1. Cloning and Expression of the Human Galanin Receptor GalR2
- Author
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Brian T. Bloomquist, Ann R. Gore-Willse, Su-Ellen Brown, Leonid Zhelnin, Paul Gregor, Linda J. Cornfield, and Michelle R. Beauchamp
- Subjects
medicine.medical_specialty ,Molecular Sequence Data ,Biophysics ,Galanin ,Galanin receptor ,Peptide hormone ,Biology ,Transfection ,Biochemistry ,Receptors, Gastrointestinal Hormone ,Iodine Radioisotopes ,Internal medicine ,medicine ,Animals ,Humans ,Secretion ,Amino Acid Sequence ,RNA, Messenger ,Cloning, Molecular ,Receptor ,Molecular Biology ,Peptide sequence ,Cloning ,Base Sequence ,Sequence Homology, Amino Acid ,digestive, oral, and skin physiology ,Sequence Analysis, DNA ,Cell Biology ,Molecular biology ,Peptide Fragments ,Endocrinology ,COS Cells ,medicine.symptom ,Receptors, Galanin ,Protein Binding ,Muscle contraction - Abstract
Galanin is a peptide hormone which modulates a wide variety of physiological processes, including secretion, muscle contraction, cognitive function, the reproductive axis, and feeding. Two galanin receptor subtypes, GalR1 and GalR2, have been cloned; however, for GalR2 only the rat sequence has been reported in the literature. Our cloning of human GalR2 reveals its amino acid sequence to be 85% identical to rat GalR2 and 39% identical to human GalR1. Binding of [ 125 I]galanin to the human GalR2 receptor transiently expressed in COS-7 cells was saturable (K d = 0.24 nM ± 0.06 nM) with a receptor density of 383 ± 66 fmol/mg protein. Human galanin(1-30) bound with high affinity to the human GalR2 receptor, with a K i value of 0.86 ± 0.12 nM. With the identification of a second galanin receptor subtype, the specific functions of human galanin receptor subtypes can now begin to be addressed.
- Published
- 1998
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