Phosphorylation and activation of a high molecular weight form of phospholipase A2 by p42 microtubule-associated protein 2 kinase and protein kinase C.

@article{Nemenoff1993PhosphorylationAA,
  title={Phosphorylation and activation of a high molecular weight form of phospholipase A2 by p42 microtubule-associated protein 2 kinase and protein kinase C.},
  author={R. Nemenoff and S. Winitz and N. Qian and V. Van Putten and G. Johnson and L. Heasley},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 3},
  pages={
          1960-4
        }
}
Phospholipase A2 (PLA2) is the enzyme regulating the release of arachidonic acid in most cell types. A high molecular mass, 85-kDa soluble form of PLA2 (cPLA2) has recently been identified, the activity of which is stably increased by stimulation of cells with hormones and growth factors. Growth factor stimulation of cells has been reported to result in increased phosphorylation of cPLA2 on serine residues, but the kinases mediating this effect have not been identified. We report here that… Expand
Regulatory mechanism and physiological role of cytosolic phospholipase A2.
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