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Hypothermia-induced tyrosine phosphorylation of SIRPα in the brain
Gunma University, Gunma University Graduate School of Medicine.
Gunma University.
Gunma University.
Gunma University.
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2012 (English)In: Journal of Neurochemistry, ISSN 0022-3042, E-ISSN 1471-4159, Vol. 121, no 6, 891-902 p.Article in journal (Refereed) Published
Abstract [en]

Signal regulatory protein α (SIRPα) is a neuronal membrane protein that undergoes tyrosine phosphorylation in the brain of mice in response to forced swim (FS) stress in cold water, and this response is implicated in regulation of depression-like behavior in the FS test. We now show that subjection of mice to the FS in warm (37°C) water does not induce the tyrosine phosphorylation of SIRPα in the brain. The rectal temperature (T(rec) ) of mice was reduced to 27° to 30°C by performance of the FS for 10 min in cold water, whereas it was not affected by the same treatment in warm water. The level of tyrosine phosphorylation of SIRPα in the brain was increased by administration of ethanol or picrotoxin, starvation, or cooling after anesthesia, all of which also induced hypothermia. Furthermore, the tyrosine phosphorylation of SIRPα in cultured hippocampal neurons was induced by lowering the temperature of the culture medium. CD47, a ligand of SIRPα, as well as Src family kinases or SH2 domain-containing protein phosphatase 2 (Shp2), might be important for the basal and the hypothermia-induced tyrosine phosphorylation of SIRPα. Hypothermia is therefore likely an important determinant of both the behavioral immobility and tyrosine phosphorylation of SIRPα observed in the FS test.

Place, publisher, year, edition, pages
John Wiley & Sons, 2012. Vol. 121, no 6, 891-902 p.
National Category
Neurosciences
Identifiers
URN: urn:nbn:se:umu:diva-54522DOI: 10.1111/j.1471-4159.2012.07748.xISI: 000305063700006PubMedID: 22468987OAI: oai:DiVA.org:umu-54522DiVA: diva2:524090
Available from: 2012-04-27 Created: 2012-04-27 Last updated: 2017-12-07Bibliographically approved

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CiteExportLink to record
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