http://purl.uniprot.org/citations/18423386 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18423386 | http://www.w3.org/2000/01/rdf-schema#comment | "Hydrolysis of phosphatidylcholine by phospholipase D (PLD) leads to the generation of phosphatidic acid (PA), which is itself a source of diacylglycerol (DAG). These two versatile lipid second messengers are at the centre of a phospholipid signalling network and as such are involved in several cellular functions. However, their role in T-cell activation and functions are still enigmatic. In order to elucidate this role, we generated a human and a murine T-cell line that stably overexpressed the PLD2 isoform. Analysis of the Ras-MAPK pathway upon phorbol myristate acetate (PMA) and ionomycin stimulation revealed that PLD2 promoted an early and sustained increase in ERK1/2 phosphorylation in both cell lines. This response was inhibited by 1-butanol, a well known distracter of PLD activity, or upon overexpression of a dominant negative PLD2, and it was concomitant with a boost of PA/DAG production. As a functional consequence of this PLD2-dependent MAPK activation, interleukin-2 production evoked by PMA/ionomycin stimulation or CD3/CD28 engagement was enhanced in the two T-cell lines overexpressing PLD2. Thus, PLD2 emerged as an early player upstream of the Ras-MAPK-IL-2 pathway in T-cells via PA and DAG production, raising new possibilities of pharmacological manipulation in immune disorders."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbalip.2008.03.005"xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Salles J.P."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Chap H."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Malet N."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Perret B."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Record M."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Coronas S."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Cariven C."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/author | "Hamdi S.M."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/name | "Biochim Biophys Acta"xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/pages | "263-269"xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/title | "Potential role of phospholipase D2 in increasing interleukin-2 production by T-lymphocytes through activation of mitogen-activated protein kinases ERK1/ERK2."xsd:string |
http://purl.uniprot.org/citations/18423386 | http://purl.uniprot.org/core/volume | "1781"xsd:string |
http://purl.uniprot.org/citations/18423386 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18423386 |
http://purl.uniprot.org/citations/18423386 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18423386 |
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