| Autor: |
Bloomquist, Brian T., Beauchamp, Michelle R., Zhelnin, Leonid, Brown, Su-Ellen, Gore-Willse, Ann R., Gregor, Paul, Cornfield, Linda J. |
| Zdroj: |
Biochemical and Biophysical Research Communications; February 1998, Vol. 243 Issue: 2 p474-479, 6p |
| Abstrakt: |
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 [125I]galanin to the human GalR2 receptor transiently expressed in COS-7 cells was saturable (Kd= 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 Kivalue 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. |
| Databáze: |
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