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    Group III metabotropic glutamate receptor activation inhibits Ca2+ influx and nitric oxide synthase activity in bone marrow stromal cells.

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    Authors
    Foreman, Megan A.
    Gu, Yuchun
    Howl, John D.
    Jones, Sarah
    Publicover, Stephen J.
    Issue Date
    2005
    
    Metadata
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    Abstract
    Nitric oxide (NO) is pivotal to bone physiology. In the central nervous system constitutive, Ca(2+)-calmodulin regulated NO synthase activity and glutamate signalling are intimately linked. Since L-glutamate signalling occurs in bone and is implicated in bone regulation, we have investigated the effect of L-glutamate on NO synthase in bone-derived cells. Treatment of marrow stromal cells with L-glutamate reduced basal NO synthase activity by 40%. Imaging showed that L-glutamate caused a rapid, usually localised and slowly-reversible fall in [Ca(2+)](i). This effect was resistant to disruption of intracellular Ca(2+) stores but sensitive to extracellular La(3+) or omission of extracellular Ca(2+), demonstrating that glutamate acts by inhibition of membrane Ca(2+) influx. The only previous description of such an effect of L-glutamate is via activation of the group III receptor, mGluR6, in the retina. Using Western blotting and RT-PCR we detected mGluR6 protein and transcripts in marrow stromal cells. The effects of L-glutamate on NOS activity and [Ca(2+)](i) in marrow stromal cells were abolished by a group III mGluR inhibitor, (S)-2-amino-2-methyl-4-phosphonobutyric acid. Recording of membrane potential showed that, similarly to the effects of retinal mGluR6 activation, L-glutamate induced membrane hyperpolarisation (-16 +/- 2 mV), which was also sensitive to group III mGluR inhibition. L-glutamate had no effect on cAMP levels. We conclude that activation of a group III mGluR in bone marrow stromal cells inhibits a Ca(2+)-permeable plasma membrane channel, reducing [Ca(2+)](i) and suppressing generation of NO. These observations directly link bone L-glutamate signalling to processes central to bone growth and regulation.
    Citation
    Journal of Cellular Physiology, 204(2): 704-713
    Publisher
    Wiley InterScience
    URI
    http://hdl.handle.net/2436/15800
    DOI
    10.1002/jcp.20353
    PubMed ID
    15799084
    Additional Links
    http://www3.interscience.wiley.com/journal/110433685/abstract
    Type
    Journal article
    Language
    en
    Description
    Metadata only
    ISSN
    0021-9541
    ae974a485f413a2113503eed53cd6c53
    10.1002/jcp.20353
    Scopus Count
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    Research Institute in Healthcare Science

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