Arakel, Eric Clement

[["dc.bibliographiccitation.firstpage","1882"],["dc.bibliographiccitation.issue","7, Part B"],["dc.bibliographiccitation.lastpage","1893"],["dc.bibliographiccitation.volume","1863"],["dc.contributor.author","Brandenburg, Sören"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Lehnart, Stephan E."],["dc.date.accessioned","2017-09-07T11:44:49Z"],["dc.date.available","2017-09-07T11:44:49Z"],["dc.date.issued","2016"],["dc.description.abstract","Atrial cardiomyocytes are essential for fluid homeostasis, ventricular filling, and survival, yet their cell biology and physiology are incompletely understood. It has become clear that the cell fate of atrial cardiomyocytes depends significantly on transcription programs that might control thousands of differentially expressed genes. Atrial muscle membranes propagate action potentials and activate myofilament force generation, producing overall faster contractions than ventricular muscles. While atria-specific excitation and contractility depend critically on intracellular Ca2+ signalling, voltage-dependent L-type Ca2+ channels and ryanodine receptor Ca2+ release channels are each expressed at high levels similar to ventricles. However, intracellular Ca2+ transients in atrial cardiomyocytes are markedly heterogeneous and fundamentally different from ventricular cardiomyocytes. In addition, differential atria-specific K+ channel expression and trafficking confer unique electrophysiological and metabolic properties. Because diseased atria have the propensity to perpetuate fast arrhythmias, we discuss our understanding about the cell-specific mechanisms that lead to metabolic and/or mitochondrial dysfunction in atrial fibrillation. Interestingly, recent work identified potential atria-specific mechanisms that lead to early contractile dysfunction and metabolic remodelling, suggesting highly interdependent metabolic, electrical, and contractile pathomechanisms. Hence, the objective of this review is to provide an integrated model of atrial cardiomyocytes, from tissue-specific cell properties, intracellular metabolism, and excitation-contraction (EC) coupling to early pathological changes, in particular metabolic dysfunction and tissue remodelling due to atrial fibrillation and aging. This article is part of a Special Issue entitled: Cardiomyocyte Biology: Integration of Developmental and Environmental Cues in the Heart edited by Marcus Schaub and Hughes Abriel. (c) 2015 Published by Elsevier B.V."],["dc.identifier.doi","10.1016/j.bbamcr.2015.11.025"],["dc.identifier.gro","3141657"],["dc.identifier.isi","000378360400022"],["dc.identifier.pmid","26620800"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6120"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/108"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A07: Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation","SFB 1002 | A09: Lokale molekulare Nanodomänen-Regulation der kardialen Ryanodin-Rezeptor-Funktion"],["dc.relation.conference","8th Ascona International Workshop on Cardiomyocyte Biology - Integration of Developmental and Environmental Cues"],["dc.relation.eissn","0006-3002"],["dc.relation.eventend","2015-05-03"],["dc.relation.eventlocation","Ascona, SWITZERLAND"],["dc.relation.eventstart","2015-05-03"],["dc.relation.ispartof","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.relation.issn","0167-4889"],["dc.relation.workinggroup","RG Brandenburg"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","The molecular and functional identities of atrial cardiomyocytes in health and disease"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2106"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","2119"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Brandenburg, Sören"],["dc.contributor.author","Uchida, Keita"],["dc.contributor.author","Zhang, Haixia"],["dc.contributor.author","Lin, Yu-Wen"],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Sulkin, Matthew S."],["dc.contributor.author","Efimov, Igor R."],["dc.contributor.author","Nichols, Colin G."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:46:16Z"],["dc.date.available","2017-09-07T11:46:16Z"],["dc.date.issued","2014"],["dc.description.abstract","The copy number of membrane proteins at the cell surface is tightly regulated. Many ion channels and receptors present retrieval motifs to COPI vesicle coats and are retained in the early secretory pathway. In some cases, the interaction with COPI is prevented by binding to 14-3- 3 proteins. However, the functional significance of this antagonism between COPI and 14-3-3 in terminally differentiated cells is unknown. Here, we show that ATP-sensitive K+ (K-ATP) channels, which are composed of Kir6.2 and SUR1 subunits, are stalled in the Golgi complex of ventricular, but not atrial, cardiomyocytes. Upon sustained beta-adrenergic stimulation, which leads to activation of protein kinase A (PKA), SUR1-containing channels reach the plasma membrane of ventricular cells. We show that PKA-dependent phosphorylation of the C-terminus of Kir6.2 decreases binding to COPI and, thereby, silences the arginine-based retrieval signal. Thus, activation of the sympathetic nervous system releases this population of KATP channels from storage in the Golgi and, hence, might facilitate the adaptive response to metabolic challenges."],["dc.identifier.doi","10.1242/jcs.141440"],["dc.identifier.gro","3142132"],["dc.identifier.isi","000335814800021"],["dc.identifier.pmid","24569881"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10660"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4900"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/3"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A05: Molekulares Imaging von kardialen Calcium-Freisetzungsdomänen"],["dc.relation","SFB 1002 | A07:Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation.eissn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.relation.workinggroup","RG Brandenburg"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Tuning the electrical properties of the heart by differential trafficking of K-ATP ion channel complexes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]