Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1989 Jul 1;170(1):259–267. doi: 10.1084/jem.170.1.259

A monoclonal antibody to sialophorin (CD43) induces homotypic adhesion and activation of human monocytes

PMCID: PMC2189387  PMID: 2787380

Abstract

Treatment of human monocytes for 24-48 h with the anti-CD43 mAb L10 caused five- to sevenfold stimulation of hydrogen peroxide-producing capacity, an established characteristic of activated monocytes. Peroxide-producing capacity induced by L10 antibody (1.6 +/- 0.3 nmol H2O2/micrograms DNA/h) was comparable with that induced by IFN-gamma (1.3 +/- 0.4 nmol H2O2/micrograms DNA/h), but appeared more rapidly (maximal at 24 h) than in the IFN-gamma-treated monocytes (maximal at 48 h). Treatment of monocytes with L10 mAb also caused dramatic increase in aggregation (homotypic adhesion). Induction of monocyte aggregation by L10 mAb required incubation for 1-8 h in the presence of Mg2+ and was abrogated by TA-1, an anti-LFA-1-alpha mAb. Thus, L10- induced monocyte activation proceeds via a Mg2+-requiring aggregation stage involving LFA-1. Whereas the extent of monocyte aggregation induced by L10 mAb and by IFN-gamma were comparable, the L10-induced aggregation occurred more rapidly (maximal at 8 h) than the IFN-gamma- induced aggregation (maximal at 24 h). The more rapid appearance of aggregation and increased hydrogen peroxide capacity in L10-treated monocytes suggests that the L10-induced activation pathway is independent of IFN-gamma-and IFN-gamma-R dependent events. These findings suggest that the surface molecule CD43 is the receptor of an independent activation pathway that leads in lymphocytes to proliferation and in monocytes to activation.

