| pubmed-article:12970090 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C0296735 | lld:lifeskim |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C1419255 | lld:lifeskim |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C1419256 | lld:lifeskim |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C0054454 | lld:lifeskim |
| pubmed-article:12970090 | lifeskim:mentions | umls-concept:C0913331 | lld:lifeskim |
| pubmed-article:12970090 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12970090 | pubmed:dateCreated | 2003-10-2 | lld:pubmed |
| pubmed-article:12970090 | pubmed:abstractText | Adrenomedullin (AM) has two known receptors formed by the calcitonin receptor-like receptor (CL) and receptor activity-modifying protein (RAMP) 2 or 3: we report the effects of the antagonist fragments of human AM and CGRP (AM22-52 and CGRP8-37) in inhibiting AM at human (h), rat (r) and mixed species CL/RAMP2 and CL/RAMP3 receptors transiently expressed in Cos 7 cells or endogenously expressed as rCL/rRAMP2 complexes by Rat 2 and L6 cells. AM22-52 (10 microM) antagonised AM at all CL/RAMP2 complexes (apparent pA2 values: 7.34+/-0.14 (hCL/hRAMP2), 7.28+/-0.06 (Rat 2), 7.00+/-0.05 (L6), 6.25+/-0.17 (rCL/hRAMP2)). CGRP8-37 (10 microM) resembled AM22-52 except on the rCL/hRAMP2 complex, where it did not antagonise AM (apparent pA2 values: 7.04+/-0.13 (hCL/hRAMP2), 6.72+/-0.06 (Rat2), 7.03+/-0.12 (L6)). On CL/RAMP3 receptors, 10 microM CGRP8-37 was an effective antagonist at all combinations (apparent pA2 values: 6.96+/-0.08 (hCL/hRAMP3), 6.18+/-0.18 (rCL/rRAMP3), 6.48+/-0.20 (rCL/hRAMP3)). However, 10 microM AM22-52 only antagonised AM at the hCL/hRAMP3 receptor (apparent pA2 6.73+/-0.14). BIBN4096BS (10 microM) did not antagonise AM at any of the receptors. Where investigated (all-rat and rat/human combinations), the agonist potency order on the CL/RAMP3 receptor was AM approximately betaCGRP>alphaCGRP. rRAMP3 showed three apparent polymorphisms, none of which altered its coding sequence. This study shows that on CL/RAMP complexes, AM22-52 has significant selectivity for the CL/RAMP2 combination over the CL/RAMP3 combination. On the mixed species receptor, CGRP8-37 showed the opposite selectivity. Thus, depending on the species, it is possible to discriminate pharmacologically between CL/RAMP2 and CL/RAMP3 AM receptors. | lld:pubmed |
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| pubmed-article:12970090 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12970090 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12970090 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12970090 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12970090 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12970090 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12970090 | pubmed:issn | 0007-1188 | lld:pubmed |
| pubmed-article:12970090 | pubmed:author | pubmed-author:SchindlerMM | lld:pubmed |
| pubmed-article:12970090 | pubmed:author | pubmed-author:SmithD MDM | lld:pubmed |
| pubmed-article:12970090 | pubmed:author | pubmed-author:LIUT TTT | lld:pubmed |
| pubmed-article:12970090 | pubmed:author | pubmed-author:HowittS GSG | lld:pubmed |
| pubmed-article:12970090 | pubmed:author | pubmed-author:PoynerD RDR | lld:pubmed |
| pubmed-article:12970090 | pubmed:author | pubmed-author:ConnerA CAC | lld:pubmed |
| pubmed-article:12970090 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12970090 | pubmed:volume | 140 | lld:pubmed |
| pubmed-article:12970090 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12970090 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12970090 | pubmed:pagination | 477-86 | lld:pubmed |
