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Cloning and characterization of the human galanin GALR2 receptor
- Source :
- Peptides. 19:1771-1781
- Publication Year :
- 1998
- Publisher :
- Elsevier BV, 1998.
-
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.
- Subjects :
- Receptors, Neuropeptide
Swine
Physiology
Molecular Sequence Data
Galanin receptor
CHO Cells
Biology
Molecular cloning
Biochemistry
Mice
Cellular and Molecular Neuroscience
Endocrinology
Cricetinae
medicine
Animals
Humans
Amino Acid Sequence
Cloning, Molecular
Galanin
Receptor
Cells, Cultured
G protein-coupled receptor
chemistry.chemical_classification
Messenger RNA
digestive, oral, and skin physiology
Molecular biology
Rats
Amino acid
medicine.anatomical_structure
nervous system
chemistry
Organ Specificity
Cerebral cortex
Receptors, Galanin
Protein Binding
Subjects
Details
- ISSN :
- 01969781
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Peptides
- Accession number :
- edsair.doi.dedup.....247edf96a3c90cbf25ef537d1d4f1282