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The Role of Platelet-Activating Factor in the Biocompatibility of Hemodialysis Membranes

  • C. Tetta
  • N. Haeffner-Cavaillon
  • C. Navino
  • S. David
  • C. Franceschi
  • F. Mariano
  • G. Camussi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 416)

Abstract

Extracorporeal treatments for acute or chronic replacement of organ function still represent a challenge for today’s technology. Activation of fluid phase (complement, coagulation, fibrinolysis) and cellular systems (leukocytes, platelets) is known to occur in hemodialysis (1). Among other biochemical indications of leukocyte activation as a conseguence of blood-surface interactions such as oxygen radicals, release of granulocyte proteinases, monocyte prostaglandin release and cytokine generation, platelet-activating factor (PAF) has drawn interest in various biocompatibility studies (reviewed in 1–5). PAF is a phospholipid mediator of inflammation with different biologic properties relevant for the development of inflammation and septic shock (7–11). PAF may act at concentrations of 10−12M and requires an ether linkage at the sn-1 position of the glycerol backbone, a short acyl chain, usually an acetyl residue, at the sn-2 position, and the polar head group of choline or ethanolamine at the sn-3 position (7–8). However, it has been shown recently that PAF belongs to a family of structurally related phospholipid molecules of biologic origin that shares many physiologic activities (12). PAF is considered a mediator of cell-to-cell communication that may function both as an intracellular and intracellular messenger. PAF is produced after immunologic or nor immunologic challenge by a variety of cells such as monocytes/macrophages, polymorphonuclear neutrophils, basophils and platelets, that may participate in the development of inflammatory reaction (13). In addition, human endothelial cells were found to produce PAF after stimulation by several inflammatory mediators including thrombin, angiotensin II, vasopressin, leukotriene C4 and D4, histamine, bradykinin, elastase, catheprin G, and plastic (14–18). PAF acts in an autocrine and paracrine way through a specific receptor for which a cDNA has been cloned (19,20). The receptor belongs to the family of “serpentine” receptors containing sever a-helical domains that weave in and out plasma membrane and it interacts with a G protein, which activates a phosphatidylinositol-specific phospholipase C (19,20). PAF receptors exist in all cells that are known targets for PAF. Recently, also human cultured endothelial cells have been shown to express PAF receptors (21). PAF promotes the permeability of the EC monolayer leading to cell retraction and formation of intracellular gaps (22). PAF induces in vitro migration of endothelial cells and promotes in vivo angiogenesis by a heparin-dependent mechanism (21). The aim of the present review is to briefly summarize early evidence for a role of PAF in bioincompatibility events and to highlight recent advances and their possible potential practical application in testing polymer biocompatibility.

Keywords

Glyceryl Ether Short Acyl Chain Haemodialysis Membrane Extracorporeal Treatment Spontaneous Adherence 
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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References

