Structural and Functional Properties of Mammalian Group III Cytosolic Phospholipases A2

  • Margarete Goppelt-Struebe
  • Wolfgang Rehfeldt
Part of the GWUMC Department of Biochemistry Annual Spring Symposia book series (GWUN)


Phospholipases A2, enzymes which hydrolyze the sn-2 fatty acyl ester bond of phosphoglycerides, are found in all mammalian cells and tissues1. They have been subdivided into two groups: group I enzymes are derived from proenzymes and secreted. These extracellular enzymes have been characterized in great detail functionally and structurally, the best known mammalian enzyme being the pancreatic phospholipase A2. Group II enzymes are structurally related to the group I enzymes. They have the same molecular weight of about 12 to 18 kD and show a high degree of sequence homology, but also typical differences such as a lacking cysteine residue in position 11, which is typical for group I enzymes. Group II phospholipases A2 are found intracellularly, often membrane bound, and are secreted upon activation of the cells. Functionally they seem to play an important role in inflammations and other disease states2,3. It has now become evident that there is a third group of calcium-dependent phospholipases A2 distinct from the ones mentioned above. These enzymes are rather labile when purified and therefore not yet well characterized. They have been described in most detail in platelets, mesangial cells, macrophages and monocytic cell lines. The present paper will discuss some of the properties of these group III enzymes (cytosolic phospholipases A2) and will focus on the phospholipase A2 from the monocytic cell line THP1.


Arachidonic Acid U937 Cell THP1 Cell Membrane Association Monocytic Cell Line 
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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • Margarete Goppelt-Struebe
    • 1
  • Wolfgang Rehfeldt
    • 1
  1. 1.Institute of Molecular PharmacologyMedical School HannoverHannover 61Germany

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