Advertisement

Mobilization and Function of Extracellular Phospholipase A2 in Inflammation

  • Jerrold Weiss
  • Grace Wright
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 275)

Abstract

A common characteristic of inflammatory exudates is the accumulation of relatively high concentrations of phospholipase A2 (PLA-2) in the cell-free fluid (1). Because many (by-)products or this enzyme’s action can exert pro-inflammatory effects (e.g. eicosanoid derivatives of arachidonic acid), these observations have prompted considerable speculation about the possible (patho-) physiological role of extracellular PLA-2 in inflammation. These ideas, in turn, have triggered many investigators and pharmaceutical companies alike to search for “specific” inhibitors of PLA-2 that could be applied therapeutically in acute or chronic inflammatory diseases.

Keywords

Ascitic Fluid Inflammatory Exudate Primary Structure Analysis Extracellular Phospholipase Rabbit Peritoneal 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    P. Vadas and W. Pruzanski, Role of extracellular phospholipase A2 in inflammation, Adv. Inflamm. Res. 7:51 (1984).Google Scholar
  2. 2.
    M. Waite, “The Phospholipases,” Plenum Press, New York (1987).CrossRefGoogle Scholar
  3. 3.
    P. Elsbach, J. Weiss, and S. Forst, Determinants of the action of phospholipases on the phospholipids of gram-negative bacteria (E. coli). In: Lipids and Biomembranes: Past, Present and Future. J. Op Den Kamp, B. Roelofsen and K.W.A. Wirtz, eds., pp. 259–286, Elsevier Science Publishers, Amsterdam, The Netherlands (1986).Google Scholar
  4. 4.
    R.M. Kini and H.J. Evans, Structure-function relationships of phospholipases. The anticoagulant region of phospholipase A2 J. Biol. Chem. 262:14402 (1987).Google Scholar
  5. 5.
    P. Elsbach and J. Weiss, Phagocytosis of bacteria and phospholipid degradation, Biochim. Biophys. Acta (Reviews of Biomembranes) 947:29 (1988).PubMedCrossRefGoogle Scholar
  6. 6.
    G. Wright, J. Weiss and P. Elsbach, Role of extracellular and cellular phospholipases in the destruction of E. coli in an inflammatory exudate, Clin Res 36:475A (1988).Google Scholar
  7. 7.
    O. Doi and S. Nojima, Nature of Escherichia coli mutants deficient in detergent-resistant and/or detergent-sensitive phospholipase A, J. Biochem. 80:1247 (1976).PubMedGoogle Scholar
  8. 8.
    P. de Geus, I. van Die, H. Bergmans, J. Tommassen and G.H. de Haas, Molecular cloning of pldA, the structural gene for outer membrane phospholipase of E. coli Kl2, Mol. Gen. Genet. 190:150 (1983).PubMedCrossRefGoogle Scholar
  9. 9.
    J. Weiss, S. Beckerdite-Quagliata and P. Elsbach, Determinants of the action of phospholipases A on the envelope phospholipids of Escherichia coli, J. Biol. Chem. 254:11010 (1979).PubMedGoogle Scholar
  10. 10.
    S. Forst, J. Weiss, and P. Elsbach, The role of phospholipase A2 lysines in phospholipolysis of Escherichia coli killed by a membrane-active neutrophil protein, J. Biol. Chem. 257:14055 (1982).PubMedGoogle Scholar
  11. 11.
    S. Forst, J. Weiss, P. Blackburn, B. Frangione, F. Goni and P. Elsbach, Amino acid sequence of a basic Agkistrodon halys blomhoffii phospholipase A2: Possible role of NH2-terminal lysines in action on phospholipids of Escherichia coli, Biochemistry 25: 4309 (1986).PubMedCrossRefGoogle Scholar
  12. 12.
    M.J. Dufton, D. Eaker and R.C. Hider, Conformational properties of phospholipases A2: Secondary structure prediction, circular dichroism and relative interface hydrophobicity, Eur. J. Biochem. 137:537 (1983).PubMedCrossRefGoogle Scholar
  13. 13.
