| pubmed-article:1331759 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1331759 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1331759 | lifeskim:mentions | umls-concept:C0018321 | lld:lifeskim |
| pubmed-article:1331759 | lifeskim:mentions | umls-concept:C0018330 | lld:lifeskim |
| pubmed-article:1331759 | lifeskim:mentions | umls-concept:C0028621 | lld:lifeskim |
| pubmed-article:1331759 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:1331759 | lifeskim:mentions | umls-concept:C0146894 | lld:lifeskim |
| pubmed-article:1331759 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1331759 | pubmed:dateCreated | 1992-12-9 | lld:pubmed |
| pubmed-article:1331759 | pubmed:abstractText | Agonist binding to guanine nucleotide-binding protein (G protein)-coupled receptors in membranes of myeloid differentiated human leukemia (HL-60) cells is inhibited by guanine nucleotides, most potently by the GTP analog guanosine 5'-(gamma-thio)triphosphate (GTP gamma S). In order to study whether GTP gamma S formed locally from adenosine 5'-(gamma-thio)triphosphate (ATP gamma S) and GDP by nucleoside diphosphokinase has any advantage over exogenously added GTP gamma S in binding to and activating G proteins, regulation of complement component 5a (C5a) binding to its receptors, as well as formation of GTP gamma S, was studied in membranes of HL-60 cells. GTP gamma S added to HL-60 membranes potently inhibited binding of 125I-C5a (IC50 about 3 nM), an effect not influenced by addition of either GDP or ATP gamma S. When HL-60 membranes were incubated with the combination of ATP gamma S and GDP, a marked potentiation (up to 300-fold) of the inhibition caused by either GDP or ATP gamma S alone was observed. By measuring nucleoside diphosphokinase-catalyzed formation of GTP gamma S and inhibition of 125I-C5a binding in the presence of GDP and ATP gamma S under identical assay conditions, it was found that formed GTP gamma S inhibited binding of 125I-C5a with an IC50 value of about 0.3 nM, thus being about 10-fold more potent than exogenously added GTP gamma S. These data suggest that the GTP gamma S-forming nucleoside diphosphokinase is closely associated with the C5a receptor-G protein complex and channels the formed GTP gamma S into the G protein. | lld:pubmed |
| pubmed-article:1331759 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1331759 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1331759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1331759 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1331759 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:1331759 | pubmed:issn | 0026-895X | lld:pubmed |
| pubmed-article:1331759 | pubmed:author | pubmed-author:WielandTT | lld:pubmed |
| pubmed-article:1331759 | pubmed:author | pubmed-author:JakobsK HKH | lld:pubmed |
| pubmed-article:1331759 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1331759 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:1331759 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1331759 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1331759 | pubmed:pagination | 731-5 | lld:pubmed |
| pubmed-article:1331759 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:meshHeading | pubmed-meshheading:1331759-... | lld:pubmed |
| pubmed-article:1331759 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1331759 | pubmed:articleTitle | Evidence for nucleoside diphosphokinase-dependent channeling of guanosine 5'-(gamma-thio)triphosphate to guanine nucleotide-binding proteins. | lld:pubmed |
| pubmed-article:1331759 | pubmed:affiliation | Institut für Pharmakologie, Universität GH Essen, FRG. | lld:pubmed |
| pubmed-article:1331759 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1331759 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1331759 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1331759 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1331759 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1331759 | lld:pubmed |
