Journal of Molecular and Cellular Cardiology Impact Factor & Information

Publisher: International Society for Heart Research, Elsevier

Journal description

The Journal of Molecular and Cellular Cardiology, the official organ of the International Society for Heart Research, provides a forum for research papers dealing with the molecular biology, physiology, pharmacology, and pathophysiology of the heart and c

Current impact factor: 5.22

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 5.218
2012 Impact Factor 5.148
2011 Impact Factor 5.166
2010 Impact Factor 5.499
2009 Impact Factor 4.965
2008 Impact Factor 5.054
2006 Impact Factor 4.859
2005 Impact Factor 3.872
2004 Impact Factor 4.198
2003 Impact Factor 4.954
2002 Impact Factor 4.091
2001 Impact Factor 3.396
2000 Impact Factor 3.383
1999 Impact Factor 2.923
1998 Impact Factor 2.72
1997 Impact Factor 3.255
1996 Impact Factor 2.742
1995 Impact Factor 2.78
1994 Impact Factor 3.008
1993 Impact Factor 3.485
1992 Impact Factor 3.115

Impact factor over time

Impact factor

Additional details

5-year impact 5.03
Cited half-life 6.30
Immediacy index 1.48
Eigenfactor 0.03
Article influence 1.67
Website Journal of Molecular and Cellular Cardiology website
Other titles Journal of molecular and cellular cardiology (Online), Journal of molecular and cellular cardiology
ISSN 0022-2828
OCLC 36945690
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details


