Potential role of phospholipase D2 in increasing interleukin-2 production by T-lymphocytes through activation of mitogen-activated protein kinases ERK1/ERK2
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 cellu...
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Published in | Biochimica et biophysica acta Vol. 1781; no. 5; pp. 263 - 269 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier B.V
01.05.2008
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Abstract | 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. |
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AbstractList | 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. 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. |
Author | Coronas, Sophie Malet, Nicole Cariven, Clotilde Record, Michel Chap, Hugues Salles, Jean-Pierre Perret, Bertrand Hamdi, Safouane M. |
Author_xml | – sequence: 1 givenname: Safouane M. surname: Hamdi fullname: Hamdi, Safouane M. email: safouane.hamdi@toulouse.inserm.fr – sequence: 2 givenname: Clotilde surname: Cariven fullname: Cariven, Clotilde – sequence: 3 givenname: Sophie surname: Coronas fullname: Coronas, Sophie – sequence: 4 givenname: Nicole surname: Malet fullname: Malet, Nicole – sequence: 5 givenname: Hugues surname: Chap fullname: Chap, Hugues – sequence: 6 givenname: Bertrand surname: Perret fullname: Perret, Bertrand – sequence: 7 givenname: Jean-Pierre surname: Salles fullname: Salles, Jean-Pierre – sequence: 8 givenname: Michel surname: Record fullname: Record, Michel |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18423386$$D View this record in MEDLINE/PubMed |
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Keywords | Mitogen-activated protein kinases (MAPK) TCR Interleukin-2 LFA-1 Phospholipase D2 Diacylglycerol IL-2 DAG MAPK PLD2 PA T-lymphocytes PC PAP ERK Phosphatidic acid |
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SubjectTerms | Animals Diacylglycerol Enzyme Activation Humans Interleukin-2 Interleukin-2 - immunology Ionomycin - metabolism Ionophores - metabolism Isoenzymes - genetics Isoenzymes - metabolism Jurkat Cells MAP Kinase Signaling System - physiology Mice Mitogen-Activated Protein Kinase 1 - genetics Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 - genetics Mitogen-Activated Protein Kinase 3 - metabolism Mitogen-activated protein kinases (MAPK) Phosphatidic acid Phospholipase D - genetics Phospholipase D - metabolism Phospholipase D2 ras Proteins - genetics ras Proteins - metabolism T-lymphocytes T-Lymphocytes - cytology T-Lymphocytes - enzymology T-Lymphocytes - immunology Tetradecanoylphorbol Acetate - metabolism |
Title | Potential role of phospholipase D2 in increasing interleukin-2 production by T-lymphocytes through activation of mitogen-activated protein kinases ERK1/ERK2 |
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