1. Academic Validation
  2. Cloning and characterization of the human galanin GALR2 receptor

Cloning and characterization of the human galanin GALR2 receptor

  • Peptides. 1998;19(10):1771-81. doi: 10.1016/s0196-9781(98)00133-8.
B Borowsky 1 M W Walker L Y Huang K A Jones K E Smith J Bard T A Branchek C Gerald
Affiliations

Affiliation

  • 1 Department of Molecular Biology, Synaptic Pharmaceutical Corporation, Paramus, New Jersey 07652, USA. bborowsky@synapticcorp.com
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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