| Soluble guanylyl cyclase appears in a specific subset of periglomerular cells in the olfactory bulb. | |
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MedLine Citation:
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PMID: 15813955 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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In the brain, nitric oxide acts as an atypical messenger in cellular nonsynaptic transmission. In the olfactory bulb, this gas is produced at the level of the olfactory glomeruli by a subpopulation of periglomerular cells that participates in the first synaptic relay of the olfactory information between the olfactory nerve and the dendritic tufts of principal cells. It has been proposed that nitric oxide modulates intraglomerular synaptic integration of sensory inputs, but its specific role in the glomerular circuitry remains to be understood. In this article, we demonstrate that, in the glomerular circuits, a specific subset of periglomerular cells, most of them expressing the calcium binding protein calbindin D-28 k, expresses the beta1 subunit of the soluble guanylyl cyclase. These cells could be the targets for the action of nitric oxide at the glomerular level via activation of soluble guanylyl cyclase and production of cGMP. |
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Authors:
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Maria Gutièrrez-Mecinas; Carlos Crespo; José Miguel Blasco-Ibáñez; Francisco Javier Gracia-Llanes; Ana Isabel Marqués-Marí; Francisco José Martínez-Guijarro |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The European journal of neuroscience Volume: 21 ISSN: 0953-816X ISO Abbreviation: Eur. J. Neurosci. Publication Date: 2005 Mar |
Date Detail:
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Created Date: 2005-04-07 Completed Date: 2005-05-27 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 8918110 Medline TA: Eur J Neurosci Country: France |
Other Details:
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Languages: eng Pagination: 1443-8 Citation Subset: IM |
Affiliation:
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Departamento de Biología Celular, Facultad de Ciencias Biológicas, Universidad de Valencia, Street Dr Moliner, 50 E-46100, Burjasot, Spain. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Calcium-Binding Protein, Vitamin D-Dependent / metabolism Female Guanylate Cyclase / metabolism* Microscopy, Immunoelectron / methods Neurons / classification, enzymology*, ultrastructure Nitric Oxide Synthase / metabolism Olfactory Bulb / cytology*, enzymology*, ultrastructure Olfactory Pathways / enzymology Protein Isoforms / metabolism Rats Rats, Wistar Tyrosine 3-Monooxygenase / metabolism gamma-Aminobutyric Acid / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Calcium-Binding Protein, Vitamin D-Dependent; 0/Protein Isoforms; 0/calbindin; 0/calretinin; 56-12-2/gamma-Aminobutyric Acid; EC 1.14.13.39/Nitric Oxide Synthase; EC 1.14.16.2/Tyrosine 3-Monooxygenase; EC 4.6.1.2/Guanylate Cyclase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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