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  • 1
    Publication Date: 1999-01-15
    Description: The mechanism by which psychostimulants act as calming agents in humans with attention-deficit hyperactivity disorder (ADHD) or hyperkinetic disorder is currently unknown. Mice lacking the gene encoding the plasma membrane dopamine transporter (DAT) have elevated dopaminergic tone and are hyperactive. This activity was exacerbated by exposure to a novel environment. Additionally, these mice were impaired in spatial cognitive function, and they showed a decrease in locomotion in response to psychostimulants. This paradoxical calming effect of psychostimulants depended on serotonergic neurotransmission. The parallels between the DAT knockout mice and individuals with ADHD suggest that common mechanisms may underlie some of their behaviors and responses to psychostimulants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gainetdinov, R R -- Wetsel, W C -- Jones, S R -- Levin, E D -- Jaber, M -- Caron, M G -- MH-40159/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1999 Jan 15;283(5400):397-401.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratories, Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9888856" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Attention Deficit Disorder with Hyperactivity/drug ; therapy/physiopathology/psychology ; Behavior, Animal/drug effects ; Carrier Proteins/antagonists & inhibitors/drug effects/genetics/metabolism ; Central Nervous System Stimulants/*pharmacology ; Corpus Striatum/*metabolism ; Dopamine/metabolism/physiology ; Dopamine Plasma Membrane Transport Proteins ; Fluoxetine/pharmacology ; Humans ; Hyperkinesis/*drug therapy/physiopathology/psychology ; Maze Learning ; Membrane Glycoproteins/drug effects/metabolism ; *Membrane Transport Proteins ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Motor Activity/drug effects ; *Nerve Tissue Proteins ; Norepinephrine Plasma Membrane Transport Proteins ; Serotonin/metabolism/*physiology ; Serotonin Plasma Membrane Transport Proteins ; Serotonin Uptake Inhibitors/pharmacology ; *Symporters ; *Synaptic Transmission
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2013-10-08
    Description: Magnetotactic bacteria align along the Earth's magnetic field using an organelle called the magnetosome, a biomineralized magnetite (Fe(II)Fe(III)2O4) or greigite (Fe(II)Fe(III)2S4) crystal embedded in a lipid vesicle. Although the need for both iron(II) and iron(III) is clear, little is known about the biological mechanisms controlling their ratio. Here we present the structure of the magnetosome-associated protein MamP and find that it is built on a unique arrangement of a self-plugged PDZ domain fused to two magnetochrome domains, defining a new class of c-type cytochrome exclusively found in magnetotactic bacteria. Mutational analysis, enzyme kinetics, co-crystallization with iron(II) and an in vitro MamP-assisted magnetite production assay establish MamP as an iron oxidase that contributes to the formation of iron(III) ferrihydrite eventually required for magnetite crystal growth in vivo. These results demonstrate the molecular mechanisms of iron management taking place inside the magnetosome and highlight the role of magnetochrome in iron biomineralization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siponen, Marina I -- Legrand, Pierre -- Widdrat, Marc -- Jones, Stephanie R -- Zhang, Wei-Jia -- Chang, Michelle C Y -- Faivre, Damien -- Arnoux, Pascal -- Pignol, David -- T32 GM066698/GM/NIGMS NIH HHS/ -- England -- Nature. 2013 Oct 31;502(7473):681-4. doi: 10.1038/nature12573. Epub 2013 Oct 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Commissariat a l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Biologie Environnementale et de Biotechnologies,, F-13108, France [2] Centre National de la Recherche Scientifique, Unite Mixte de Recherche Biologie Vegetale et Microbiologie Environnementales, Saint-Paul-lez-Durance, F-13108, France [3] Aix-Marseille Universite, Saint-Paul-lez-Durance, F-13108, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24097349" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*cytology/enzymology/genetics/*metabolism ; Bacterial Proteins/chemistry/genetics/metabolism ; Conserved Sequence ; Ferric Compounds/metabolism ; Ferrosoferric Oxide/*metabolism ; Genes, Bacterial/genetics ; Iron/metabolism ; Magnetosomes/*metabolism ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases/chemistry/genetics/metabolism ; Protein Multimerization ; Protein Structure, Tertiary ; Static Electricity
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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