Cloning and characterization of the human galanin GALR2 receptor |
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Authors: | B Borowsky MW Walker LY Huang KA Jones KE Smith J Bard TA Branchek C Gerald |
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Affiliation: | Department of Molecular Biology, Synaptic Pharmaceutical Corporation, Paramus, New Jersey 07652, USA. bborowsky@synapticcorp.com |
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Abstract: | We present the molecular cloning and characterization of the human galanin receptor, hGALR2. hGALR2 shares 85%, 39%, and 57% amino acid identities to rGALR2, hGALR1, and hGALR3, respectively. hGALR2, along with rGALR2, can be distinguished from the other cloned galanin receptors by a tolerance for both N-terminal extension and C-terminal deletion of galanin, as well as by a primary signaling mechanism involving phosphatidyl inositol hydrolysis and calcium mobilization. By RT-PCR, GALR2 mRNA was abundant in human hippocampus, hypothalamus, heart, kidney, liver, and small intestine. A weak GALR2 mRNA signal was detected in human retina, and no signal was detected in cerebral cortex, lung, spleen, stomach, or pituitary. |
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