Differential contributions of the two cell surface G‐protein coupled neurotensin (NT) receptors (NTr1 and NTr2) in open field accommodation (839.7)
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چکیده
منابع مشابه
Agonism, inverse agonism, and neutral antagonism at the constitutively active human neurotensin receptor 2.
Two G protein-coupled neurotensin (NT) receptors, termed NTR1 and NTR2, have been identified so far. In contrast to the NTR1, which has been extensively studied, little is known about the pharmacological and biological properties of the NTR2. In the course of characterizing NT analogs that exhibited binding selectivity for the NTR2, we discovered that this receptor constitutively activated inos...
متن کاملRecycling ability of the mouse and the human neurotensin type 2 receptors depends on a single tyrosine residue.
Receptor recycling plays a key role in the modulation of cellular responses to extracellular signals. The purpose of this work was to identify residues in G-protein coupled neurotensin receptors that are directly involved in recycling. Both the high affinity receptor-1 (NTR1) and the levocabastine-sensitive NTR2 are internalized after neurotensin binding. Here, we show that only the mouse NTR2 ...
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چکیده ندارد.
15 صفحه اولIdentification of the receptor subtype involved in the analgesic effect of neurotensin.
The neuropeptide neurotensin (NT) elicits hypothermic and naloxone-insensitive analgesic responses after brain injection. Recent pharmacological evidence obtained with NT agonists and antagonists suggests that these effects are mediated by a receptor distinct from the initially cloned high-affinity NT receptor (NTR1). The recent cloning of a second NT receptor (NTR2) prompted us to evaluate its...
متن کاملPivotal role of an aspartate residue in sodium sensitivity and coupling to G proteins of neurotensin receptors.
The highly conserved aspartate residue in the second transmembrane domain of G protein-coupled receptors is present in position 113 in the type 1 neurotensin receptor (NTR1) but is replaced by an Ala residue in position 79 in the type 2 neurotensin receptor (NTR2). NTR1 couples to Galphaq to stimulate phospholipase C and its binding affinity for neurotensin is decreased by sodium ions and GTP a...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2014
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.28.1_supplement.839.7