Journal of Neurochemistry

Cover image for Vol. 132 Issue 3

Edited By: Jörg Schulz

Impact Factor: 4.244

ISI Journal Citation Reports © Ranking: 2013: 63/252 (Neurosciences); 74/291 (Biochemistry & Molecular Biology)

Online ISSN: 1471-4159

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Recently Published Articles

  1. Systemically administered neuregulin-1β1 rescues nigral dopaminergic neurons via the ErbB4 receptor tyrosine kinase in MPTP mouse models of Parkinson's disease

    Candan Depboylu, Thomas W. Rösler, Anderson de Andrade, Wolfgang H. Oertel and Günter U. Höglinger

    Article first published online: 26 JAN 2015 | DOI: 10.1111/jnc.13026

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    Previously, we demonstrated that systemically administered neuregulin-1β1 (Nrg1β1) passes the blood-brain barrier, phosphorylates ErbB4 receptors and elevates dopamine (DA) levels in the nigrostriatal system of healthy mice. Nrg1β1 protects nigral DAergic neurons in the 6-hydroxydopamine (6-OHDA) mouse model of Parkinson's disease (PD). Here, we show that Nrg1β1 rescues nigral DAergic neurons also against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced cell death. ErbB4 expression is essential for the neuroprotective effect of Nrg1β1 on midbrain DAergic neurons. Nrg1β1 might be beneficial in PD treatment.

  2. Dopamine transporter oligomerization: impact of combining protomers with differential cocaine analog binding affinities

    Juan Zhen, Tamara Antonio, Shu-Yuan Cheng, Solav Ali, Kymry T. Jones and Maarten E. A. Reith

    Article first published online: 26 JAN 2015 | DOI: 10.1111/jnc.13025

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    The dopamine transporter (DAT) can exist as an oligomer but it is unknown whether the protomers function independently. The present results indicate that protomers that are superpotent or deficient in cocaine analog binding can confer enhanced or reduced potency to the oligomer, respectively. In this respect, positive or negative cooperativity is revealed in the DAT oligomer.

  3. Substantially elevating the levels of αB-crystallin in spinal motor neurons of mutant SOD1 mice does not significantly delay paralysis or attenuate mutant protein aggregation

    Guilian Xu, Susan Fromholt, Jacob I. Ayers, Hilda Brown, Zoe Siemienski, Keith W. Crosby, Christopher A. Mayer, Christopher Janus and David R. Borchelt

    Article first published online: 26 JAN 2015 | DOI: 10.1111/jnc.13022

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    Enhancing the protein chaperone function may present a therapeutic approach to amyotrophic lateral sclerosis caused by mutations in SOD1, and other neurodegenerative disorders characterized by cytosolic protein aggregation. Previous studies in cell models suggested that the chaperone known as αB-crystallin (αB-crys) can prevent mutant SOD1 aggregation. We report that transgenic expression of αB-crys at > 6-fold the normal level in spinal cords of mice expressing mutant SOD1 produces no therapeutic benefit.

  4. Side-chain interactions in the regulatory domain of human glutamate dehydrogenase determine basal activity and regulation

    Vasileios Mastorodemos, Konstantinos Kanavouras, Shobana Sundaram, Maria Providaki, Zoe Petraki, Michael Kokkinidis, Ioannis Zaganas, Diomedes E. Logothetis and Andreas Plaitakis

    Article first published online: 26 JAN 2015 | DOI: 10.1111/jnc.13019

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    Glutamate dehydrogenase (GDH) is central to the metabolism of the excitatory transmitter glutamate, and links it with carbohydrate metabolism in energy homeostasis and cell signaling. The isoform hGDH2, in contrast to hGDH1, is dissociated from GTP (guanosine triphosphate) control, has a reduced basal activity, but remains highly responsive to ADP/L-leucine activation. Substitution of Serine (Ser) for arginine (Arg443) in hGDH1 diminishes basal activity (< 2% of capacity) and abrogates L-leucine activation. We provide evidence that side-chain interactions between 409 and 443 positions in the regulatory domain of GDH are crucial for basal catalytic activity, allosteric regulation, and relative resistance to thermal inactivation.

  5. A novel DYRK1A (Dual specificity tyrosine phosphorylation-regulated kinase 1A) inhibitor for the treatment of Alzheimer's disease: effect on Tau and amyloid pathologies in vitro

    Séverine Coutadeur, Hélène Benyamine, Laurence Delalonde, Catherine de Oliveira, Bertrand Leblond, Alicia Foucourt, Thierry Besson, Anne-Sophie Casagrande, Thierry Taverne, Angélique Girard, Matthew P. Pando and Laurent Désiré

    Article first published online: 26 JAN 2015 | DOI: 10.1111/jnc.13018

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    Inhibition of the dual specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A) is a new high-potential therapeutic approach for Alzheimer disease. Here we describe EHT 5372, a novel potent and selective DYRK1A inhibitor. EHT 5372 inhibits DYRK1A-induced Tau phosphorylation, Aβ production and Aβ effects on phospho-Tau, including Tau aggregation.