http://purl.uniprot.org/citations/25375133 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/25375133 | http://www.w3.org/2000/01/rdf-schema#comment | "Niacin has been demonstrated to activate a PI3K/Akt signaling cascade to prevent brain damage after stroke and UV-induced skin damage; however, the underlying molecular mechanisms for HCA2-induced Akt activation remain to be elucidated. Using CHO-K1 cells stably expressing HCA2 and A431 cells, a human epidermoid cell line with high levels of endogenous expression of functional HCA2 receptors, we first demonstrated that niacin induced a robust Akt phosphorylation at both Thr308 and Ser473 in a time-dependent fashion, with a maximal activation at 5 min and a subsequent reduction to baseline by 30 min through HCA2, and that the activation was significantly blocked by pertussis toxin. The HCA2-mediated activation of Akt was also significantly inhibited by the PKC inhibitors GF109203x and Go6983 in both cell lines, by the PDGFR-selective inhibitor tyrphostin A9 in CHO-HCA2 cells and by the MMP inhibitor GM6001 and EGFR-specific inhibitor AG1478 in A431 cells. These results suggest that the PKC pathway and PDGFR/EGFR transactivation pathway play important roles in HCA2-mediated Akt activation. Further investigation indicated that PI3K and the Gβγ subunit were likely to play an essential role in HCA2-induced Akt activation. Moreover, Immunobloting analyses using an antibody that recognizes p70S6K1 phosphorylated at Thr389 showed that niacin evoked p70S6K1 activation via the PI3K/Akt pathway. The results of our study provide new insight into the signaling pathways involved in HCA2 activation."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0112310"xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Lu J."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Li G."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Sun H."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Shi Y."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Zhang W."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Yu Y."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Zhou Q."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Zhou N."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/author | "Offermanns S."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/pages | "e112310"xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/title | "Niacin activates the PI3K/Akt cascade via PKC- and EGFR-transactivation-dependent pathways through hydroxyl-carboxylic acid receptor 2."xsd:string |
http://purl.uniprot.org/citations/25375133 | http://purl.uniprot.org/core/volume | "9"xsd:string |
http://purl.uniprot.org/citations/25375133 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25375133 |
http://purl.uniprot.org/citations/25375133 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25375133 |
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