  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Pre-print allowed on any website or open access repository
    • Voluntary deposit by author of authors post-print allowed on authors' personal website, or institutions open scholarly website including Institutional Repository, without embargo, where there is not a policy or mandate
    • Deposit due to Funding Body, Institutional and Governmental policy or mandate only allowed where separate agreement between repository and the publisher exists.
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months .
    • Set statement to accompany deposit
    • Published source must be acknowledged
    • Must link to journal home page or articles' DOI
    • Publisher's version/PDF cannot be used
    • Articles in some journals can be made Open Access on payment of additional charge
    • NIH Authors articles will be submitted to PubMed Central after 12 months
    • Publisher last contacted on 18/10/2013
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: BACKGROUND: Cardiac alternans are proarrhythmic and mechanistically link cardiac mechanical dysfunction and sudden cardiac death. Beat-to-beat alternans occur when beats with large Ca2+ transients and long action potential duration (APD) alternate with the converse. APD alternans are typically driven by Ca2+ alternans and sarcoplasmic reticulum (SR) Ca2+ release alternans. But the effect of intercellular communication via gap junctions (GJ) on alternans in intact heart remains unknown. OBJECTIVE: We assessed the effects of cell-to-cell coupling on local alternans in intact Langendorff-perfused mouse hearts, measuring single myocyte [Ca2+] alternans synchronization among neighboring cells, and effects of β-adrenergic receptor (β-AR) activation and reduced GJ coupling. METHODS AND RESULTS: Mouse hearts (C57BL/6) were retrogradely perfused and loaded with Fluo-8 AM to record cardiac myocyte [Ca2+] in situ with confocal microscopy. Single cell resolution allowed analysis of alternans within the intact organ during alternans induction. Carbenoxolone (25 μM), a GJ inhibitor, significantly increased the occurrence and amplitude of alternans in single cells within the intact heart. Alternans were concordant between neighboring cells throughout the field of view, except transiently during onset. β-AR stimulation only reduced Ca2+ alternans in tissue that had reduced GJ coupling, matching effects seen in isolated myocytes. CONCLUSIONS: Ca2+ alternans among neighboring myocytes is predominantly concordant, likely because of electrical coupling between cells. Consistent with this, partial GJ uncoupling increased propensity and amplitude of Ca2+ alternans, and made them more sensitive to reversal by β-AR activation, as in isolated myocytes. Electrical coupling between myocytes may thus limit the alternans initiation, but also allow alternans to be more stable once established.
    Journal of Molecular and Cellular Cardiology 03/2015; DOI:10.1016/j.yjmcc.2015.03.012.
  • Source
    Journal of Molecular and Cellular Cardiology 03/2015; 81. DOI:10.1016/j.yjmcc.2015.02.023
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    ABSTRACT: Depressed sarcoplasmic reticulum (SR) calcium cycling, reflecting impaired SR Ca-transport and Ca-release, is a key and universal characteristic of human and experimental heart failure. These SR processes are regulated by multimeric protein complexes, including protein kinases and phosphatases as well as their anchoring and regulatory subunits that fine-tune Ca-handling in specific SR sub-compartments. SR Ca-transport is mediated by the SR Ca-ATPase (SERCA2a) and its regulatory phosphoprotein, phospholamban (PLN). Dephosphorylated PLN is an inhibitor of SERCA2a and phosphorylation by protein kinase A (PKA) or calcium-calmodulin-dependent protein kinases (CAMKII) relieves these inhibitory effects. Recent studies identified additional regulatory proteins, associated with PLN, that control SR Ca-transport. These include the inhibitor-1 (I-1) of protein phosphatase 1 (PP1), the small heat shock protein 20 (Hsp20) and the HS-1 associated protein X-1 (HAX1). In addition, the intraluminal histidine-rich calcium binding protein (HRC) has been shown to interact with both SERCA2a and triadin. Notably, there is physical and direct interaction between these protein players, mediating a fine-cross talk between SR Ca-uptake, storage and release. Importantly, regulation of SR Ca-cycling by the PLN/SERCA interactome does not only impact cardiomyocyte contractility, but also survival and remodeling. Indeed, naturally occurring variants in these Ca-cycling genes modulate their activity and interactions with other protein partners, resulting in depressed contractility and accelerated remodeling. These genetic variants may serve as potential prognostic or diagnostic markers in cardiac pathophysiology.
    Journal of Molecular and Cellular Cardiology 12/2014; 77. DOI:10.1016/j.yjmcc.2014.10.005
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    ABSTRACT: The phosphorylation level of MLC-2v is decreased by I/R.•This decrease contributes to the depressed myofilament Ca2 + sensitivity after I/R.•The loss of cMLCK but not cMLCP inhibits the phosphorylation of MLC-2v during I/R.•I/R-activated MMP-2 but not calpains, caspase-3, or proteasome cleaves cMLCK.•MMP-2 inhibition also improves post-ischemic Ca2 + transients in cardiomyocytes.
    Journal of Molecular and Cellular Cardiology 12/2014; 77. DOI:10.1016/j.yjmcc.2014.10.004
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    ABSTRACT: The incretin hormone glucagon-like peptide-1 (Glp1) is cardioprotective in models of ischemia-reperfusion injury, myocardial infarction and gluco/lipotoxicity. Inflammation is a factor in these models, yet it is unknown whether Glp1 receptor (Glp1r) agonists are protective against cardiac inflammation. We tested the hypothesis that the Glp1r agonist Exendin-4 (Ex4) is cardioprotective in mice with cardiac-specific monocyte chemoattractant protein-1 overexpression. These MHC-MCP1 mice exhibit increased cardiac monocyte infiltration, endoplasmic reticulum (ER) stress, apoptosis, fibrosis and left ventricular dysfunction. Ex4 treatment for 8 weeks improved cardiac function and reduced monocyte infiltration, fibrosis and apoptosis in MHC-MCP1 mice. Ex4 enhanced expression of the ER chaperone glucose-regulated protein-78 (GRP78), decreased expression of the pro-apoptotic ER stress marker CCAAT/-enhancer-binding protein homologous protein (CHOP) and increased expression of the ER calcium regulator Sarco/Endoplasmic Reticulum Calcium ATPase-2a (SERCA2a). These findings suggest that the Glp1r is a viable target for treating cardiomyopathies associated with stimulation of pro-inflammatory factors.
    Journal of Molecular and Cellular Cardiology 11/2014; 76. DOI:10.1016/j.yjmcc.2014.08.022
