Effective G-protein coupling of Y2 receptors along axonal fiber tracts and its relevance for epilepsy. (February 2017)
- Record Type:
- Journal Article
- Title:
- Effective G-protein coupling of Y2 receptors along axonal fiber tracts and its relevance for epilepsy. (February 2017)
- Main Title:
- Effective G-protein coupling of Y2 receptors along axonal fiber tracts and its relevance for epilepsy
- Authors:
- Dum, Elisabeth
Fürtinger, Sabine
Gasser, Elisabeth
Bukovac, Anneliese
Drexel, Meinrad
Tasan, Ramon
Sperk, Günther - Abstract:
- Abstract: Neuropeptide Y (NPY)-Y2 receptors are G-protein coupled receptors and, upon activation, induce opening of potassium channels or closing of calcium channels. They are generally presynaptically located. Depending on the neuron in which they are expressed they mediate inhibition of release of NPY and of the neuron's classical transmitter GABA, glutamate or noradrenaline, respectively. Here we provide evidence that Y2 receptor binding is inhibited dose-dependently by GTPγS along Schaffer collaterals, the stria terminalis and the fimbria indicating that Y2 receptors are functionally coupled to G-proteins along these fiber tracts. Double immune fluorescence revealed coexistence of Y2-immunoreactivity with β-tubulin, a marker for axons in the stria terminalis, but not with synaptophysin labeling presynaptic terminals, supporting the localization of Y2 receptors along axonal tracts. After kainic acid-induced seizures in rats, GTPγS-induced inhibition of Y2 receptor binding is facilitated in the Schaffer collaterals but not in the stria terminalis. Our data indicate that Y2 receptors are not only located at nerve terminals but also along fiber tracts and are there functionally coupled to G-proteins. Highlights: NPY-Y2 receptors are expressed along fiber tracts. Y2 specific receptor binding is inhibited by GTPγS. Y2 receptor binding is functionally coupled to G-proteins. Y2 specific receptor binding is enhanced after strong seizures. Y2 binding is more sensitive to GTPγSAbstract: Neuropeptide Y (NPY)-Y2 receptors are G-protein coupled receptors and, upon activation, induce opening of potassium channels or closing of calcium channels. They are generally presynaptically located. Depending on the neuron in which they are expressed they mediate inhibition of release of NPY and of the neuron's classical transmitter GABA, glutamate or noradrenaline, respectively. Here we provide evidence that Y2 receptor binding is inhibited dose-dependently by GTPγS along Schaffer collaterals, the stria terminalis and the fimbria indicating that Y2 receptors are functionally coupled to G-proteins along these fiber tracts. Double immune fluorescence revealed coexistence of Y2-immunoreactivity with β-tubulin, a marker for axons in the stria terminalis, but not with synaptophysin labeling presynaptic terminals, supporting the localization of Y2 receptors along axonal tracts. After kainic acid-induced seizures in rats, GTPγS-induced inhibition of Y2 receptor binding is facilitated in the Schaffer collaterals but not in the stria terminalis. Our data indicate that Y2 receptors are not only located at nerve terminals but also along fiber tracts and are there functionally coupled to G-proteins. Highlights: NPY-Y2 receptors are expressed along fiber tracts. Y2 specific receptor binding is inhibited by GTPγS. Y2 receptor binding is functionally coupled to G-proteins. Y2 specific receptor binding is enhanced after strong seizures. Y2 binding is more sensitive to GTPγS after seizures. … (more)
- Is Part Of:
- Neuropeptides. Volume 61(2017)
- Journal:
- Neuropeptides
- Issue:
- Volume 61(2017)
- Issue Display:
- Volume 61, Issue 2017 (2017)
- Year:
- 2017
- Volume:
- 61
- Issue:
- 2017
- Issue Sort Value:
- 2017-0061-2017-0000
- Page Start:
- 49
- Page End:
- 55
- Publication Date:
- 2017-02
- Subjects:
- NPY -- Y2 receptors -- Schaffer collaterals -- Stria terminalis -- GTPγS -- G-protein coupling -- Kainic acid -- Epilepsy
Neuropeptides -- Periodicals
Neuropeptides
Neuropeptides -- Périodiques
Neuropeptides
Electronic journals
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572.65 - Journal URLs:
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http://firstsearch.oclc.org/journal=0143-4179;screen=info;ECOIP ↗
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http://www.idealibrary.com/cgi-bin/links/toc/npep ↗
http://www.sciencedirect.com/science/journal/01434179 ↗
http://www.clinicalkey.com/dura/browse/journalIssue/01434179 ↗
http://www.clinicalkey.com.au/dura/browse/journalIssue/01434179 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.npep.2016.10.005 ↗
- Languages:
- English
- ISSNs:
- 0143-4179
- Deposit Type:
- Legaldeposit
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