Full Text

The Full Text of this article is available as a PDF (554.1 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aguet M., Dembić Z., Merlin G. Molecular cloning and expression of the human interferon-gamma receptor. Cell. 1988 Oct 21;55(2):273–280. doi: 10.1016/0092-8674(88)90050-5. [DOI] [PubMed] [Google Scholar]
  2. Anderson D. C., Springer T. A. Leukocyte adhesion deficiency: an inherited defect in the Mac-1, LFA-1, and p150,95 glycoproteins. Annu Rev Med. 1987;38:175–194. doi: 10.1146/annurev.me.38.020187.001135. [DOI] [PubMed] [Google Scholar]
  3. Arnaout M. A., Todd R. F., 3rd, Dana N., Melamed J., Schlossman S. F., Colten H. R. Inhibition of phagocytosis of complement C3- or immunoglobulin G-coated particles and of C3bi binding by monoclonal antibodies to a monocyte-granulocyte membrane glycoprotein (Mol). J Clin Invest. 1983 Jul;72(1):171–179. doi: 10.1172/JCI110955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Axelsson B., Youseffi-Etemad R., Hammarström S., Perlmann P. Induction of aggregation and enhancement of proliferation and IL-2 secretion in human T cells by antibodies to CD43. J Immunol. 1988 Nov 1;141(9):2912–2917. [PubMed] [Google Scholar]
  5. Beatty P. G., Ledbetter J. A., Martin P. J., Price T. H., Hansen J. A. Definition of a common leukocyte cell-surface antigen (Lp95-150) associated with diverse cell-mediated immune functions. J Immunol. 1983 Dec;131(6):2913–2918. [PubMed] [Google Scholar]
  6. Borche L., Lozano F., Vilella R., Vives J. CD43 monoclonal antibodies recognize the large sialoglycoprotein of human leukocytes. Eur J Immunol. 1987 Oct;17(10):1523–1526. doi: 10.1002/eji.1830171023. [DOI] [PubMed] [Google Scholar]
  7. Carlsson S. R., Fukuda M. Isolation and characterization of leukosialin, a major sialoglycoprotein on human leukocytes. J Biol Chem. 1986 Sep 25;261(27):12779–12786. [PubMed] [Google Scholar]
  8. Ding A., Wright S. D., Nathan C. Activation of mouse peritoneal macrophages by monoclonal antibodies to Mac-1 (complement receptor type 3). J Exp Med. 1987 Mar 1;165(3):733–749. doi: 10.1084/jem.165.3.733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Ey P. L., Prowse S. J., Jenkin C. R. Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose. Immunochemistry. 1978 Jul;15(7):429–436. doi: 10.1016/0161-5890(78)90070-6. [DOI] [PubMed] [Google Scholar]
  10. Johnston R. B., Jr, Kitagawa S. Molecular basis for the enhanced respiratory burst of activated macrophages. Fed Proc. 1985 Nov;44(14):2927–2932. [PubMed] [Google Scholar]
  11. KISSANE J. M., ROBINS E. The fluorometric measurement of deoxyribonucleic acid in animal tissues with special reference to the central nervous system. J Biol Chem. 1958 Jul;233(1):184–188. [PubMed] [Google Scholar]
  12. Killeen N., Barclay A. N., Willis A. C., Williams A. F. The sequence of rat leukosialin (W3/13 antigen) reveals a molecule with O-linked glycosylation of one third of its extracellular amino acids. EMBO J. 1987 Dec 20;6(13):4029–4034. doi: 10.1002/j.1460-2075.1987.tb02747.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LeBien T. W., Bradley J. G., Koller B. Preliminary structural characterization of the leukocyte cell surface molecule recognized by monoclonal antibody TA-1. J Immunol. 1983 Apr;130(4):1833–1836. [PubMed] [Google Scholar]
  14. Mentzer S. J., Faller D. V., Burakoff S. J. Interferon-gamma induction of LFA-1-mediated homotypic adhesion of human monocytes. J Immunol. 1986 Jul 1;137(1):108–113. [PubMed] [Google Scholar]
  15. Nathan C. F., Murray H. W., Wiebe M. E., Rubin B. Y. Identification of interferon-gamma as the lymphokine that activates human macrophage oxidative metabolism and antimicrobial activity. J Exp Med. 1983 Sep 1;158(3):670–689. doi: 10.1084/jem.158.3.670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Nishizuka Y. Studies and perspectives of protein kinase C. Science. 1986 Jul 18;233(4761):305–312. doi: 10.1126/science.3014651. [DOI] [PubMed] [Google Scholar]
  17. Pabst M. J., Johnston R. B., Jr Increased production of superoxide anion by macrophages exposed in vitro to muramyl dipeptide or lipopolysaccharide. J Exp Med. 1980 Jan 1;151(1):101–114. doi: 10.1084/jem.151.1.101. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Remold-O'Donnell E., Davis A. E., 3rd, Kenney D., Bhaskar K. R., Rosen F. S. Purification and chemical composition of gpL115, the human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome. J Biol Chem. 1986 Jun 5;261(16):7526–7530. [PubMed] [Google Scholar]
  19. Remold-O'Donnell E., Kenney D. M., Parkman R., Cairns L., Savage B., Rosen F. S. Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome. J Exp Med. 1984 Jun 1;159(6):1705–1723. doi: 10.1084/jem.159.6.1705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Remold-O'Donnell E. Structure and function of macrophage adhesion molecule examined by epitope mapping. J Immunol. 1988 Aug 1;141(3):905–912. [PubMed] [Google Scholar]
  21. Remold-O'Donnell E., Zimmerman C., Kenney D., Rosen F. S. Expression on blood cells of sialophorin, the surface glycoprotein that is defective in Wiskott-Aldrich syndrome. Blood. 1987 Jul;70(1):104–109. [PubMed] [Google Scholar]
  22. Todd R. F., 3rd, Van Agthoven A., Schlossman S. F., Terhorst C. Structural analysis of differentiation antigens Mo1 and Mo2 on human monocytes. Hybridoma. 1982;1(3):329–337. doi: 10.1089/hyb.1.1982.1.329. [DOI] [PubMed] [Google Scholar]
  23. Wright S. D., Rao P. E., Van Voorhis W. C., Craigmyle L. S., Iida K., Talle M. A., Westberg E. F., Goldstein G., Silverstein S. C. Identification of the C3bi receptor of human monocytes and macrophages by using monoclonal antibodies. Proc Natl Acad Sci U S A. 1983 Sep;80(18):5699–5703. doi: 10.1073/pnas.80.18.5699. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES