Source:http://linkedlifedata.com/resource/pubmed/id/18810483
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-12-23
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pubmed:abstractText |
Intraganglionic laminar endings (IGLEs) represent the major vagal afferent terminals throughout the gut. Electrophysiological experiments revealed a modulatory role of ATP in the IGLE-mechanotransduction process and the P2X(2)-receptor has been described in IGLEs of mouse, rat and guinea pig. Another purinoceptor, the P2X(3)-receptor, was found in IGLEs of the rat esophagus. These findings prompted us to investigate occurrence and distribution of the P2X(3)-receptor in the mouse esophagus. Using multichannel immunofluorescence and confocal microscopy, P2X(3)-immunoreactivity (-iry) was found colocalized with the vesicular glutamate transporter 2 (VGLUT2), a specific marker for IGLEs, on average in three-fourths of esophageal IGLEs. The distribution of P2X(3) immunoreactive (-ir) IGLEs was similar to that of P2X(2)-iry and showed increasing numbers towards the abdominal esophagus. P2X(3)/P2X(2)-colocalization within IGLEs suggested the occurrence of heteromeric P2X(2/3) receptors. In contrast to the rat, where only a few P2X(3)-ir perikarya were described, P2X(3) stained perikarya in ~80% of myenteric ganglia in the mouse. Detailed analysis revealed P2X(3)-iry in subpopulations of nitrergic (nNOS) and cholinergic (ChAT) myenteric neurons and ganglionic neuropil of the mouse esophagus. We conclude that ATP might act as a neuromodulator in IGLEs via a (P2X(2))-P2X(3) receptor-mediated pathway especially in the abdominal portion of the mouse esophagus.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2X2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2X3,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Glutamate Transport...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1432-119X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
131
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13-27
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18810483-Adenosine Triphosphate,
pubmed-meshheading:18810483-Animals,
pubmed-meshheading:18810483-Esophagus,
pubmed-meshheading:18810483-Ganglia,
pubmed-meshheading:18810483-Immunohistochemistry,
pubmed-meshheading:18810483-Mice,
pubmed-meshheading:18810483-Mice, Inbred C57BL,
pubmed-meshheading:18810483-Receptors, Purinergic P2,
pubmed-meshheading:18810483-Receptors, Purinergic P2X2,
pubmed-meshheading:18810483-Receptors, Purinergic P2X3,
pubmed-meshheading:18810483-Vesicular Glutamate Transport Protein 2
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pubmed:year |
2009
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pubmed:articleTitle |
Distribution of P2X(3) receptor immunoreactivity in myenteric ganglia of the mouse esophagus.
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pubmed:affiliation |
Institut für Anatomie, Lehrstuhl I, Universität Erlangen-Nürnberg, Krankenhausstr. 9, 91054 Erlangen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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