Skip to main content
NCBI home page
Infection and Immunity logoLink to Infection and Immunity
. 1977 Sep;17(3):613–620. doi: 10.1128/iai.17.3.613-620.1977

Macrophage-Agglutinating Factor Produced In Vitro by BCG-Sensitized Lymphocytes

L F Garcia-Moreno 1,†, Quentin N Myrvik 1
PMCID: PMC421171  PMID: 332629

Abstract

Supernatant fluids from cultures of BCG-sensitized rabbit lymph node and spleen cells contained a factor that strongly agglutinated normal rabbit alveolar macrophages within 3 min at room temperature. In contrast, fluids from nonsensitized cell cultures did not agglutinate normal rabbit alveolar macrophages. This factor was designated macrophage-agglutinating factor (MAgF) because it is similar to the previously described factor found in lung lavages of rabbits exhibiting a BCG-induced pulmonary delayed hypersensitivity reaction. The kinetics of MAgF production in vitro by sensitized lymph node cells and its inhibition by puromycin and actinomycin D suggest active synthesis; sensitized spleen cells exhibited kinetics resembling release rather than synthesis. Studies on purified lymphocyte and macrophage populations from sensitized spleen and lymph nodes indicated that lymphocytes are responsible for MAgF production. However, MAgF production was not induced in normal cells incubated in vitro with concanavalin A or phytohemagglutinin. Fractionation of cell culture supernatant fluids in Sephadex G-100 or Ultrogel AcA-34 clearly separated MAgF from migration inhibition factor; MAgF was present in the void volume of the eluates, suggesting a molecular weight of over 400,000, whereas migration inhibition factor was recovered in the same peak as albumin. The role of MAgF in vivo is unknown, but it is postulated that it may cause the adherence of macrophages during granuloma formation.

Full text

PDF
613

Selected References

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

  1. Anderson L. C., Nordling S., Häyry P. Electrophoretic fractionation of guniea pig lymphocytes: evidence for different subsets of T and B cells in spleen and lymph node. J Immunol. 1975 Apr;114(4):1226–1229. [PubMed] [Google Scholar]
  2. Cantey J. R., Hand W. L. Cell-mediated immunity after bacterial infection of the lower respiratory tract. J Clin Invest. 1974 Nov;54(5):1125–1134. doi: 10.1172/JCI107856. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cantor H., Boyse E. A. Functional subclasses of T-lymphocytes bearing different Ly antigens. I. The generation of functionally distinct T-cell subclasses is a differentiative process independent of antigen. J Exp Med. 1975 Jun 1;141(6):1376–1389. doi: 10.1084/jem.141.6.1376. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ford W. H., Ashworth L. A., Inder S. Effect of the concentration of inducing agent on the output of lymphokines in the guinea pig. Eur J Immunol. 1976 Feb;6(2):135–138. doi: 10.1002/eji.1830060213. [DOI] [PubMed] [Google Scholar]
  5. Fox R. A., Gregory D. S., Feldman J. D. Macrophage receptors for migration inhibitory factor (MIF), migration stimulatory factor (MSF), and agglutinating factor. J Immunol. 1974 May;112(5):1867–1872. [PubMed] [Google Scholar]
  6. Fox R. A., MacSween J. M. The isolation of migration inhibition factor. Immunol Commun. 1974;3(4):375–389. doi: 10.3109/08820137409061117. [DOI] [PubMed] [Google Scholar]
  7. GOLDBERG I. H., RABINOWITZ M., REICH E. Basis of actinomycin action. I. DNA binding and inhibition of RNA-polymerase synthetic reactions by actinomycin. Proc Natl Acad Sci U S A. 1962 Dec 15;48:2094–2101. doi: 10.1073/pnas.48.12.2094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Galindo B., Myrvik Q. N., Love S. H. A macrophage agglutinating factor produced during a pulmonary delayed hypersensitivity reaction. J Reticuloendothel Soc. 1975 Nov;18(5):295–304. [PubMed] [Google Scholar]
  9. Galindo B., Myrvik Q. N. Migratory response of granulomatous alveolar cells from BCG-sensitized rabbits. J Immunol. 1970 Jul;105(1):227–237. [PubMed] [Google Scholar]
  10. Gotoff S. P., Lolekha S., Lopata M., Kopp J., Kopp R. L., Malecki T. J. The macrophage aggregation assay for cell-mediated immunity in man. Studies of patients with Hodgkin's disease and sarcoidosis. J Lab Clin Med. 1973 Oct;82(4):682–691. [PubMed] [Google Scholar]
  11. Kühner A. L., David J. R. Partial characterization of murine migration inhibitory factor (MIF). J Immunol. 1976 Jan;116(1):140–145. [PubMed] [Google Scholar]
  12. Leu R. W., Eddleston A. L., Hadden J. W., Good R. A. Mechanism of action of migration inhibitory factor (MIF). I. Evidence for a receptor for MIF present on the peritoneal macrophage but not on the alveolar macrophage. J Exp Med. 1972 Sep 1;136(3):589–603. doi: 10.1084/jem.136.3.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lolekha S., Dray S., Gotoff S. P. Macrophage aggregation in vitro: a correlate of delayed hypersensitivity. J Immunol. 1970 Feb;104(2):296–304. [PubMed] [Google Scholar]
  14. MYRVIK Q., LEAKE E. S., FARISS B. Studies on pulmonary alveolar macrophages from the normal rabbit: a technique to procure them in a high state of purity. J Immunol. 1961 Feb;86:128–132. [PubMed] [Google Scholar]
  15. Moore V. L., Myrvik Q. N. Inhibition of normal rabbit alveolar macrophages by factor(s) resembling migration inhibition factor. J Reticuloendothel Soc. 1974 Jul;16(1):21–26. [PubMed] [Google Scholar]
  16. Phillips S. M., Carpenter C. B., Merrill J. P. Cellular immunity in the mouse. II. Correlation of in vivo and in vitro phenomena. Cell Immunol. 1972 Oct;5(2):249–263. doi: 10.1016/0008-8749(72)90051-2. [DOI] [PubMed] [Google Scholar]
  17. Postlethwaite A. E., Kang A. H. Guinea pig lymphocyte-derived macrophage aggregation factor: its separation from macrophage migration inhibitory factor. J Immunol. 1976 Nov;117(5 Pt 1):1651–1655. [PubMed] [Google Scholar]
  18. Waksman B. H., Namba Y. On soluble mediators of immunologic regulation. Cell Immunol. 1976 Jan;21(1):161–176. doi: 10.1016/0008-8749(76)90337-3. [DOI] [PubMed] [Google Scholar]
  19. Wilson B. S., Teodorescu M., Dray S. Enumeration and isolation of rabbit T and B lymphocytes by using antibody-coated erythrocytes. J Immunol. 1976 May;116(5):1306–1312. [PubMed] [Google Scholar]
  20. Yarmolinsky M. B., Haba G. L. INHIBITION BY PUROMYCIN OF AMINO ACID INCORPORATION INTO PROTEIN. Proc Natl Acad Sci U S A. 1959 Dec;45(12):1721–1729. doi: 10.1073/pnas.45.12.1721. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES