Cardiovascular Research (CARDIOVASC RES )

Publisher: British Medical Association; British Cardiac Society; European Society of Cardiology, Elsevier

Description

Cardiovascular Research is the International Basic Science Journal of the European Society of Cardiology. The Journal is concerned with both basic and clinical research in the field of cardiovascular physiology and pathophysiology. The Journal welcomes submission of papers both at the molecular, subcellular, cellular, organ and organism level, and of clinically oriented papers offering insight into (patho)physiological mechanisms.

  • Impact factor
    5.94
    Show impact factor history
     
    Impact factor
  • 5-year impact
    6.11
  • Cited half-life
    7.00
  • Immediacy index
    1.69
  • Eigenfactor
    0.05
  • Article influence
    1.93
  • Website
    Cardiovascular Research website
  • Other titles
    Cardiovascular research, CVR
  • ISSN
    0008-6363
  • OCLC
    1553351
  • Material type
    Periodical, Internet resource
  • Document type
    Journal / Magazine / Newspaper, Internet Resource

Publisher details

Elsevier

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Voluntary deposit by author of pre-print allowed on Institutions open scholarly website and pre-print servers
    • Voluntary deposit by author of authors post-print allowed on institutions open scholarly website including Institutional Repository
    • Deposit due to Funding Body, Institutional and Governmental mandate only allowed where separate agreement between repository and publisher exists
    • 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 PMC after 12 months
    • Authors who are required to deposit in subject repositories may also use Sponsorship Option
    • Pre-print can not be deposited for The Lancet
  • Classification
    ​ green