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    ABSTRACT: Consumption of adenosine triphosphate (ATP) by the heart can change dramatically as the energetic demands increase from a period of rest to strenuous activity. Mitochondrial ATP production is central to this metabolic response since the heart relies largely on oxidative phosphorylation as its source of intracellular ATP. Significant evidence has been acquired indicating that Ca2 + plays a critical role in regulating ATP production by the mitochondria. Here the evidence that the Ca2 + concentration in the mitochondrial matrix ([Ca2 +]m) plays a pivotal role in regulating ATP production by the mitochondria is critically reviewed and aspects of this process that are under current active investigation are highlighted. Importantly, current quantitative information on the bidirectional Ca2 + movement across the inner mitochondrial membrane (IMM) is examined in two parts. First, we review how Ca2 + influx into the mitochondrial matrix depends on the mitochondrial Ca2 + channel (i.e., the mitochondrial calcium uniporter or MCU). This discussion includes how the MCU open probability (PO) depends on the cytosolic Ca2 + concentration ([Ca2 +]i) and on the mitochondrial membrane potential (ΔΨm). Second, we discuss how steady-state [Ca2 +]m is determined by the dynamic balance between this MCU-based Ca2 + influx and mitochondrial Na+/Ca2 + exchanger (NCLX) based Ca2 + efflux. These steady-state [Ca2 +]m levels are suggested to regulate the metabolic energy supply due to Ca2 +-dependent regulation of mitochondrial enzymes of the tricarboxylic acid cycle (TCA), the proteins of the electron transport chain (ETC), and the F1F0 ATP synthase itself. We conclude by discussing the roles played by [Ca2 +]m in influencing mitochondrial responses under pathological conditions. This article is part of a Special Issue entitled "Mitochondria: From BasicMitochondrial Biology to Cardiovascular Disease."
    Journal of Molecular and Cellular Cardiology 11/2014; 78. DOI:10.1016/j.yjmcc.2014.10.019
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    ABSTRACT: Phospholamban (PLB) regulates the cardiac Ca(2+) pump (SERCA2a). To test how different species of PLB mutants compete to interact with the Ca(2+)-free, E2 conformation of SERCA2a, using the insect cell expression system, we examined how various exogenous PLB mutants regulated SER-20G-PLB, a chimeric WT-SERCA2a-Gly-WT-PLB construct, which retains a fully catalytic active Ca(2+)-pump and its intrinsically regulatory PLB-tether. Exogenous gain-of-function PLB mutants dominantly super-inhibited the WT-PLB-tethered SERCA2a. Further, in the Ca(2+)-free condition, co-expressed normal- or super-inhibitory PLB mutant with either engineered N30C or V49C residue cross-linked to Lys328 or V89C of SER-20G-PLB at the cytoplasmic or transmembrane domain, respectively, suggesting that these freely diffusing PLB mutants completely replaced the WT-PLB-tether and fit into the binding pocket previously occupied by WT-PLB. Micromolar Ca(2+) completely inhibited cross-linking, yielding a similar Ca(2+)-dependency regardless of the presence of the WT-PLB-tether. In contrast, the PLB mutant with the loss-of-function L31A mutation has decreased binding affinity for SERCA2a, thus cross-linking weakly to the WT-PLB-tethered SERCA2a, and only marginally affected the activity of SER-20G-PLB. Thus, there is a reversible equilibrium between different PLB mutants for binding to E2, in which PLB mutants possessing higher binding affinity for SERCA2a produce more stable E2•PLB and lower the Ca(2+) affinity.
    Journal of Molecular and Cellular Cardiology 11/2014; 76. DOI:10.1016/j.yjmcc.2014.08.020
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    ABSTRACT: The miR-126-3p/5p pair promotes endothelial regeneration to limit atherosclerosis.•A miR-342-5p and miR-155 tandem regulates macrophage inflammation through ceRNAs.•Lipoprotein/microvesicle-based miR delivery systems provide new therapeutic options.
    Journal of Molecular and Cellular Cardiology 11/2014; DOI:10.1016/j.yjmcc.2014.10.021
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    ABSTRACT: ATP-sensitive potassium (KATP) channels are abundantly expressed in the myocardium. Although a definitive role for the channel remains elusive they have been implicated in the phenomenon of cardioprotection, but the precise mechanism is unclear. We set out to test the hypothesis that the channel protects by opening early during ischemia to shorten action potential duration and reduce electrical excitability thus sparing intracellular ATP. This could reduce reperfusion injury by improving calcium homeostasis. Using a combination of contractile function analysis, calcium fluorescence imaging and patch clamp electrophysiology in cardiomyocytes isolated from adult male Wistar rats, we demonstrated that the opening of sarcolemmal KATP channels was markedly delayed after cardioprotective treatments: ischemic preconditioning, adenosine and PMA. This was due to the preservation of intracellular ATP for longer during simulated ischemia therefore maintaining sarcolemmal KATP channels in the closed state for longer. As the simulated ischemia progressed, KATP channels opened to cause contractile, calcium transient and action potential failure; however there was no indication of any channel activity early during simulated ischemia to impart an energy sparing hyperpolarization or action potential shortening. We present compelling evidence to demonstrate that an early opening of sarcolemmal KATP channels during simulated ischemia is not part of the protective mechanism imparted by ischemic preconditioning or other PKC-dependent cardioprotective stimuli. On the contrary, channel opening was actually delayed. We conclude that sarcolemmal KATP channel opening is a consequence of ATP depletion, not a primary mechanism of ATP preservation in these cells.
    Journal of Molecular and Cellular Cardiology 11/2014; 79. DOI:10.1016/j.yjmcc.2014.10.016
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    ABSTRACT: Calcium is of critical importance to mitochondrial and cell function, and calcium signaling is highly localized in the cell. When stimulated, mitochondria are capable of rapidly taking up calcium, affecting both matrix energetics within mitochondria and shaping the amplitude and frequency of cytosolic calcium “waves”. During pathological conditions a large increase in mitochondrial calcium levels is thought to activate the mitochondrial permeability transition pore, resulting in cell death. The protein responsible for mitochondrial calcium uptake, the mitochondrial calcium uniporter (MCU), was identified in 2011 and its molecular elucidation has stimulated and invigorated research in this area. MCU knockout mice have been created, a variety of other regulators have been identified, and a disease phenotype in humans has been attributed to the loss of a uniporter regulator. In the three years since its molecular elucidation, further research into the MCU has revealed a complex uniporter, and raised many questions about its physiologic and pathologic cell roles. This article is part of a Special Issue entitled "Mitochondria: From Basic Mitochondrial Biology to Cardiovascular Disease".
    Journal of Molecular and Cellular Cardiology 11/2014; 78. DOI:10.1016/j.yjmcc.2014.10.013