Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 108-119 |
| Number of pages | 12 |
| Journal | Annals of the New York Academy of Sciences |
| Volume | 863 |
| DOIs | |
| State | Published - Dec 1 1998 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Cloning and evaluation of the role of rat GALR-2, a novel subtype of galanin receptor, in the control of pain perception. / Ahmad, Sultan; O'Donnell, Dajan; Payza, Kem; Ducharme, Julie; Ménard, Daniel; Brown, William; Schmidt, Ralf; Wahlestedt, Claes R; Shen, S. H.; Walker, Philippe.
In: Annals of the New York Academy of Sciences, Vol. 863, 01.12.1998, p. 108-119.Research output: Contribution to journal › Article
}
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 R
AU - Shen, S. H.
AU - Walker, Philippe
PY - 1998/12/1
Y1 - 1998/12/1
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.
UR - http://www.scopus.com/inward/record.url?scp=0032430274&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032430274&partnerID=8YFLogxK
U2 - 10.1111/j.1749-6632.1998.tb10688.x
DO - 10.1111/j.1749-6632.1998.tb10688.x
M3 - Article
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 -