Publications in this journal

  • [show abstract] [hide abstract]
    ABSTRACT: Aim. Nitric oxide (NO) plays a key role in vascular homeostasis and is produced by endothelial NO synthase (eNOS), encoded by NOS3 gene. We previously reported the genetic association between NOS3 rs753482-A>C polymorphism on intron 19 and coronary artery disease (CAD). In the attempt of conferring functional implication to the rs753482-A>C polymorphism, we investigated its influence on transcript maturation. Methods and Results. A transcript variant skipping exons 20-21 is prevalent in carriers of the rs753482-C allele and is translated in a novel truncated form of eNOS. The truncated eNOS displays increased basal NO production, is insensitive to calcium stimulation, and, upon heterodimerization with the full-length eNOS protein, exerts a dominant-negative effect on NO production. CAD patients and healthy subjects carriers of the rs753482-C genotype are characterized by increased NO basal levels in peripheral blood and platelets, and negatively respond to oral glucose load by failing to increase NO synthesis following insulin wave. Furthermore, forearm vasodilation after reactive hyperemia is dramatically impaired in rs753482-C carriers. Conclusions. We demonstrated that subjects carrying the rs753482-C genotype express a novel stable truncated form of eNOS with altered enzymatic activity that influences NO production and endothelial function. These findings open to new intriguing perspectives to several diseases involving vascular response to NO.
    Cardiovascular Research 12/2013; 100(3).
  • [show abstract] [hide abstract]
    ABSTRACT: AIMS: Urotensin-II (UII) is a vasoactive peptide that promotes vascular smooth muscle cells (VSMCs) proliferation and is involved in the pathogenesis of atherosclerosis, restenosis and vascular remodeling. This study aimed to determine the role of calcium (Ca2+)-dependent signaling and alternative signaling pathways in UII-evoked VSMCs proliferation focussing on store-operated Ca2+ entry (SOCE) and epithelium growth factor receptor (EGFR) transactivation. METHODS AND RESULTS: We used primary cultures of VSMCs isolated from wistar rat aorta to investigate the effects of UII on intracellular Ca2+ mobilization, and proliferation determined by 5-bromo-2-deoxyuridine (BrdU) assay. We found that UII enhanced intracellular Ca2+ concentration ([Ca2+]i) which was significantly reduced by classical SOCE inhibitors and by knockdown of essential components of the SOCE such as STIM1, Orai1, or TRPC1. Moreover, UII activated a Gd3+-sensitive current with similar features of the Ca2+ release-activated Ca2+ current (ICRAC). Additionally, UII stimulated VSMCs proliferation and Ca2+/cAMP response element-binding protein (CREB) activation through SOCE pathway that involved STIM1, Orai1, and TRPC1. Co-immunoprecipitation experiments showed that UII promoted the association between Orai1 and STIM1, and between Orai1 and TRPC1. Moreover, we determined that epithelium growth factor receptor (EGFR) transactivation, extracellular signal-regulated kinase (ERK) and Ca2+/calmodulin-dependent kinase (CaMK) signaling pathways were involved in both UII-mediated Ca2+ influx, CREB activation and VSMCs proliferation. CONCLUSION: Our data show for the first time that UII-induced VSMCs proliferation and CREB activation requires a complex signaling pathway that involves on the one hand SOCE mediated by STIM1, Orai1 and TRPC1, and on the other hand EGFR, ERK, and CaMK activation.
    Cardiovascular Research 08/2013;
  • [show abstract] [hide abstract]
    ABSTRACT: Connexins form a family of transmembrane proteins that consists of 20 members in humans and 21 members in mice. Six connexins assemble into a connexon that can function as a hemichannel or connexon that can dock to a connexon expressed by a neighboring cell, thereby forming a gap junction channel. Such intercellular channels synchronize responses in multicellular organisms through direct exchange of ions, small metabolites and other second messenger molecules between the cytoplasms of adjacent cells. Multiple connexins are expressed in the cardiovascular system. These connexins not only experience the different biomechanical forces within this system but may also act as effector proteins in coordinating responses within groups of cells towards these forces. This review discusses recent insights regarding regulation of cardiovascular connexins by mechanical forces and junctions. It specifically addresses effects of i) shear stress on endothelial connexins, ii) hypertension on vascular connexins and iii) changes in afterload and the composition of myocardial mechanical junctions on cardiac connexins.
    Cardiovascular Research 04/2013;
  • [show abstract] [hide abstract]
    ABSTRACT: AIMS: Activation of β(1)-adrenergic receptors and their G proteins, G(s), induces cardiac hypertrophy. However, activation of classic Gα(s)-effectors, adenylyl cyclases (AC) and protein kinase A, is not sufficient for induction of hypertrophy, which suggests the involvement of additional pathway(s) activated by G(s). Recently, we discovered that βγ-subunits of G(q) induce phosphorylation of the extracellular regulated kinases (Erk) 1/2 at threonine188 and thereby induce hypertrophy. Here we investigated whether β-adrenergic receptors might also induce cardiac hypertrophy via Erk(Thr188)phosphorylation.Methods and Resultsβ-adrenergic receptor activation induced Erk(Thr188)-phosphorylation in mouse hearts and in neonatal cardiomyocytes. Inhibition of Erk1/2 or overexpression of Erk(Thr188)phosphorylation-deficient mutants (Erk2(T188A) and Erk2(T188S)) significantly attenuated βadrenergic cardiomyocyte hypertrophy in vitro. Erk-activity was stimulated by both isoproterenol and the direct AC-activator forskolin, but only isoproterenol induced Erk(Thr188)phosphorylation. Erk(Thr188)phosphorylation required Gβγ released from G(s), and was prevented by Gβγ-inhibition. Similarly, isoproterenol but not forskolin induced nuclear accumulation of Erk and cardiomyocyte hypertrophy. Long-term application of isoproterenol in mice caused left ventricular hypertrophy and cardiac remodeling, and this was reduced in mice transgenic for Erk2(T188S), supporting the physiological relevance of Erk(Thr188)-phosphorylation. CONCLUSIONS: Activation of G(s) by β-adrenergic receptors leads to (i) canonical Erk1/2-activation via AC and (ii) release of Gβγ, which then associate with activated Erk1/2 and induce Erk(Thr188)phosphorylation, causing nuclear accumulation of Erk and ultimately cardiomyocyte hypertrophy. These findings reveal a new pathway critically involved in β-adrenergically mediated cardiac hypertrophy, and may yield new therapeutic strategies against hypertrophic remodeling.
    Cardiovascular Research 07/2012;
  • Cardiovascular Research 01/2012; 93(1):S55.
  • Cardiovascular Research 01/2012; 93(1):S8.
  • [show abstract] [hide abstract]
    ABSTRACT: AIMS: Agonists that evoke smooth muscle cell hyperpolarization have the potential to stimulate both local and conducted dilation. We investigated whether the endothelium-dependent vasodilators acetylcholine (ACh) and SLIGRL stimulated conducted dilation and whether this was altered by deficiency in apolipoprotein E (ApoE(-/-)). METHODS AND RESULTS: Isolated mesenteric arteries were cannulated, pressurized, and precontracted with phenylephrine. Agonists were either added to the bath to study local dilation or were restricted to one end of arteries to study conducted dilation. An enhanced sensitivity to both ACh and SLIGRL was observed in mesenteric arteries from ApoE(-/-) mice compared with wild-type controls. Inhibition of nitric oxide (NO) synthase blocked ACh responses, but had no effect on maximum dilation to SLIGRL. SLIGRL increased endothelial cell Ca(2+), hyperpolarized smooth muscle cells, and fully dilated arteries. The NO-independent dilation to SLIGRL was blocked with high [KCl] or Ca(2+)-activated K(+)-channel blockers. The hyperpolarization and dilation to SLIGRL passed through the artery to at least 2.5 mm upstream. The conducted dilation was not affected by a deficit in ApoE and could also be stimulated by ACh, suggesting NO itself could stimulate conducted dilation. CONCLUSION: In small mesenteric arteries of ApoE(-/-) mice, NO-independent dilation is enhanced. Since both NO-dependent and -independent pathways can stimulate local and conducted dilation, the potential for reducing vascular resistance is improved in these vessels.
    Cardiovascular Research 11/2011;

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