| pubmed-article:12721098 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12721098 | lifeskim:mentions | umls-concept:C0242299 | lld:lifeskim |
| pubmed-article:12721098 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:12721098 | lifeskim:mentions | umls-concept:C0243192 | lld:lifeskim |
| pubmed-article:12721098 | lifeskim:mentions | umls-concept:C0541284 | lld:lifeskim |
| pubmed-article:12721098 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:12721098 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12721098 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:12721098 | pubmed:dateCreated | 2003-4-30 | lld:pubmed |
| pubmed-article:12721098 | pubmed:abstractText | 1. The human orphan G-protein coupled receptor bombesin receptor subtype 3 (hBRS-3) was screened for peptide ligands by a Ca(2+)mobilization assay resulting in the purification and identification of two specific ligands, the naturally occurring VV-hemorphin-7 (VV-H-7) and LVV-hemorphin-7 (LVV-H-7), from human placental tissue. These peptides were functionally characterized as full agonists with unique specificity albeit low affinity for hBRS-3 compared to other bombesin receptors. 2. VV-H-7 and LVV-H-7 induced a dose-dependent response in hBRS-3 overexpressing CHO cells, as well as in NCI-N417 cells expressing the hBRS-3 endogenously. The affinity of VV-H-7 was higher in NCI-N417 cells compared to overexpressing CHO cells. In detail, the EC(50) values were 45+/-15 microM for VV-H-7 and 183+/-60 microM for LVV-H-7 in CHO cells, and 19+/-6 microM for VV-H-7 and 38+/-18 microM for LVV-H-7 in NCI-N417 cells. Other hemorphins had no effect. Gastrin-releasing peptide (GRP) and neuromedin B (NMB) showed similar EC(50) values of 13-20 microM (GRP) and of 1-2 microM (NMB) on both cell lines. 3. Structure-function analysis revealed that both the N-terminal valine and the C-terminal phenylalanine residues of VV-H-7 are critical for the ligand-receptor interaction. 4. Endogenous hBRS-3 in NCI-N417 activated by VV-H-7 couples to phospholipase C resulting in changes of intracellular calcium, which is initially released from an inositol trisphosphate (IP(3))-sensitive store followed by a capacitive calcium entry from extracellular space. 5. VV-H-7-induced hBRS-3 activation led to phosphorylation of p42/p44-MAP kinase in NCI-N417 cells, but did not stimulate cell proliferation. In contrast, phosphorylation of focal adhesion kinase (p125(FAK)) was not observed. | lld:pubmed |
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| pubmed-article:12721098 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12721098 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12721098 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12721098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12721098 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12721098 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12721098 | pubmed:issn | 0007-1188 | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:ForssmannWolf... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:MeyerMarkusM | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:MarondeErikE | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:BergerClaudia... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:EickelmannPet... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:LammerichHans... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:BusmannAnnett... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:KutzlebChrist... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:WendlandMarti... | lld:pubmed |
| pubmed-article:12721098 | pubmed:author | pubmed-author:SeilerPetraP | lld:pubmed |
| pubmed-article:12721098 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12721098 | pubmed:volume | 138 | lld:pubmed |
| pubmed-article:12721098 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12721098 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12721098 | pubmed:pagination | 1431-40 | lld:pubmed |
| pubmed-article:12721098 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:meshHeading | pubmed-meshheading:12721098... | lld:pubmed |
| pubmed-article:12721098 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12721098 | pubmed:articleTitle | Identification and functional characterization of hemorphins VV-H-7 and LVV-H-7 as low-affinity agonists for the orphan bombesin receptor subtype 3. | lld:pubmed |
| pubmed-article:12721098 | pubmed:affiliation | IPF PharmaCeuticals GmbH, Feodor-Lynen-Strasse 31, 30625 Hannover, Germany. | lld:pubmed |
| pubmed-article:12721098 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12721098 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12721098 | lld:pubmed |
