Source:http://linkedlifedata.com/resource/pubmed/id/17593952
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2007-6-27
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| pubmed:abstractText |
Oxytocin (OT) is one of the neuropituitary hormones and is synthesized in the neurons of the paraventricular nucleus (PVN) and supraoptic nucleus (SON). Previous studies have shown that the mRNAs encoding OT are delivered from the soma to both dendrites and axons of the neurons in the PVN and SON. However, it has not been elucidated whether a translational regulation mechanism to enable local synthesis of the hormone exists in the axons of the neurons of PVN and SON. Elongation factor 2 (EF2) is essential for polypeptide synthesis during protein translation. Moreover, phosphorylation of EF2 by EF2 kinase enhances the translation of certain mRNA species. In the present study, in order to shed light on the mechanisms involved in the translational regulation of OT synthesis, we investigated the localization of phosphorylated EF2. Phospho-EF2 was localized in the soma of the neurons in PVN and SON, and in the swellings of the median eminence where axonal tracts of the neurons in the PVN and SON exist. The phosphorylated form was also observed in the rat hypophysis. Moreover, phospho-EF2 and OT were colocalized in a part of the neurons in the PVN and SON. These results suggest that OT may be partially translated in the axons of neurons in the PVN and SON, and then secreted from the pituitary.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0386-300X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
61
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
161-6
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| pubmed:meshHeading |
pubmed-meshheading:17593952-Animals,
pubmed-meshheading:17593952-Hypothalamus,
pubmed-meshheading:17593952-Immunohistochemistry,
pubmed-meshheading:17593952-Male,
pubmed-meshheading:17593952-Neurons,
pubmed-meshheading:17593952-Oxytocin,
pubmed-meshheading:17593952-Peptide Elongation Factor 2,
pubmed-meshheading:17593952-Phosphorylation,
pubmed-meshheading:17593952-Rats,
pubmed-meshheading:17593952-Rats, Wistar
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| pubmed:year |
2007
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| pubmed:articleTitle |
Colocalization of oxytocin and phosphorylated form of elongation factor 2 in the rat hypothalamus.
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| pubmed:affiliation |
Department of Physiology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8558, Japan.
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| pubmed:publicationType |
Journal Article
|