    R. Renetseder, S. Brunie, B.W. Dijkstra, J. Drenth and P.B. Sigler, A comparison of the crystal structures of phospholipase A2 from bovine pancreas and Crotalus Atrox venom, J. Biol. Chem. 260:11627 (1985).PubMedGoogle Scholar
  14. 14.
    G.E. Schulz and R.H. Schirmer, “Principles of protein structure” Springer-Verlag, New York (1979).CrossRefGoogle Scholar
  15. 15.
    A. Randolph and R.L. Heinrikson, Crotalus atrox phospholipase A2. Amino acid sequence and studies on the function of the NH2-terminal region, J. Biol. Chem.257:2155 (1982).PubMedGoogle Scholar
  16. 16.
    R. Franson, R. Dobrow, J. Weiss, P. Elsbach and W. Weglicki, Isolation and characterization of a phospholipase A2 from an inflammatory exudate, J. Lipid Res. 19:18 (1978).PubMedGoogle Scholar
  17. 17.
    P. Elsbach, J. Weiss, R.C. Franson, S. Beckerdite-Quagliata, A. Schneider and L. Harris, Separation and purification of a potent bactericidal/permeability-lncreasing protein and a closely associated phospholipase A2 from rabbit polymorphonuclear leukocytes, J. Biol. Chem. 254;1l000 (1979:).Google Scholar
  18. 18.
    S. Forst, J. Weiss, P. Elsbach, J.M. Maraganore, I. Reardon and R.L. Heinrikson, Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate, Biochemistry 25:8381 (1986).PubMedCrossRefGoogle Scholar
  19. 19.
    R.L. Heinrikson, E.T. Krueger, and P.S. Keim, Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus adamanteus: A new classification of phospholipase A2 based upon structural determinants, J.Biol. Chem. 252:4913 (1977).PubMedGoogle Scholar
  20. 20.
    H. Mizushima, I. Kudo, K. Horigome, M. Murakami, M. Hayakawa, D.K. Kim, E. Kondo, M. Tomita and K. Inoue, Purification of rabbit platelet secretory phospholipase A2 and its characteristics, J. Biochem. 105:520 (1989).PubMedGoogle Scholar
  21. 21.
    R.M. Kramer, C. Hession, B. Johansen, G. Hayes, P. McGray, E.P. Chow, R. Tizard and R.B. Pepinsky, Structure and properties of a human non-pancreatic phospholipase A2, J. Biol. Chem. 264: 5768 (1989).PubMedGoogle Scholar
  22. 22.
    R. Verger, F. Ferrato, CM. Mansbach and G.Pieroni, A novel intestinal phospholipase A2: Purification and some molecular characteristics, Biochemistry 21:6883 (1982).PubMedCrossRefGoogle Scholar
  23. 23.
    G.C. Wright, C. E. Ooi, J. Weiss and P. Elsbach, Purification of a cellular (granulocyte) and an extracellular (serum) phospholipase A2 that participate in the destruction of Escherichia coli in a rabbit inflammatory exudate, submitted for publication, (1989).Google Scholar
  24. 24.
    G. Wright, J, Weiss, J. Van den Bergh, H. Verheij and P. Elsbach, Genetic engineering of pig pancreas phospholipase A2 to convert an inactive to an active ezyme in the bactericidal/ permeability-increasing protein (BPI)-mediated bacterial phospholipolysis, Clin. Res. 37:444A (1989).Google Scholar
  25. 25.
    D.K. Kim, I. Kudo and K. Inoue, Detection in human platelets of phospholipase A2 activity which preferentially hydrolyzes an arachidonoyl residue, J. Biochem. 104:492 (1988).PubMedGoogle Scholar
  26. 26.
    J.J. Seilhamer, W. Pruzanski, P. Vadas, S. Plant, J.A. Miller, J. Kloss and L.K. Johnson, Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid, J. Biol. Chem. 264:5335 (1989).PubMedGoogle Scholar
  27. 27.
    See reference # 20.Google Scholar
  28. 28.
    C Lanni and E.L. Becker, Release of phospholipase A2 activity from rabbit peritoneal neutrophils by f-Met-Leu-Phe, Am. J. Pathol. 113:90 (1983).PubMedCentralPubMedGoogle Scholar
  29. 29.
    See reference # 23.Google Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Jerrold Weiss
    • 1
  • Grace Wright
    • 1
  1. 1.Departments of Microbiology and MedicineNew York University School of MedicineNYUSA

Personalised recommendations