  1. 1.
    Churchill DN. Efficiency and biocompatibility of membranes. In Dialysis Membranes: Structure and Predictions, V. Bonomini and Y. Berland, Editors, Contributions To Nephrology 113, 1994, 60–71.Google Scholar
  2. 2.
    Tetta C., David S., Biancone L., Canino F., Cambi V., Camussi G. Role of platelet activating factor in hemodialysis. Kidney Int 1993; 43 (suppl. 39): S154 - S157.Google Scholar
  3. 3.
    Chenoweth DE. Anaphylatoxin formation in extracorporeal circuits. Complement 1986; 3: 162–165.Google Scholar
  4. 4.
    Aljama P. Biocompabilidad. Nefrologia 1990; X (3): 18–22.Google Scholar
  5. 5.
    Kazatchkine MD, Carreno MP. Activation of the complement system at the interface between blood and artificial surfaces. Biomaterials 1988; 9: 30–35.PubMedCrossRefGoogle Scholar
  6. 6.
    Snyder F. Platelet-activating factor and related acetylated lipids as potent biological acting cellular mediators. Am J Physiol 1990; 259: 697.Google Scholar
  7. 7.
    Pinckard R.N., McManus L., Hanahan D.J. Chemistry and biology of acetyl glyceryl ether phosphorylcholine (platelegt-activating factor). Adv lnfflammation Rev 1982; 4: 147.Google Scholar
  8. 8.
    Venable M.E., Zimmerman G.A., McIntyre T.M., Prescott S.M. Platelet-activating factor: a phospholipid autcoid with diverse actions. J Lipid Res 1993; 34: 691.PubMedGoogle Scholar
  9. 9.
    Camussi G., Tetta C., Baglioni C. The role of platelet-activating factor in inflammation. Clin Immun Immunopathol 1990; 57: 331.CrossRefGoogle Scholar
  10. 10.
    Yue T.L., Rabinovici R., Feuerstein G. Platelet-activating factor (PAF), a putative mediator in inflammatory tissue injury. Adv Exp Med Biol 1991; 314: 223.PubMedCrossRefGoogle Scholar
  11. 11.
    McManus L.M., Woodard D.S., Deavers S.I., Pinckard R.N. PAF Molecular heterogeneity: pathobiological implications. Lab Invest 1993; 69: 639.PubMedGoogle Scholar
  12. 12.
    Bratton D., Henson P.M. Cellular origin of PAF. In: Platelet-Activating Factor and human Diseases. P.J. Barnes, C.P. Page, P.M. Henson, eds. Blackwell Scientific Publications, London, 1989, p. 23.Google Scholar
  13. 13.
    Camussi G., Aglietta M., Malavasi F., Tetta C., Piacibello W., Sanavio F., Bussolino F. The release of platelet-activating factor from human endothelial cells in culture. J Immunol 1983; 131: 2397.Google Scholar
  14. 14.
    Prescott S.M., Zimmerman G.A. McIntyre T.M. Human endothelial cells in culture produce platewlet-activating factor (1-alkyl-2-acetyl-sn-glycero-3-phosphocholine) when stimulated with thrombin. Proc Natl Acad Sci USA 1984; 81: 3534.PubMedCrossRefGoogle Scholar
  15. 15.
    McIntyre T.M., Zimmerman G.A., Satoh K., Prescott S.M. Cultured endothelial cells synthesize both platelet-activating factor and prostacyclin in response to histamine, bradykinin, and adenosine triphosphate. J Clin Invest 1985; 76: 271.PubMedCrossRefGoogle Scholar
  16. 16.
    Camussi G., Tetta C., Bussolino F., Baglioni C. Synthesis and release of platelet-activating factor is ihnibited by plasma a1-proteinase inhibitor or ai-antichymotrypsin and is stimulated by proteinases. J Exp Med 1988; 1681: 293.Google Scholar
  17. 17.
    Montrucchio G., Bergerone S., Bussolino F. et al. Streptokinase induces intravascular release of platelet-activating factor in patients with acute myocardial infarction and stimulates its synthesis by cultured human endothelial cells. Circulation 1993; 88: 1476.PubMedCrossRefGoogle Scholar
  18. 18.
    Nakamura M., Honda Z.I., Izumi T. et al. Molecular cloning and expression of platelet-activating factor receptor from human leukocytes. J Biol Chem 1991; 266: 20400.PubMedGoogle Scholar
  19. 19.
    Ye R.D., Prossitz E.R., Zuo A., Cochrane C.G. Characterization of a human cDNA that encodes a functional receptor for platelet-activating factor. Biochem Biophys Res Commun 1991; 180: 105.PubMedCrossRefGoogle Scholar
  20. 20.
    Camussi G., Montrucchio G., Lupia E. et al. Platelet-activating factor directly stimulates in vitro migration of endothelial cells and promotes in vivo angiogenesis by a heparin-dependent mechanism. J Immunol 1995; 154: 6492–6501.PubMedGoogle Scholar
  21. 21.
    Camussi G., Turello E., Bussolino F., Baglioni C. Tumor necrosis factor alters cytoskeletal organization and barrier function of endothelial cells. Int Arch Allergy Appl Immunol 1991; 96: 84.PubMedCrossRefGoogle Scholar
  22. 22.
    Mahiout A., Courtney J.M. Effect of dialyser membranes on extracellular and intracellular granulocyte and monocyte activation in ex vivo pyrogen-free conditions. Biomaterials 1994; 15 (12): 969.PubMedCrossRefGoogle Scholar
