| pubmed-article:8383439 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8383439 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8383439 | lifeskim:mentions | umls-concept:C0227263 | lld:lifeskim |
| pubmed-article:8383439 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:8383439 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8383439 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:8383439 | pubmed:issue | 2 Pt 1 | lld:pubmed |
| pubmed-article:8383439 | pubmed:dateCreated | 1993-4-2 | lld:pubmed |
| pubmed-article:8383439 | pubmed:abstractText | Vasoactive intestinal peptide (VIP) receptors were characterized in epithelial plasma membranes from human small intestine. Native VIP inhibited the binding of 125I-labeled VIP to jejunal membranes, and Scatchard analysis of these data was consistent with the existence of one class of receptor with a dissociation constant of 42 pM and a maximal binding of 256 fmol/mg membrane protein. VIP stimulated adenylyl cyclase activity in human jejunal membranes in the 0.01 nM-1 microM range [half-maximal effective dose = 0.7 nM]. Coupling of VIP receptors with a Gs protein was further assessed by the ability of GTP (10(-8) to 10(-3) M) to inhibit 125I-VIP binding to membranes. 125I-VIP binding was seven to eight times higher in villus cells than in crypt cells. Finally, 125I-VIP binding was detectable throughout the small and large intestines with the highest binding in jejunum. Among the natural peptides structurally related to VIP, some inhibited 125I-VIP binding with the following order of potency: VIP = pituitary adenylate cyclase-activating peptide (PACAP)-27 = PACAP-38 > helodermin >> peptide histidine methionineamide = human growth hormone-releasing factor > secretin. The same order of potency of peptides for inhibiting 125I-VIP or 125I-labeled PACAP was observed, supporting that the two tracers bound to a common VIP-PACAP receptor site. This order of potency was also observed for the stimulation of adenylyl cyclase activity by these peptides. 125I-VIP was cross-linked to membranes using disuccinimidyl suberate. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, one single band of 70,000 mol wt was observed.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:8383439 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8383439 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8383439 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8383439 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8383439 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8383439 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:SalomonRR | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:LaburtheMM | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:VoisinTT | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:CouvineauAA | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:DarmoulDD | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:BlaisAA | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:Rouyer-Fessar... | lld:pubmed |
| pubmed-article:8383439 | pubmed:author | pubmed-author:LavalléeDD | lld:pubmed |
| pubmed-article:8383439 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8383439 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:8383439 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8383439 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8383439 | pubmed:pagination | E294-300 | lld:pubmed |
| pubmed-article:8383439 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:8383439 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8383439 | pubmed:articleTitle | Characterization of a common VIP-PACAP receptor in human small intestinal epithelium. | lld:pubmed |
| pubmed-article:8383439 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale, Unité 239, Faculté de Médecine X. Bichat, Paris, France. | lld:pubmed |
| pubmed-article:8383439 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8383439 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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