals
Antitumor activity
Antitumor cell effects
Apoptosis
Azetidines - pharmacology
Breast cancer
Cancer therapies
Cell death
Cell Line, Tumor
Covalent modification
Epidermal growth factor
Fibroblasts
Gene expression
Humans
Hydrochloric acid
Janus kinase
Kinases
Laboratory animals
Mass spectroscopy
Mice
Peptides
Phosphorylation
Proteins
Scientific imaging
Signal transducer and activator of transcription
Signal Transduction
Site-directed mutagenesis
Small-molecule inhibitors
Stat1 protein
Stat3 protein
STAT3 Transcription Factor - metabolism
Stat5 protein
Therapeutic targets
Transcription
Triple Negative Breast Neoplasms - drug therapy
Triple Negative Breast Neoplasms - genetics
Tumor growth inhibition
Xenografts
Signal transducer and activator of transcription
Antitumor cell effects
Small-molecule inhibitors
Covalent modification
Tumor growth inhibition
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Abstract Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies the Stat3-inhibitory activity of lead compounds to levels previously unseen. The azetidine-based compounds, including H172 (9f) and H182, irreversibly bind to Stat3 and selectively inhibit Stat3 activity (IC50 0.38–0.98 μM) over Stat1 or Stat5 (IC50 > 15.8 μM) in vitro. Mass spectrometry detected the Stat3 cysteine peptides covalently bound to the azetidine compounds, and the key residues, Cys426 and Cys468, essential for the high potency inhibition, were confirmed by site-directed mutagenesis. In triple-negative breast cancer (TNBC) models, treatment with the azetidine compounds inhibited constitutive and ligand-induced Stat3 signaling, and induced loss of viable cells and tumor cell death, compared to no effect on the induction of Janus kinase (JAK)2, Src, epidermal growth factor receptor (EGFR), and other proteins, or weak effects on cells that do not harbor aberrantly-active Stat3. H120 (8e) and H182 as a single agent inhibited growth of TNBC xenografts, and H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse TNBC growth and improved survival in syngeneic models. We identify potent azetidine-based, selective, irreversible Stat3 inhibitors that inhibit TNBC growth in vivo. •Azetidine-based compounds, exemplified by H182 inhibit Stat3 activity with nanomolar-sub-micromolar potency•Azetidine-based compounds irreversibly bind to Stat3•Mass spectrometry detected the covalent binding to the key residues, Cys328, Cys426, Cys468, and Cys542•H182, H120 and other azetidine compounds inhibit constitutive and ligand-induced Stat3 signaling in triple-negative breast cancer cells•H120 or H182 as a single agent inhibited growth of triple-negative breast tumor xenografts•H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse triple-negative breast cancer growth and improved survival in syngeneic models
AbstractList Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies the Stat3-inhibitory activity of lead compounds to levels previously unseen. The azetidine-based compounds, including H172 (9f) and H182, irreversibly bind to Stat3 and selectively inhibit Stat3 activity (IC 0.38-0.98 μM) over Stat1 or Stat5 (IC  > 15.8 μM) in vitro. Mass spectrometry detected the Stat3 cysteine peptides covalently bound to the azetidine compounds, and the key residues, Cys426 and Cys468, essential for the high potency inhibition, were confirmed by site-directed mutagenesis. In triple-negative breast cancer (TNBC) models, treatment with the azetidine compounds inhibited constitutive and ligand-induced Stat3 signaling, and induced loss of viable cells and tumor cell death, compared to no effect on the induction of Janus kinase (JAK)2, Src, epidermal growth factor receptor (EGFR), and other proteins, or weak effects on cells that do not harbor aberrantly-active Stat3. H120 (8e) and H182 as a single agent inhibited growth of TNBC xenografts, and H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse TNBC growth and improved survival in syngeneic models. We identify potent azetidine-based, selective, irreversible Stat3 inhibitors that inhibit TNBC growth in vivo.
Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies the Stat3-inhibitory activity of lead compounds to levels previously unseen. The azetidine-based compounds, including H172 (9f) and H182, irreversibly bind to Stat3 and selectively inhibit Stat3 activity (IC50 0.38–0.98 μM) over Stat1 or Stat5 (IC50 > 15.8 μM) in vitro. Mass spectrometry detected the Stat3 cysteine peptides covalently bound to the azetidine compounds, and the key residues, Cys426 and Cys468, essential for the high potency inhibition, were confirmed by site-directed mutagenesis. In triple-negative breast cancer (TNBC) models, treatment with the azetidine compounds inhibited constitutive and ligand-induced Stat3 signaling, and induced loss of viable cells and tumor cell death, compared to no effect on the induction of Janus kinase (JAK)2, Src, epidermal growth factor receptor (EGFR), and other proteins, or weak effects on cells that do not harbor aberrantly-active Stat3. H120 (8e) and H182 as a single agent inhibited growth of TNBC xenografts, and H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse TNBC growth and improved survival in syngeneic models. We identify potent azetidine-based, selective, irreversible Stat3 inhibitors that inhibit TNBC growth in vivo.
Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies the Stat3-inhibitory activity of lead compounds to levels previously unseen. The azetidine-based compounds, including H172 (9f) and H182, irreversibly bind to Stat3 and selectively inhibit Stat3 activity (IC50 0.38–0.98 μM) over Stat1 or Stat5 (IC50 > 15.8 μM) in vitro. Mass spectrometry detected the Stat3 cysteine peptides covalently bound to the azetidine compounds, and the key residues, Cys426 and Cys468, essential for the high potency inhibition, were confirmed by site-directed mutagenesis. In triple-negative breast cancer (TNBC) models, treatment with the azetidine compounds inhibited constitutive and ligand-induced Stat3 signaling, and induced loss of viable cells and tumor cell death, compared to no effect on the induction of Janus kinase (JAK)2, Src, epidermal growth factor receptor (EGFR), and other proteins, or weak effects on cells that do not harbor aberrantly-active Stat3. H120 (8e) and H182 as a single agent inhibited growth of TNBC xenografts, and H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse TNBC growth and improved survival in syngeneic models. We identify potent azetidine-based, selective, irreversible Stat3 inhibitors that inhibit TNBC growth in vivo. •Azetidine-based compounds, exemplified by H182 inhibit Stat3 activity with nanomolar-sub-micromolar potency•Azetidine-based compounds irreversibly bind to Stat3•Mass spectrometry detected the covalent binding to the key residues, Cys328, Cys426, Cys468, and Cys542•H182, H120 and other azetidine compounds inhibit constitutive and ligand-induced Stat3 signaling in triple-negative breast cancer cells•H120 or H182 as a single agent inhibited growth of triple-negative breast tumor xenografts•H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse triple-negative breast cancer growth and improved survival in syngeneic models
Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies the Stat3-inhibitory activity of lead compounds to levels previously unseen. The azetidine-based compounds, including H172 ( 9f) and H182, irreversibly bind to Stat3 and selectively inhibit Stat3 activity (IC 50 0.38–0.98 μM) over Stat1 or Stat5 (IC 50 > 15.8 μM) in vitro . Mass spectrometry detected the Stat3 cysteine peptides covalently bound to the azetidine compounds, and the key residues, Cys426 and Cys468, essential for the high potency inhibition, were confirmed by site-directed mutagenesis. In triple-negative breast cancer (TNBC) models, treatment with the azetidine compounds inhibited constitutive and ligand-induced Stat3 signaling, and induced loss of viable cells and tumor cell death, compared to no effect on the induction of Janus kinase (JAK)2, Src, epidermal growth factor receptor (EGFR), and other proteins, or weak effects on cells that do not harbor aberrantly-active Stat3. H120 ( 8e ) and H182 as a single agent inhibited growth of TNBC xenografts, and H278 (hydrochloric acid salt of H182) in combination with radiation completely blocked mouse TNBC growth and improved survival in syngeneic models. We identify potent azetidine-based, selective, irreversible Stat3 inhibitors that inhibit TNBC growth in vivo .
ArticleNumber 215613
Author Pan, Songqin
Yue, Peibin
Verma, Nagendra
Sheffler, Douglas J.
Tius, Marcus A.
