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Control of cell proliferation via transduction of sPLA 2 ‐I activity and possible PPAR activation at the nuclear level
Author(s) -
Specty O.,
Pageaux J.F.,
Dauça M.,
Lagarde M.,
Laugier C.,
Fayard J.M.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02414-5
Subject(s) - internalization , receptor , cell growth , phospholipase a2 , microbiology and biotechnology , nuclear receptor , cell culture , signal transduction , peroxisome , chemistry , cell , peroxisome proliferator activated receptor , biochemistry , biology , enzyme , transcription factor , gene , genetics
Pancreatic phospholipase A 2 (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.