A role of p44/42 mitogen-activated protein kinases in formyl-peptide receptor-mediated phospholipase D activity and oxidant production.

@article{Paruch2006ARO,
  title={A role of p44/42 mitogen-activated protein kinases in formyl-peptide receptor-mediated phospholipase D activity and oxidant production.},
  author={Sylvain Paruch and Jamel El-Benna and Bahia Djerdjouri and Stefano Marullo and Axel P{\'e}rianin},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2006},
  volume={20 1},
  pages={142-4}
}
Phosphatidylcholine-specific phospholipase D (PLD) is a major cellular source of phosphatidic acid and choline, which regulate various physiopathological processes. PLD activation mediated by chemoattractants involves protein phosphorylation. This study provides pharmacological and biochemical evidence of a major role of p44/42 MAP kinases (ERK1/2) in PLD activation induced by the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (fMLP). ERK1/2 inhibition by the MEK1/2 antagonist… CONTINUE READING

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