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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fehrentz, Jean-alain Martinez, Jean Ryan, Joanne Le Gallic, Lionel Oiry, Catherine Gagne, Didier Mousseaux, Delphine Galleyrand, Jean-claude |
| Description | Author Affiliation: Mousseaux D ( Laboratoire des Aminoacides, Peptides et Protéines (LAPP), CNRS UMR-5810, UMI et UMII, UFR Pharmacie, 15 avenue Charles Flahault, Montpellier 34093, Cedex 5, France.) |
| Abstract | 1. The growth hormone secretagogue receptor 1a (GHSR-1a) is a G-protein coupled receptor, involved in the biological actions of ghrelin by triggering inositol phosphates and calcium intracellular second messengers. It has also been reported that ghrelin could activate the 44- and 42-kDa extracellular signal-regulated protein kinases (ERK1/2) in different cell lines, but it is not clear whether this regulation is GHSR-1a dependent or not. 2. To provide direct evidence for the coupling of GHSR-1a to ERK1/2 activation, this pathway has been studied in a heterologous expression system. 3. Thus, in Chinese hamster ovary (CHO) cells we showed that ghrelin induced, via the human GHSR-1a, a transient and dose-dependent activation of ERK1/2 leading to activation of the transcriptional factor Elk1. 4. We then investigated the precise mechanisms involved in GHSR-1a-mediated ERK1/2 activation using various specific inhibitors and dominant-negative mutants and found that internalization of GHSR-1a was not necessary. Our results also indicate that phospholipase C (PLC) was involved in GHSR-1a-mediated ERK1/2 activation, however, pathways like tyrosine kinases, including Src, and phosphoinositide 3-kinases were not found to be involved. GHSR-1a-mediated ERK1/2 activation was abolished both by a general protein kinase C (PKC) inhibitor, Gö6983, and by PKC depletion using overnight pretreatment with phorbol ester. Moreover, the calcium chelator, BAPTA-AM, and the inhibitor of conventional PKCs, Gö6976, had no effect on the GHSR-1a-mediated ERK1/2 activation, suggesting the involvement of novel PKC isoforms (epsilon, delta), but not conventional or atypical PKCs. Further analyses suggest that PKCepsilon is required for the activation of ERK1/2. 5. Taken together, these data suggest that ghrelin, through GHSR-1a, activates the Elk1 transcriptional factor and ERK1/2 by a PLC- and PKCepsilon-dependent pathway. |
| ISSN | 00071188 |
| e-ISSN | 14765381 |
| Journal | British Journal of Pharmacology |
| Issue Number | 3 |
| Volume Number | 148 |
| Language | English |
| Publisher | Wiley Online Library(on behalf of The British Pharmacological Society) |
| Publisher Date | 2006-06-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Mitogen-Activated Protein Kinase 1 Metabolism Mitogen-Activated Protein Kinase 3 Peptide Hormones Physiology Protein Kinase C-epsilon Receptors, G-Protein-Coupled Animals CHO Cells Cricetinae Ghrelin Receptors, Ghrelin Transfection Type C Phospholipases Ets-Domain Protein Elk-1 Pharmacology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Pharmacology |
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