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  • 1
    Publication Date: 2001-05-08
    Description: Glial cells express a variety of neurotransmitter receptors. Notably, Bergmann glial cells in the cerebellum have Ca2+-permeable alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPARs) assembled without the GluR2 subunit. To elucidate the role of these Ca2+-permeable AMPARs, we converted them into Ca2+-impermeable receptors by adenoviral-mediated delivery of the GluR2 gene. This conversion retracted the glial processes ensheathing synapses on Purkinje cell dendritic spines and retarded the removal of synaptically released glutamate. Furthermore, it caused multiple innervation of Purkinje cells by the climbing fibers. Thus, the glial Ca2+-permeable AMPARs are indispensable for proper structural and functional relations between Bergmann glia and glutamatergic synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iino, M -- Goto, K -- Kakegawa, W -- Okado, H -- Sudo, M -- Ishiuchi, S -- Miwa, A -- Takayasu, Y -- Saito, I -- Tsuzuki, K -- Ozawa, S -- New York, N.Y. -- Science. 2001 May 4;292(5518):926-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gunma University School of Medicine, Maebashi, Gunma 371-8511, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11340205" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Animals ; Astrocytes/cytology/*physiology ; Calcium/*metabolism ; Calcium Signaling ; Excitatory Postsynaptic Potentials ; Genetic Vectors ; Green Fluorescent Proteins ; In Vitro Techniques ; Luminescent Proteins/genetics ; Membrane Potentials ; Patch-Clamp Techniques ; Permeability ; Purkinje Cells/cytology/*physiology ; Rats ; Receptors, AMPA/genetics/*metabolism ; Synapses/metabolism/*physiology ; *Synaptic Transmission ; Transfection ; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid/pharmacology
    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: 1985-06-14
    Description: Eukaryotic microorganisms, as well as higher animals and plants, display many autonomous physiological and biochemical rhythmicities having periods approximating 24 hours. In an attempt to determine the nature of the timing mechanisms that are responsible for these circadian periodicities, two primary operational assumptions were postulated. Both the perturbation of a putative element of a circadian clock within its normal oscillatory range and the direct activation as well as the inhibition of such an element should yield a phase shift of an overt rhythm generated by the underlying oscillator. Results of experiments conducted in the flagellate Euglena suggest that nicotinamide adenine dinucleotide (NAD+), the mitochondrial Ca2+-transport system, Ca2+, calmodulin, NAD+ kinase, and NADP+ phosphatase represent clock "gears" that, in ensemble, might constitute a self-sustained circadian oscillating loop in this and other organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goto, K -- Laval-Martin, D L -- Edmunds, L N Jr -- 2S07RR05736/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1284-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2988128" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; Biological Transport ; Calcium/physiology ; Calmodulin/physiology ; *Circadian Rhythm ; Euglena/*physiology ; Mitochondria/physiology ; NAD/physiology ; NADP/physiology ; Nucleotidases/*physiology ; Oxidation-Reduction ; Phosphotransferases/metabolism ; *Phosphotransferases (Alcohol Group Acceptor)
    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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