Cloning and characterization of the human galanin GALR2 receptor
Autor: | Christophe P. G. Gerald, Jonathan A. Bard, Kelli E. Smith, Beth Borowsky, Kenneth A. Jones, Ling-Yan Huang, Mary W. Walker, Theresa Branchek |
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Rok vydání: | 1998 |
Předmět: |
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 |
Zdroj: | Peptides. 19:1771-1781 |
ISSN: | 0196-9781 |
DOI: | 10.1016/s0196-9781(98)00133-8 |
Popis: | 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. |
Databáze: | OpenAIRE |
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