Cloning and characterization of the human galanin GALR2 receptor

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 b oth N-terminal extension and C-terminal deletion of galanin, as well as by a primary signaling mechanism involving phosphatidyl inositol hydrolysis an d calcium mobilization. By RT-PCR, GALR2 mRNA was abundant in human hippoca mpus, hypothalamus, heart, kidney, Liver, and small intestine. A weak GALR2 mRNA signal was detected in human retina, and no signal was detected in ce rebral cortex, lung, spleen, stomach, or pituitary.