Control of cell proliferation via transduction of sPLA(2)-I activity and possible PPAR activation at the nuclear level

Pancreatic phospholipase A2 (PLA(2)-I) stimulates U(III) cells proliferation, a rat uterine cell line, after binding to membrane receptors, internalization and translocation. Here, we demonstrate that during these steps of internalization, PLA(2)-I retains its hydrolytic activity and thus could exer...

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Bibliographic Details
Published in:FEBS letters 2001-02, Vol.490 (1-2), p.88-92
Main Authors: Specty, O, Pageaux, J F, Dauça, M, Lagarde, M, Laugier, C, Fayard, J M
Format: Article
Language:English
Subjects:
Animals
Cell Division
Cell Line
Cell Nucleus - metabolism
Eicosanoids - metabolism
Enzyme Activation
Female
Group II Phospholipases A2
Hydrolysis
Microscopy, Fluorescence
Phospholipases A - metabolism
Phospholipases A2
Phospholipids - metabolism
Rats
Receptors, Cytoplasmic and Nuclear - metabolism
Time Factors
Transcription Factors - metabolism
Transduction, Genetic
Uterus - metabolism
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Summary:Pancreatic phospholipase A2 (PLA(2)-I) stimulates U(III) cells proliferation, a rat uterine cell line, after binding to membrane receptors, internalization and translocation. Here, we demonstrate that during these steps of internalization, PLA(2)-I retains its hydrolytic activity and thus could exert its proliferative effect via nuclear phospholipids hydrolysis. Since fatty acids and eicosanoids released by such activity are known to be ligands of PPAR, we study the expression of these nuclear receptors and demonstrate that, in the experimental conditions where PLA(2)-I stimulates U(III) cells proliferation, PLA(2)-I also regulates PPAR expression indicating a possible mechanism of its proliferative effect.
ISSN:0014-5793
DOI:10.1016/S0014-5793(00)02414-5