| pubmed-article:2998337 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0338106 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0042395 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0282639 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C1510779 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2998337 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:2998337 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2998337 | pubmed:dateCreated | 1985-12-4 | lld:pubmed |
| pubmed-article:2998337 | pubmed:abstractText | The human colon adenocarcinoma cell line HT-29 in culture exhibits a cyclic AMP production system highly sensitive to vasoactive intestinal peptide (VIP), making HT-29 cells a unique cultured cell system for studying the mechanism of VIP action [Laburthe, Rousset, Boissard, Chevalier, Zweibaum & Rosselin (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 2772-2775]. The quantitative characteristics of VIP receptors in HT-29 cells and their structural requirement and molecular size were studied. 125I-labeled VIP bound in a time-dependent manner to HT-29 cell homogenates. At equilibrium (60 min incubation at 30 degrees C), unlabelled VIP in the 0.01-10 nM concentration range competed with 125I-VIP for binding to cell homogenates. Scatchard analysis of binding data gave a straight line, indicating that VIP bound to a single population of sites with a KD of 0.12 +/- 0.02 nM and a capacity of 120 +/- 9 fmol/mg of protein. The structural requirement of these receptors was studied with peptides structurally related to VIP, either natural or synthetic. Several peptides inhibited 125I-VIP binding to HT-29 cell homogenates with the following order of potency, which is typical of the human VIP receptor: VIP (IC50 = 0.1 nM) greater than VIP-(2-28)-peptide (IC50 = 13 nM) greater than human growth hormone releasing factor (IC50 = 56 nM) greater than peptide histidine isoleucine amide (IC50 = 80 nM) greater than secretin (IC50 greater than 10 000 nM). To characterize the molecular component(s) of the VIP receptor in HT-29 cells, 125I-VIP was covalently bound to cell homogenates by using the cross-linker dithiobis(succinimidyl propionate). Sodium dodecyl sulphate/polyacrylamide-gel autoradiographic studies of affinity-labelled cell homogenates revealed two major bands, corresponding to 125I-VIP-protein complexes of Mr 66 000 and 16 000. The labelling of the Mr-66 000 component was specific, since it was abolished by native VIP, whereas that of the Mr-16 000 component was not. Densitometric scanning of autoradiographs indicated that the labelling of the Mr-66 000 complex was inhibited by low VIP concentrations in the 0.1-10 nM range (IC50 = 0.6 nM), but was unaffected by 1 microM-glucagon or octapeptide of cholecystokinin. It was also decreased by VIP-(2-28)-peptide with a potency 1% that of VIP. Assuming that one molecule of 125I-VIP bound per molecule of protein, one protein of Mr 63 000 was identified as a component of the VIP receptor in HT-29 cells. | lld:pubmed |
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| pubmed-article:2998337 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2998337 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2998337 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2998337 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2998337 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2998337 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2998337 | pubmed:author | pubmed-author:LaburtheMM | lld:pubmed |
| pubmed-article:2998337 | pubmed:author | pubmed-author:RoussetMM | lld:pubmed |
| pubmed-article:2998337 | pubmed:author | pubmed-author:CouvineauAA | lld:pubmed |
| pubmed-article:2998337 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2998337 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2998337 | pubmed:volume | 231 | lld:pubmed |
| pubmed-article:2998337 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2998337 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2998337 | pubmed:pagination | 139-43 | lld:pubmed |
| pubmed-article:2998337 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2998337 | pubmed:meshHeading | pubmed-meshheading:2998337-... | lld:pubmed |
| pubmed-article:2998337 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2998337 | pubmed:articleTitle | Molecular identification and structural requirement of vasoactive intestinal peptide (VIP) receptors in the human colon adenocarcinoma cell line, HT-29. | lld:pubmed |
| pubmed-article:2998337 | pubmed:publicationType | Journal Article | lld:pubmed |
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