| Autor: |
Ling, Maria K., Hotta, Eri, Kilianova, Zuzana, Haitina, Tatjana, Ringholm, Aneta, Johansson, Lisa, Gallo-Payet, Nicole, Takeuchi, Sakae, Schiöth, Helgi B. |
| Předmět: |
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| Zdroj: |
British Journal of Pharmacology; Nov2004, Vol. 143 Issue 5, p626-637, 12p |
| Abstrakt: |
1 Melanocortin (MC) receptors are widely distributed throughout the body of chicken, like in mammals, and participate in a wide range of physiological functions. 2 To clarify the pharmacological impact of ligands acting in the MC system, we expressed the chicken MC1, MC2, MC3, MC4 and MC5 (cMC1–5) receptors in eukaryotic cells and performed comprehensive pharmacological characterization of the potency of endogenous and synthetic melanocortin peptides. 3 Remarkably, the cMC mentors displayed high affinity for ACTH-derived peptides and in general low affinity for α-MSH. It is evident that not only the cMC2 receptor but also the other cMC receptors interact with ACTH-derived peptide through an epitope beyond the sequence of α-MSH. 4 The synthetic ligand MTII was found to be a potent agonist whereas HS024 was a potent antagonist at the cMC4 receptor, indicating that these ligands are suitable for physiological studies in chicken. 5 We also show the presence of prohormone convertase 1 (PC1) and PC2 genes in chicken, and that these peptides are coexpressed with proopiomelanocortin (POMC) in various tissues. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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