Zhu, Yinsong
Mikhael, Simoun
Nakamura, Kayo
Turkson, James
Cosford, Nicholas D.P.
Chen, Yue
Lopez-Tapia, Francisco
Chen, Jasmine
Kershaw, Kathleen M.
Limpert, Allison S.
Fu, Wenzhen
Brotherton-Pleiss, Christine
Medina-Kauwe, Lali
Celeridad, Maria
Shiao, Stephen L.
Chen, Weiliang
Alonso-Valenteen, Felix
AuthorAffiliation d Department of Chemistry, University of Hawaii, Manoa, 2545 McCarthy Mall, Honolulu, HI, 96825, USA
e Department of Biomedical Sciences, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Los Angeles, CA, 90048, USA
c Cancer Biology Program, University of Hawaii Cancer Center, 701 Ilalo St, Honolulu, HI, 96813, USA
g Cell and Molecular Biology of Cancer Program, Cancer Center, Sanford Burnham Prebys Medical Discovery Institute, 10901 N. Torrey Pines Rd, La Jolla, CA, 92037, USA
h W. M. Keck Proteomics Laboratory, University of California, Riverside, CA, 92521, USA
a Department of Medicine, Division of Medical Oncology, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Los Angenes, CA, 90048, USA
b Cancer Biology Program, Cedars-Sinai Cancer, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Los Angeles, CA, 90048, USA
f Department of Radiation Oncology, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Los Angeles, CA, 90048, USA
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/35276290$$D View this record in MEDLINE/PubMed
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ISSN 0304-3835
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Thu Sep 26 16:51:09 EDT 2024
Thu Oct 24 09:17:58 EDT 2024
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Keywords Signal transducer and activator of transcription
Antitumor cell effects
Small-molecule inhibitors
Covalent modification
Tumor growth inhibition
Language English
License This is an open access article under the CC BY license.
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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ORCID 0000-0002-6964-1602
OpenAccessLink https://www.sciencedirect.com/science/article/pii/S030438352200088X
PMID 35276290
PQID 2640562469
PQPubID 2031080
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pubmed_primary_35276290
elsevier_sciencedirect_doi_10_1016_j_canlet_2022_215613
PublicationCentury 2000
PublicationDate 2022-05-28
PublicationDateYYYYMMDD 2022-05-28
PublicationDate_xml – month: 05
  year: 2022
  text: 2022-05-28
  day: 28
PublicationDecade 2020
PublicationPlace Ireland
PublicationPlace_xml – name: Ireland
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PublicationTitle Cancer letters
PublicationTitleAlternate Cancer Lett
PublicationYear 2022
Publisher Elsevier B.V
Elsevier Limited
Publisher_xml – name: Elsevier B.V
– name: Elsevier Limited
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Snippet Signal transducer and activator of transcription (Stat)3 is a valid anticancer therapeutic target. We have discovered a highly potent chemotype that amplifies...
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pubmed
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 215613
SubjectTerms Animals
Antitumor activity
Antitumor cell effects
Apoptosis
Azetidines - pharmacology
Breast cancer
Cancer therapies
Cell death
Cell Line, Tumor
Covalent modification
Epidermal growth factor
Fibroblasts
Gene expression
Humans
Hydrochloric acid
Janus kinase
Kinases
Laboratory animals
Mass spectroscopy
Mice
Peptides
Phosphorylation
Proteins
Scientific imaging
Signal transducer and activator of transcription
Signal Transduction
Site-directed mutagenesis
Small-molecule inhibitors
Stat1 protein
Stat3 protein
STAT3 Transcription Factor - metabolism
Stat5 protein
Therapeutic targets
Transcription
Triple Negative Breast Neoplasms - drug therapy
Triple Negative Breast Neoplasms - genetics
Tumor growth inhibition
Xenografts
Title Novel potent azetidine-based compounds irreversibly inhibit Stat3 activation and induce antitumor response against human breast tumor growth in vivo
URI https://dx.doi.org/10.1016/j.canlet.2022.215613
https://www.ncbi.nlm.nih.gov/pubmed/35276290
https://www.proquest.com/docview/2640562469
https://pubmed.ncbi.nlm.nih.gov/PMC9867837
Volume 534
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