Bromoenol lactone promotes cell death by a mechanism involving phosphatidate phosphohydrolase-1 rather than calcium-independent phospholipase A2.

@article{Fuentes2003BromoenolLP,
  title={Bromoenol lactone promotes cell death by a mechanism involving phosphatidate phosphohydrolase-1 rather than calcium-independent phospholipase A2.},
  author={Luc{\'i}a Beatriz Fuentes and Rosana Peir{\'o} P{\'e}rez and M L Nieto and Jes{\'u}s Balsinde and Mar{\'i}a A Balboa},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 45},
  pages={
          44683-90
        }
}
Originally described as a serine protease inhibitor, bromoenol lactone (BEL) has recently been found to potently inhibit Group VI calcium-independent phospholipase A2 (iPLA2). Thus, BEL is widely used to define biological roles of iPLA2 in cells. However, BEL is also known to inhibit another key enzyme of phospholipid metabolism, namely the magnesium-dependent phosphatidate phosphohydrolase-1 (PAP-1). In this work we report that BEL is able to promote apoptosis in a variety of cell lines… CONTINUE READING

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Involvement in Cell Death

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