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Regulation of Plasma Membrane Phospholipase A2 Activity by Phosphorylation/Dephosphorylation: Is Glucocorticoid Action Mediated by Induction of Protein Phosphatase?

  • U. Zor
  • N. Reiss
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)

Summary

Phospholipase A2 (PLA2) is a key enzyme for the liberation of arachidonic acid — the main substrate for eicosanoid production. Regulation of membrane PLA2 activity is a complicated issue, involving second and third messengers, including protein kinases. The main protein kinase responsible for stimulating PLA2 activity may be protein kinase C (PKC), while another serine kinase, cyclic AMP-dependent protein kinase (PKA) switches it off. Glucocorticoids (GC) also inhibit PLA2 activity, via a mechanism that involves induction of protein synthesis. Our hypothesis suggests that at least one of these proteins is a protein phosphatase which reduces the level of phosphorylated PLA2, thereby suppressing its activity.

Keywords

Protein Phosphatase Okadaic Acid PLA2 Activity Include Protein Kinase Phosphoprotein Phosphatase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • U. Zor
    • 1
  • N. Reiss
    • 1
  1. 1.Department of Hormone ResearchThe Weizmann Institute of ScienceRehovotIsrael

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