The Purification of Two Intracellular Phospholipase A2s and the Effects of Phospholipase A2 Activating Protein and Mellitin on Their Activities

  • Marion R. Steiner
  • John S. Bomalaski
  • Mike A. Clark
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)


Inflammatory disease processes are often mediated or modulated by eicosanoids, produced and released by leukocytes, platelets and endothelial cells (for reviews see 1–3). A rate limiting step in eicosanoid biosynthesis is the availability of free arachidonic acid. Increased phospholipase A2 activity is the major mechanism for the release of arachidonic acid for eicosanoid biosynthesis in inflammatory cells (4–17). There appear to be several different modes of regulation of phospholipase A2 activity in response to treatment of cells with different agonists. Stimulation of phospholipase A2 activity may occur in response to an increase in the intracellular Ca+2 concentration (3,4,9,16). Since inhibitors of RNA and protein synthesis inhibit the release of arachidonic acid stimulated by some agonists, new protein synthesis is required for arachidonic acid release mediated by these agonists (7–15). Based on these data, we set out to identify a mammalian phospholipase A2 activating protein whose synthesis is regulated by proinflammatory agents. We have identified such a protein and have termed it PLAP, i.e., phospholipase A2 activating protein (17).


Arachidonic Acid Ammonium Sulfate Arachidonic Acid Release Free Arachidonic Acid Fold Stimulation 
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

  • Marion R. Steiner
    • 1
  • John S. Bomalaski
    • 2
  • Mike A. Clark
    • 3
  1. 1.University of KentuckyLexingtonUSA
  2. 2.University of PennsylvaniaPhiladelphiaUSA
  3. 3.Washington UniversitySt. LouisUSA

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