Interference with ERK-dimerization at the nucleocytosolic interface targets pathological ERK1/2 signaling without cardiotoxic side-effects

Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERK -autophosphorylation was identi...

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Published inNature communications Vol. 11; no. 1; pp. 1733 - 16
Main Authors Tomasovic, Angela, Brand, Theresa, Schanbacher, Constanze, Kramer, Sofia, Hümmert, Martin W, Godoy, Patricio, Schmidt-Heck, Wolfgang, Nordbeck, Peter, Ludwig, Jonas, Homann, Susanne, Wiegering, Armin, Shaykhutdinov, Timur, Kratz, Christoph, Knüchel, Ruth, Müller-Hermelink, Hans-Konrad, Rosenwald, Andreas, Frey, Norbert, Eichler, Jutta, Dobrev, Dobromir, El-Armouche, Ali, Hengstler, Jan G, Müller, Oliver J, Hinrichs, Karsten, Cuello, Friederike, Zernecke, Alma, Lorenz, Kristina
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 07.04.2020
Nature Publishing Group UK
Nature Portfolio
Subjects
Animals
Cancer
Cardiomyocytes
Cardiotoxicity
Cell Culture Techniques
Cell proliferation
Cell-Penetrating Peptides - chemical synthesis
Cell-Penetrating Peptides - pharmacology
Cell-Penetrating Peptides - toxicity
Colonic Neoplasms - drug therapy
Colonic Neoplasms - metabolism
Congestive heart failure
Coronary artery disease
Dimerization
Disorders
Drug delivery
Drug Delivery Systems
Extracellular signal-regulated kinase
Extracellular Signal-Regulated MAP Kinases - drug effects
Extracellular Signal-Regulated MAP Kinases - metabolism
Heart failure
Heart Failure - drug therapy
Heart Failure - metabolism
Humans
Hypertrophy
Interference
Kinases
Lung Neoplasms - drug therapy
Lung Neoplasms - metabolism
MAP Kinase Signaling System - drug effects
MAP Kinase Signaling System - physiology
Mice
Mice, Inbred C57BL
Molecular Medicine
Phosphorylation
Rats
Rats, Sprague-Dawley
Side effects
Signal Transduction
Signaling
Strategy
Online AccessGet full text

