Nucleoside diphosphate kinase-C suppresses cAMP formation in human heart failure
Background:Chronic heart failure (HF) is associated with altered signal transduction via β-adrenoceptors and G proteins and with reduced cAMP formation. Nucleoside diphosphate kinases (NDPKs) are enriched at the plasma membrane of patients with end-stage HF, but the functional consequences of this a...
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| Hauptverfasser: | , , , , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2017
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| In: |
Circulation
Year: 2017, Jahrgang: 135, Heft: 9, Pages: 881-897 |
| ISSN: | 1524-4539 |
| DOI: | 10.1161/CIRCULATIONAHA.116.022852 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1161/CIRCULATIONAHA.116.022852 Verlag, Volltext: https://www.ahajournals.org/doi/10.1161/CIRCULATIONAHA.116.022852 
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| Verfasserangaben: | Issam H. Abu-Taha, PhD, Jordi Heijman, PhD, Hans-Jörg Hippe, MD, Nadine M. Wolf, PhD, Ali El-Armouche, MD, Viacheslav O. Nikolaev, PhD, Marina Schäfer, MSc, Christina M. Würtz, PhD, Stefan Neef, MD, Niels Voigt, MD, István Baczkó, MD, PhD, András Varró, MD, PhD, DSc, Marion Müller, MSc, Benjamin Meder, MD, Hugo A. Katus, MD, Katharina Spiger, PhD, Christiane Vettel, PhD, Lorenz H. Lehmann, MD, Johannes Backs, MD, Edward Y. Skolnik, MD, Susanne Lutz, PhD, Dobromir Dobrev, MD, Thomas Wieland, PhD |
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| 245 | 1 | 0 | |a Nucleoside diphosphate kinase-C suppresses cAMP formation in human heart failure |c Issam H. Abu-Taha, PhD, Jordi Heijman, PhD, Hans-Jörg Hippe, MD, Nadine M. Wolf, PhD, Ali El-Armouche, MD, Viacheslav O. Nikolaev, PhD, Marina Schäfer, MSc, Christina M. Würtz, PhD, Stefan Neef, MD, Niels Voigt, MD, István Baczkó, MD, PhD, András Varró, MD, PhD, DSc, Marion Müller, MSc, Benjamin Meder, MD, Hugo A. Katus, MD, Katharina Spiger, PhD, Christiane Vettel, PhD, Lorenz H. Lehmann, MD, Johannes Backs, MD, Edward Y. Skolnik, MD, Susanne Lutz, PhD, Dobromir Dobrev, MD, Thomas Wieland, PhD |
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| 520 | |a Background:Chronic heart failure (HF) is associated with altered signal transduction via β-adrenoceptors and G proteins and with reduced cAMP formation. Nucleoside diphosphate kinases (NDPKs) are enriched at the plasma membrane of patients with end-stage HF, but the functional consequences of this are largely unknown, particularly for NDPK-C. Here, we investigated the potential role of NDPK-C in cardiac cAMP formation and contractility.Methods:Real-time polymerase chain reaction, (far) Western blot, immunoprecipitation, and immunocytochemistry were used to study the expression, interaction with G proteins, and localization of NDPKs. cAMP levels were determined with immunoassays or fluorescent resonance energy transfer, and contractility was determined in cardiomyocytes (cell shortening) and in vivo (fractional shortening).Results:NDPK-C was essential for the formation of an NDPK-B/G protein complex. Protein and mRNA levels of NDPK-C were upregulated in end-stage human HF, in rats after long-term isoprenaline stimulation through osmotic minipumps, and after incubation of rat neonatal cardiomyocytes with isoprenaline. Isoprenaline also promoted translocation of NDPK-C to the plasma membrane. Overexpression of NDPK-C in cardiomyocytes increased cAMP levels and sensitized cardiomyocytes to isoprenaline-induced augmentation of contractility, whereas NDPK-C knockdown decreased cAMP levels. In vivo, depletion of NDPK-C in zebrafish embryos caused cardiac edema and ventricular dysfunction. NDPK-B knockout mice had unaltered NDPK-C expression but showed contractile dysfunction and exacerbated cardiac remodeling during long-term isoprenaline stimulation. In human end-stage HF, the complex formation between NDPK-C and Gαi2 was increased whereas the NDPK-C/Gαs interaction was decreased, producing a switch that may contribute to an NDPK-C-dependent cAMP reduction in HF.Conclusions:Our findings identify NDPK-C as an essential requirement for both the interaction between NDPK isoforms and between NDPK isoforms and G proteins. NDPK-C is a novel critical regulator of β-adrenoceptor/cAMP signaling and cardiac contractility. By switching from Gαs to Gαi2 activation, NDPK-C may contribute to lower cAMP levels and the related contractile dysfunction in HF. | ||
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