  23. 23.
    Haeffner-Cavaillon N., Cavaillon JM., Ciancioni C., Bacle F., Delous S., Kazatchine MD. In vitro induction of interleukin-1 during hemodialysis. Kidney Int 1989; 35: 121–1218.CrossRefGoogle Scholar
  24. 24.
    Tetta C., Segoloni G., Turello E. The production of cytokines in hemodialysis. Blood Purif 1990; 8: 337–346.PubMedCrossRefGoogle Scholar
  25. 25.
    Bingel M., Lonnemann G., Koch KM., Dinarello CA., Shaldon S. Plasma interleukin-1 activity during hemodialysis: the influences of dialysis membranes. Nephron 1988; 50: 273–282.PubMedCrossRefGoogle Scholar
  26. 26.
    Herbelin A., Nguyen AT., Zingraff J., Urena P., Descamps-Latscha B. Influence of uremia and hemodialysis on circulating interleukin-1 and tumor necrosis factor-a. Kidney Int 1990; 37: 116–125.PubMedCrossRefGoogle Scholar
  27. 27.
    Laude M., Haeffner-Cavaillon N., Pusineri C. Induction of interleukin-I production during hemodialysis with non-complement activating high-permeability membrane (Abstr). lymphokine Res 1988; 7: 335.Google Scholar
  28. 28.
    Herbelin A., Urena P., Nguyen AT., Zingraff J., Descamps-Latscha B. Elevated circulating levels of interleukin-6 in patients with chronic renal failure. Kidney Int 1991; 39: 954–960.PubMedCrossRefGoogle Scholar
  29. 29.
    Luger A., Kovanik J., Stummvoll HK., Urbanska A., luger T. Blood-membrane interaction in hemodialysis leads to increased cytokine production. Kidney Int 1987; 32: 84–88.PubMedCrossRefGoogle Scholar
  30. 30.
    Blumenstein M., Schmidt B., Ward RA., Ziegler-Heitbrock HWL., Gurland Hi. Altered interleukin-1 production in patients undergoing hemodialysis. Nephron 1988; 50: 277–281.PubMedCrossRefGoogle Scholar
  31. 31.
    Chollet-Martin S., Stamatakis G., Bailly S., Mery JP., Gougerot-pacidalo MA. Inducation of tumor necrosis factor-a during hemodialysis: influence of the membrane type. Clin Exp Immunol 1991; 83: 329–332.PubMedCrossRefGoogle Scholar
  32. 32.
    Pertosa G., Marfella C., Tarantino EA. et al. Involvement of peripheral blood monocytes in haemodialysis: in-vivo induction of tumor necrosis factor alpha, interleukin-6, and ß,-microglobulin. Nephrol Dial Transplant 1991; 2: 18–23.Google Scholar
  33. 33.
    Schindler R. Lonnemann G., Shaldon S., Koch KM, Dinarello CA. Transcription, not synthesis of interleukin-1 and tumor necrosis factor by complement. Kidney Int 1990; 37: 85–93.Google Scholar
  34. 34.
    David S. Tetta C., Camussi G. et al. Adherence of human monocytes to haemodialysis membranes. Nephrol Dial Transplant 1993; 8: 1223–1227.PubMedGoogle Scholar
  35. 35.
    Tetta C., Tropea F., Camussi G. et al. Adherence of human monocytes to haemodialysis membranes: LFA 1 (CD11a/CD18) CRI (CD35) and CR3 (CDL lb/CDI8) triggering promotes the biosynthesis of platelet-activating factor and adherence. Nephrol Dial Transplant 1995; 10.Google Scholar
  36. 36.
    Lo SK., Detmers PA., Levin SM., Wright SD. Transient adhesion of neutrophils to endothelium. J Exp Med 1989; 169: 1779–1793.PubMedCrossRefGoogle Scholar
  37. 37.
    Wright SD., Rao PE., Van Vorrhis WC. et al. Identification of the C3bi receptor of human monocytes and macrophages by using monoclonal antibodies. Proc Natl Acad Sci Usa 1983; 80: 5699.PubMedCrossRefGoogle Scholar
  38. 38.
    Wright SD., Meyer BC. Phorbal esters cause sequential activation and deactivation of complement receptors on polymorphonuclear leukocytes. J Immunol 1986; 136: 1759.PubMedGoogle Scholar
  39. 39.
    Camussi G. potential role of platelet-activating factor in renal pathophysiology. Kidney Int 1986; 29: 469–475.PubMedCrossRefGoogle Scholar
  40. 40.
    Elstad MR., Parker CJ., Cowley FS. et al. CD11b/CDI8 integrinb and a b-glucan receptors are in concert to induce the synthesis of platelet-activating factor by monocytes. J Immunol 1994; 152: 220–230.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • C. Tetta
    • 1
  • N. Haeffner-Cavaillon
    • 2
  • C. Navino
    • 3
  • S. David
    • 4
  • C. Franceschi
    • 5
  • F. Mariano
    • 6
  • G. Camussi
    • 6
  1. 1.Clinical and Laboratory Research DepartmentBellco S.p.A.Mirandola (MO)Italy
  2. 2.INSERM, U430Hopital BroussaisParis
  3. 3.Civil HospitalNovaraItaly
  4. 4.Chair of NephrologyUniversity of ParmaParmaItaly
  5. 5.Department of Biomedical Sciences Section of General PathologyUniversity of ModenaModenaItaly
  6. 6.Institute of Medicine and Public Health 2nd Faculty of MedicineUniversity of Pavia at VareseVareseItaly

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