Selective Inhibition of Polymorphonuclear Leukocyte Oxidative Burst and CD11b/CD16 Expression by Prostaglandin E2

  • J. A. Lieberman
  • J. M. Waldman
  • J. K. Horn


Following injury, prostaglandin E2 (PGE2) is released from stimulated mononuclear cells. Abnormally elevated levels of PGE2 have been measured in supernatants of macrophages obtained from burned mice [1], and in posttraumatic patients PGE2 suppresses interleukin-2 production by T lymphocytes [2]. Human polymorphonuclear leukocytes (PMN) contain on their surface an adhesion glycoprotein, identified as the receptor for C3bi (CR3) [3]. CR3 is a heterodimer composed of a 170-kDa α-chain (CD11b) and an invariant 95-kDa β-chain (CD18). Also contained on the PMN surface are several receptors for the Fc portion of immunoglobulins (FcγR). In particular, the 50 to 70-kDa FcγR III is a low-affinity receptor that binds immune-complexed IgG and has been designated CD16 [4]. Together, these two surface proteins have been used to identify phenotypic subclasses of PMN [5].


Phorbol Myristate Acetate Polymorphonuclear Leukocyte Phorbol Myristate Acetate Human Polymorphonuclear Leukocyte Oxidative Burst Activity 
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  1. 1.
    Miller-Graziano CL, Fink M, Wu JY, Szabo G, Kodys K (1988) Mechanisms of altered monocyte prostaglandin E2 production in severely injured patients. Arch Surg 123:293–299PubMedCrossRefGoogle Scholar
  2. 2.
    Faist E, Mewes A, Baker CC et al. (1987) Prostaglandin E2 (PGE2)-dependent suppression of interleukin 2 (IL-2) production in patients with major trauma. J Trauma 27:837–848PubMedCrossRefGoogle Scholar
  3. 3.
    Fearon DT (1980) Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorponuclear leukocyte, B lymphocyte, and monocyte. J Exp Med 152:20–30PubMedCrossRefGoogle Scholar
  4. 4.
    Fleit HB, Wright SD, Unkeless JC (1984) Human neutrophil Fcγ receptor distribution and structure. Proc Natl Acad Sci USA 79:3275–3279CrossRefGoogle Scholar
  5. 5.
    Babcock GF, Alexander JW, Warden GD (1990) Flow cytometric analysis of neutrophil subsets in thermally injured patients developing infection. Clin Immunol Immunopathol 54:117–125PubMedCrossRefGoogle Scholar
  6. 6.
    Parks DR, Bryan VM, Oi VM, Oi VT, Herzenberg LA (1979) Antigen specific identification and cloning of hybridomas with a fluorescence activated cell sorter (FACS). Proc Natl Acad Sci USA 76:1962PubMedCrossRefGoogle Scholar
  7. 7.
    Bass DA, Parce JW (1983) Flow cytometric studies of oxidative product formation by neutrophils: a graded response to membrane stimulation. J Immunol 130:1910–1917PubMedGoogle Scholar
  8. 8.
    Bass DA, Olbrantz P, Szejda P, Seeds MC, McCall CE (1986) Subpopulations of neutrophils with increased oxidative product formation in blood of patients with infections. J Immunol 136:860–866PubMedGoogle Scholar
  9. 9.
    Berger M, O’Shea J, Cross AS, Folks TM, Chused TM, Brown EJ, Frank MM (1984) Human neutrophils increase expression of C3bi as well as C3b receptors upon activation. J Clin Invest 74:1566PubMedCrossRefGoogle Scholar
  10. 10.
    Kishimoto TK, Jutila MA, Berg EL, Butcher EC (1989) Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors. Science 245:1238–1241PubMedCrossRefGoogle Scholar
  11. 11.
    O’Shea J, Brown EJ, Seligmann BE, Metcalf JA, Frank MM, Gallin JI (1985) Evidence for distinct intracellular pools of receptors for C3b and C3bi in human neutrophils. J Immunol 134: 2580PubMedGoogle Scholar
  12. 12.
    Huizinga TW, van der Schoot CE, Jost C, Klaassen R, Kleijer M, von dem Borne AE, Roos D, Tetteroo PA (1988) The Pi-linked receptor FcRIII is released on stimulation of neutrophils. Nature 333(6174):667–669PubMedCrossRefGoogle Scholar
  13. 13.
    Davis JM, Dineen P, Gallin JI (1980) Neutrophil degranulation and abnormal Chemotaxis after thermal injury. J Immunol 124:263–274Google Scholar
  14. 14.
    Freeman TR, Shelby J (1988) Effect of anti-PGE antibody on cell-mediated immune response in thermally injured mice. J Trauma 28:190–194PubMedCrossRefGoogle Scholar
  15. 15.
    Snyder DA, Beller DI, Unanue ER (1982) Prostaglandins modulate macrophage Ia expression. Nature 299:263–265CrossRefGoogle Scholar
  16. 16.
    Stephan RN, Conrad PJ, Saizawa M, Dean RE, Chaudry IH (1988) Prostaglandin E2 depresses antigen-presenting cell function of peritoneal macrophages. J Surg Res 44:733–739PubMedCrossRefGoogle Scholar
  17. 17.
    Waymack JP, Yurt RW (1988) Effect of prostaglandin E on immune function in multiple animal models. Arch Surg 123(11):1429–1432PubMedCrossRefGoogle Scholar
  18. 18.
    Ward PA, Sulavik MC, Johnson KJ (1984) Rat neutrophil activation and effects of lipoxygenase and cyclooxygenase inhibitors. Am J Pathol 116(2):223–233PubMedGoogle Scholar
  19. 19.
    Styrt B, Klempner MS, Rocklin RE (1988) Comparison of prostaglandins E2 and D2 as inhibitors of respiratory burst in neutrophils from atopic and nonatopic subjects. Inflammation 12(3):213–221PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag, Berlin Heidelberg 1993

Authors and Affiliations

  • J. A. Lieberman
    • 1
  • J. M. Waldman
    • 1
  • J. K. Horn
    • 1
  1. 1.Departments of Surgery and Laboratory MedicineUniversity of CaliforniaSan FranciscoUSA

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