TY - JOUR
T1 - Cloning and evaluation of the role of rat GALR-2, a novel subtype of galanin receptor, in the control of pain perception
AU - Ahmad, Sultan
AU - O'Donnell, Dajan
AU - Payza, Kem
AU - Ducharme, Julie
AU - Ménard, Daniel
AU - Brown, William
AU - Schmidt, Ralf
AU - Wahlestedt, Claes
AU - Shen, S. H.
AU - Walker, Philippe
N1 - Funding Information:
This research was supported, in part, by the Perinatology Research Branch , Division of Intramural Research , Eunice Kennedy Shriver National Institute of Child Health and Human Development , National Institutes of Health , Department of Health and Human Services .
PY - 1998
Y1 - 1998
N2 - We have identified a novel subtype of galanin receptor (GALR-2) in rat dorsal root ganglia and spinal cord. The open reading frame of GALR-2 is 1116 nucleotides long, encoding a protein of 372 amino acids with a theoretical molecular mass of 40.7 kD. Membranes prepared from stable pools of 293 cells expressing GALR-2, but not wild-type 293 cells, demonstrated high affinity galanin binding sites. Rat galanin and galanin-related peptides M40, C7, M15, and galanin1-16 effectively competed for binding; peptide C7 demonstrated a lower affinity for rGALR-2, and all these peptides were agonists at rGALR-2 when assessed on a microphysiometer. Studies on the expression of GALR-2 in various tissues by Northern and in situ hybridization analyses suggest a low abundance but wide distribution of GALR-2 mRNA, including several discrete areas in brain and spinal cord and a high abundance in the dorsal root ganglia.
AB - We have identified a novel subtype of galanin receptor (GALR-2) in rat dorsal root ganglia and spinal cord. The open reading frame of GALR-2 is 1116 nucleotides long, encoding a protein of 372 amino acids with a theoretical molecular mass of 40.7 kD. Membranes prepared from stable pools of 293 cells expressing GALR-2, but not wild-type 293 cells, demonstrated high affinity galanin binding sites. Rat galanin and galanin-related peptides M40, C7, M15, and galanin1-16 effectively competed for binding; peptide C7 demonstrated a lower affinity for rGALR-2, and all these peptides were agonists at rGALR-2 when assessed on a microphysiometer. Studies on the expression of GALR-2 in various tissues by Northern and in situ hybridization analyses suggest a low abundance but wide distribution of GALR-2 mRNA, including several discrete areas in brain and spinal cord and a high abundance in the dorsal root ganglia.
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U2 - 10.1111/j.1749-6632.1998.tb10688.x
DO - 10.1111/j.1749-6632.1998.tb10688.x
M3 - Article
C2 - 9928164
AN - SCOPUS:0032430274
VL - 863
SP - 108
EP - 119
JO - Annals of the New York Academy of Sciences
JF - Annals of the New York Academy of Sciences
SN - 0077-8923
ER -