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Marie-Françoise Simon

Researcher at French Institute of Health and Medical Research

Publications -  37
Citations -  2207

Marie-Françoise Simon is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Lysophosphatidic acid & Phospholipase A2. The author has an hindex of 22, co-authored 37 publications receiving 2154 citations. Previous affiliations of Marie-Françoise Simon include Paul Sabatier University.

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Journal ArticleDOI

Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from activated cells

TL;DR: It is concluded that upon loss of phospholipid asymmetry, cell-derived microvesicles provide a preferential substrate for sPLA2, and the novel lipid mediator LPA can be generated by this pathway.
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Lysophosphatidic acid synthesis and release.

TL;DR: The different physio-pathological situations associated with LPA production, as well as the potential role played by LPA in genesis of certain diseases (cancer, obesity, arteriosclerosis) are listed and analyzed.
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Lysophosphatidic acid as a phospholipid mediator: pathways of synthesis

TL;DR: A survey of literature data indicates some interesting issues which might be used as the basis for further molecular characterization of phospholipases A able to degrade phosphatidic acid.
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Phosphatidic and lysophosphatidic acid production in phospholipase C-and thrombin-treated platelets. Possible involvement of a platelet lipase.

TL;DR: A mechanism for phosph atidic and lysophosphatidic acid production is proposed, involving a phosphorylation of the di- and monoglycerides formed upon phospholipase C and lipase action, and the possible role of such a pathway in regulating arachidonic acid release from phospholIPids during platelet activation is discussed.
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Lysophosphatidic acid-induced Ca2+ mobilization in human A431 cells: structure-activity analysis.

TL;DR: The results indicate that, although many features of the LPA structure are important for optimal activity, the phosphate group is most critical, suggesting that this moiety is directly involved in receptor activation.