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 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.
Borowsky
B
B
Department of Molecular Biology, Synaptic Pharmaceutical Corporation, Paramus, New Jersey 07652, USA. bborowsky@synapticcorp.com
Walker
M W
MW
Huang
L Y
LY
Jones
K A
KA
Smith
K E
KE
Bard
J
J
Branchek
T A
TA
Gerald
C
C
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002478:Cells, Cultured; D003001:Cloning, Molecular; D006224:Cricetinae; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009928:Organ Specificity / Q000235:genetics; D011485:Protein Binding; D051381:Rats; D044088:Receptors, Galanin; D018013:Receptors, Neuropeptide / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D013552:Swine
D044088:Receptors, Galanin; D018013:Receptors, Neuropeptide