Cover

Abstract Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERK -autophosphorylation was identified to cause pathological cardiac hypertrophy. Here we report that interference with ERK-dimerization, a prerequisite for ERK -phosphorylation, minimizes cardiac hypertrophy without inducing cardiac adverse effects: an ERK-dimerization inhibitory peptide (EDI) prevents ERK -phosphorylation, nuclear ERK1/2-signaling and cardiomyocyte hypertrophy, protecting from pressure-overload-induced heart failure in mice whilst preserving ERK1/2-activity and cytosolic survival signaling. We also examine this alternative ERK1/2-targeting strategy in cancer: indeed, ERK -phosphorylation is strongly upregulated in cancer and EDI efficiently suppresses cancer cell proliferation without causing cardiotoxicity. This powerful cardio-safe strategy of interfering with ERK-dimerization thus combats pathological ERK1/2-signaling in heart and cancer, and may potentially expand therapeutic options for ERK1/2-related diseases, such as heart failure and genetic syndromes.
AbstractList Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERKT188-autophosphorylation was identified to cause pathological cardiac hypertrophy. Here we report that interference with ERK-dimerization, a prerequisite for ERKT188-phosphorylation, minimizes cardiac hypertrophy without inducing cardiac adverse effects: an ERK-dimerization inhibitory peptide (EDI) prevents ERKT188-phosphorylation, nuclear ERK1/2-signaling and cardiomyocyte hypertrophy, protecting from pressure-overload-induced heart failure in mice whilst preserving ERK1/2-activity and cytosolic survival signaling. We also examine this alternative ERK1/2-targeting strategy in cancer: indeed, ERKT188-phosphorylation is strongly upregulated in cancer and EDI efficiently suppresses cancer cell proliferation without causing cardiotoxicity. This powerful cardio-safe strategy of interfering with ERK-dimerization thus combats pathological ERK1/2-signaling in heart and cancer, and may potentially expand therapeutic options for ERK1/2-related diseases, such as heart failure and genetic syndromes.Drugs targeting dysregulated ERK1/2 signaling can cause severe cardiac side effects, precluding their wide therapeutic application. Here, a new and cardio-safe targeting strategy is presented that interferes with ERK dimerization to prevent pathological ERK1/2 signaling in the heart and cancer.
Drugs targeting dysregulated ERK1/2 signaling can cause severe cardiac side effects, precluding their wide therapeutic application. Here, a new and cardio-safe targeting strategy is presented that interferes with ERK dimerization to prevent pathological ERK1/2 signaling in the heart and cancer.
Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERK T188 -autophosphorylation was identified to cause pathological cardiac hypertrophy. Here we report that interference with ERK-dimerization, a prerequisite for ERK T188 -phosphorylation, minimizes cardiac hypertrophy without inducing cardiac adverse effects: an ERK-dimerization inhibitory peptide (EDI) prevents ERK T188 -phosphorylation, nuclear ERK1/2-signaling and cardiomyocyte hypertrophy, protecting from pressure-overload-induced heart failure in mice whilst preserving ERK1/2-activity and cytosolic survival signaling. We also examine this alternative ERK1/2-targeting strategy in cancer: indeed, ERK T188 -phosphorylation is strongly upregulated in cancer and EDI efficiently suppresses cancer cell proliferation without causing cardiotoxicity. This powerful cardio-safe strategy of interfering with ERK-dimerization thus combats pathological ERK1/2-signaling in heart and cancer, and may potentially expand therapeutic options for ERK1/2-related diseases, such as heart failure and genetic syndromes. Drugs targeting dysregulated ERK1/2 signaling can cause severe cardiac side effects, precluding their wide therapeutic application. Here, a new and cardio-safe targeting strategy is presented that interferes with ERK dimerization to prevent pathological ERK1/2 signaling in the heart and cancer.
Abstract Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERK T188 -autophosphorylation was identified to cause pathological cardiac hypertrophy. Here we report that interference with ERK-dimerization, a prerequisite for ERK T188 -phosphorylation, minimizes cardiac hypertrophy without inducing cardiac adverse effects: an ERK-dimerization inhibitory peptide (EDI) prevents ERK T188 -phosphorylation, nuclear ERK1/2-signaling and cardiomyocyte hypertrophy, protecting from pressure-overload-induced heart failure in mice whilst preserving ERK1/2-activity and cytosolic survival signaling. We also examine this alternative ERK1/2-targeting strategy in cancer: indeed, ERK T188 -phosphorylation is strongly upregulated in cancer and EDI efficiently suppresses cancer cell proliferation without causing cardiotoxicity. This powerful cardio-safe strategy of interfering with ERK-dimerization thus combats pathological ERK1/2-signaling in heart and cancer, and may potentially expand therapeutic options for ERK1/2-related diseases, such as heart failure and genetic syndromes.
Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer. Inhibition of ERK1/2, however, can cause severe cardiac side-effects, precluding its wide therapeutic application. ERK -autophosphorylation was identified to cause pathological cardiac hypertrophy. Here we report that interference with ERK-dimerization, a prerequisite for ERK -phosphorylation, minimizes cardiac hypertrophy without inducing cardiac adverse effects: an ERK-dimerization inhibitory peptide (EDI) prevents ERK -phosphorylation, nuclear ERK1/2-signaling and cardiomyocyte hypertrophy, protecting from pressure-overload-induced heart failure in mice whilst preserving ERK1/2-activity and cytosolic survival signaling. We also examine this alternative ERK1/2-targeting strategy in cancer: indeed, ERK -phosphorylation is strongly upregulated in cancer and EDI efficiently suppresses cancer cell proliferation without causing cardiotoxicity. This powerful cardio-safe strategy of interfering with ERK-dimerization thus combats pathological ERK1/2-signaling in heart and cancer, and may potentially expand therapeutic options for ERK1/2-related diseases, such as heart failure and genetic syndromes.
ArticleNumber 1733
Author Tomasovic, Angela
Wiegering, Armin
Homann, Susanne
Kramer, Sofia
Eichler, Jutta
Dobrev, Dobromir
Godoy, Patricio
Hengstler, Jan G
Hinrichs, Karsten
Rosenwald, Andreas
Kratz, Christoph
Shaykhutdinov, Timur
Nordbeck, Peter
Cuello, Friederike
Müller-Hermelink, Hans-Konrad
Schanbacher, Constanze
Schmidt-Heck, Wolfgang
Ludwig, Jonas
El-Armouche, Ali
Brand, Theresa
Frey, Norbert
Knüchel, Ruth
Lorenz, Kristina
Zernecke, Alma
Müller, Oliver J
Hümmert, Martin W
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  organization: Comprehensive Heart Failure Center, 97078, Würzburg, Germany. lorenz@toxi.uni-wuerzburg.de
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32265441$$D View this record in MEDLINE/PubMed
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Snippet Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer....
Abstract Dysregulation of extracellular signal-regulated kinases (ERK1/2) is linked to several diseases including heart failure, genetic syndromes and cancer....
Drugs targeting dysregulated ERK1/2 signaling can cause severe cardiac side effects, precluding their wide therapeutic application. Here, a new and cardio-safe...
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SubjectTerms Animals
Cancer
Cardiomyocytes
Cardiotoxicity
Cell Culture Techniques
Cell proliferation
Cell-Penetrating Peptides - chemical synthesis
Cell-Penetrating Peptides - pharmacology
Cell-Penetrating Peptides - toxicity
Colonic Neoplasms - drug therapy
Colonic Neoplasms - metabolism
Congestive heart failure
Coronary artery disease
Dimerization
Disorders
Drug delivery
Drug Delivery Systems
Extracellular signal-regulated kinase
Extracellular Signal-Regulated MAP Kinases - drug effects
Extracellular Signal-Regulated MAP Kinases - metabolism
Heart failure
Heart Failure - drug therapy
Heart Failure - metabolism
Humans
Hypertrophy
Interference
Kinases
Lung Neoplasms - drug therapy
Lung Neoplasms - metabolism
MAP Kinase Signaling System - drug effects
MAP Kinase Signaling System - physiology
Mice
Mice, Inbred C57BL
Molecular Medicine
Phosphorylation
Rats
Rats, Sprague-Dawley
Side effects
Signal Transduction
Signaling
Strategy
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Title Interference with ERK-dimerization at the nucleocytosolic interface targets pathological ERK1/2 signaling without cardiotoxic side-effects
URI https://www.ncbi.nlm.nih.gov/pubmed/32265441
https://www.proquest.com/docview/2387244869/abstract/
https://pubmed.ncbi.nlm.nih.gov/PMC7138859
https://doaj.org/article/422072e270cd48449067eb1413f577cb
Volume 11
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