Nucleoside Diphosphate Kinase-C Suppresses cAMP Formation in Human Heart Failure

Circulation. 2017 Feb 28;135(9):881-897. doi: 10.1161/CIRCULATIONAHA.116.022852. Epub 2016 Dec 7.

Abstract

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.

Keywords: heart failure; myocardial contraction; receptors, adrenergic, beta; signal transduction.

MeSH terms

  • Animals
  • Cell Line
  • Cell Membrane / metabolism
  • Cyclic AMP / analysis*
  • Cyclic AMP / metabolism
  • Disease Models, Animal
  • Embryo, Nonmammalian / metabolism
  • GTP-Binding Protein alpha Subunits, G12-G13 / metabolism
  • Heart Failure / metabolism
  • Heart Failure / pathology*
  • Humans
  • Isoproterenol / pharmacology
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Myocytes, Cardiac / cytology
  • Myocytes, Cardiac / drug effects
  • Myocytes, Cardiac / metabolism
  • NM23 Nucleoside Diphosphate Kinases / analysis*
  • NM23 Nucleoside Diphosphate Kinases / antagonists & inhibitors
  • NM23 Nucleoside Diphosphate Kinases / genetics
  • NM23 Nucleoside Diphosphate Kinases / metabolism
  • Protein Binding
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • RNA Interference
  • RNA, Small Interfering / metabolism
  • Rats
  • Rats, Wistar
  • Zebrafish / growth & development

Substances

  • NM23 Nucleoside Diphosphate Kinases
  • Protein Isoforms
  • RNA, Small Interfering
  • Cyclic AMP
  • GTP-Binding Protein alpha Subunits, G12-G13
  • Isoproterenol