| pubmed-article:15466451 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15466451 | lifeskim:mentions | umls-concept:C0008051 | lld:lifeskim |
| pubmed-article:15466451 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:15466451 | lifeskim:mentions | umls-concept:C0254370 | lld:lifeskim |
| pubmed-article:15466451 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
| pubmed-article:15466451 | lifeskim:mentions | umls-concept:C0449560 | lld:lifeskim |
| pubmed-article:15466451 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:15466451 | pubmed:dateCreated | 2004-10-29 | lld:pubmed |
| pubmed-article:15466451 | pubmed:abstractText | 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 receptors displayed high affinity for ACTH-derived peptides and in general low affinity for alpha-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 alpha-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. | lld:pubmed |
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| pubmed-article:15466451 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15466451 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15466451 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15466451 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15466451 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15466451 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15466451 | pubmed:issn | 0007-1188 | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:Gallo-PayetNi... | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:SchiöthHelgi... | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:TakeuchiSakae... | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:RingholmAneta... | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:LingMaria KMK | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:HaitinaTatjan... | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:KilianovaZuza... | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:HottaEriE | lld:pubmed |
| pubmed-article:15466451 | pubmed:author | pubmed-author:JohanssonLisa... | lld:pubmed |
| pubmed-article:15466451 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15466451 | pubmed:volume | 143 | lld:pubmed |
| pubmed-article:15466451 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15466451 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15466451 | pubmed:pagination | 626-37 | lld:pubmed |
| pubmed-article:15466451 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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