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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Wendland, Martin Berger, Claudia Forssmann, Wolf-georg Maronde, Erik Kutzleb, Christian Busmann, Annette Meyer, Markus Seiler, Petra Lammerich, Hans-peter Eickelmann, Peter |
| Description | Author Affiliation: Lammerich HP ( IPF PharmaCeuticals GmbH, Feodor-Lynen-Strasse 31, 30625 Hannover, Germany.) |
| Abstract | 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. |
| ISSN | 00071188 |
| e-ISSN | 14765381 |
| Journal | British Journal of Pharmacology |
| Issue Number | 8 |
| Volume Number | 138 |
| Language | English |
| Publisher | Wiley Online Library(on behalf of The British Pharmacological Society) |
| Publisher Date | 2003-04-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Hemoglobins Pharmacology Peptide Fragments Receptors, Bombesin Agonists Animals CHO Cells Cell Line Cricetinae Dose-Response Relationship, Drug Metabolism Protein Binding Drug Effects Physiology Biosynthesis Genetics Research Support, Non-U.S. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Pharmacology |
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