| http://purl.uniprot.org/citations/25677823 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25677823 | http://www.w3.org/2000/01/rdf-schema#comment | "QRFP (RFamide) peptides are neuropeptides involved in food intake and adiposity regulation in rodents. We have previously shown that QRFP-43 (43RFa) and QRFP-26 (26RFa) inhibited isoproterenol (ISO)-induced lipolysis in adipocytes. However, the antilipolytic signaling pathways activated by QRFP peptides have not been investigated. In the present study, 3T3-L1 adipocytes were used to identify the main pathways involved in QRFP-43 decreasing ISO-induced lipolysis. Our results show that QRFP-43 reduced ISO-induced phosphorylation of perilipin A (PLIN) and hormone-sensitive lipase (HSL) on Ser660 by 43 and 25%, respectively, but increased Akt phosphorylation by 44%. However, the inhibition of phosphodiesterase 3B (PDE3B), a regulator of lipolysis activated by Akt, did not reverse the antilipolytic effect of QRFP-43. PDE3B inhibition reversed the decrease of Ser660 HSL phosphorylation associated with QRFP-43 antilipolytic effect. QRFP-43 also prevented PKC activation and ISO-induced Src kinases activation leading to the inhibition of the caveolin-1 (CAV-1) translocation on lipid droplets. Indeed, QRFP-43 attenuated phorbol 12-myristate 13-acetate-induced lipolysis and ISO-induced extracellular signal-regulated and Src kinases by 28, 37 and 48%, respectively. The attenuation of ISO-induced lipolysis by QRFP-43 was associated with a decrease of phosphorylated Ser660 HSL, PKA-catalytic (PKA-c) subunit and CAV-1 translocation on lipid droplets by 37, 50 and 46%, respectively. The decrease in ISO-induced CAV-1 and PKA-c translocation was associated with a reduction of PLIN phosphorylation by 44% in QRFP-43-treated adipocytes. These results suggest that QRFP-43 attenuated ISO-induced lipolysis by preventing the formation of an active complex on lipid droplets and the activation of Src kinases and PKC."xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbalip.2015.02.005"xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/author | "Ong H."xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/author | "Granata R."xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/author | "Mulumba M."xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/author | "Marleau S."xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/pages | "657-666"xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/title | "QRFP-43 inhibits lipolysis by preventing ligand-induced complex formation between perilipin A, caveolin-1, the catalytic subunit of protein kinase and hormone-sensitive lipase in 3T3-L1 adipocytes."xsd:string |
| http://purl.uniprot.org/citations/25677823 | http://purl.uniprot.org/core/volume | "1851"xsd:string |
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