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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bennett, Robert G. Simpson, Ronda L. Singh, Sudhir |
| Description | Author Affiliation: Singh S ( From the Medical Research Service, The Department of Veterans Affairs, Nebraska-Western Iowa Health Care System, Omaha, Nebraska 68105 and the Departments of Biochemistry & Molecular Biology, Internal Medicine and Pharmacology & Experimental Neuroscience, University of Nebraska Medical Center, Omaha, Nebraska 68198.); Simpson RL ( From the Medical Research Service, The Department of Veterans Affairs, Nebraska-Western Iowa Health Care System, Omaha, Nebraska 68105 and the Departments of Biochemistry & Molecular Biology, Internal Medicine and Pharmacology & Experimental Neuroscience, University of Nebraska Medical Center, Omaha, Nebraska 68198.); Bennett RG ( From the Medical Research Service, The Department of Veterans Affairs, Nebraska-Western Iowa Health Care System, Omaha, Nebraska 68105 and the Departments of Biochemistry & Molecular Biology, Internal Medicine and Pharmacology & Experimental Neuroscience, University of Nebraska Medical Center, Omaha, Nebraska 68198 rgbennet@unmc.edu.) |
| Abstract | Relaxin activation of its receptor RXFP1 triggers multiple signaling pathways. Previously, we have shown that relaxin activates PPARγ transcriptional activity in a ligand-independent manner, but the mechanism for this effect was unknown. In this study, we examined the signaling pathways of downstream of RXFP1 leading to PPARγ activation. Using cells stably expressing RXFP1, we found that relaxin regulation of PPARγ activity requires accumulation of cAMP and subsequent activation of cAMP-dependent protein kinase (PKA). The activated PKA subsequently phosphorylated cAMP response element-binding protein (CREB) at Ser-133 to activate it directly, as well as indirectly through mitogen activated protein kinase p38 MAPK. Activated CREB was required for relaxin stimulation of PPARγ activity, while there was no evidence for a role of the nitric oxide or ERK MAPK pathways. Relaxin increased the mRNA and protein levels of the coactivator protein PGC1 , and this effect was dependent on PKA, and was completely abrogated by a dominant-negative form of CREB. This mechanism was confirmed in a hepatic stellate cell line stably that endogenously expresses RXFP1. Reduction of PGC1 levels using siRNA diminished the regulation of PPARγ by relaxin. These results suggest that relaxin activates the cAMP/PKA and p38 MAPK pathways to phosphorylate CREB, resulting in increased PGC1 levels. This provides a mechanism for the ligand-independent activation of PPARγ in response to relaxin. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 2 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-01-09 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | PPAR Gamma Biosynthesis Receptors, G-Protein-Coupled Receptors, Peptide Relaxin Metabolism Signal Transduction Genetics Transcription Factors Cell Line Cyclic AMP Response Element-Binding Protein Cyclic AMP-Dependent Protein Kinases Ligands MAP Kinase Signaling System Phosphorylation P38 Mitogen-Activated Protein Kinases Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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