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. 1977 May;87(2):ENG.

Attachment and ingestion of mycoplasmas by mouse macrophages. I. Kinetics of the interaction and effects on phagocyte glucose metabolism.

T C Jones, 331-45, L Hang
PMCID: PMC2032032  PMID: 851167

Abstract

Rates of attachment and ingestion of Mycoplasma pulmonis by mouse peritoneal macrophages and the effect of the organism on phagocyte glucose metabolism were studied in vitro. Antimycoplasma antibody, but not complement, enhances attachment of mycoplasma to macrophages. Antibody-mediated attachment is not affected by the length of time the cell is maintained in culture or its adherence to a glass surface. Adherence of mycoplasma by nonimmunologic means to cell spread on glass is significantly greater than attachment to macrophages in suspension. Mycoplasmas attached to macrophage membrane do not increase glucose metabolism via the hexose monophosphate shunt. Because of this, the rate of glucose metabolism by macrophages is an accurate quantitative correlate of the recognition and ingestion stage of phagocytosis of mycoplasmas. Antibody induces a more rapid rate of particle ingestion than does altering the mycoplasma by proteolysis. Complement does not augment the rate of ingestion induced by antimycoplasma antibody. By analogy with enzyme and absorption kinetics, it appears likely that differences observed between phagocytosis induced by antibody and that induced by trypsin are due to different rates of recognition between particles rather than different ingestion mechanisms. (Am J Pathol 87:331-346, 1977).

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Selected References

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

  1. Bianco C., Griffin F. M., Jr, Silverstein S. C. Studies of the macrophage complement receptor. Alteration of receptor function upon macrophage activation. J Exp Med. 1975 Jun 1;141(6):1278–1290. doi: 10.1084/jem.141.6.1278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bystryn J. C., Siskind G. W., Uhr J. W. Binding of antigen by immunocytes. I. Effect of ligand valence on binding affinity of MOPC 315 cells for DNP conjugates. J Exp Med. 1973 Feb 1;137(2):301–316. doi: 10.1084/jem.137.2.301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. COHN Z. A. The fate of bacteria within phagocytic cells. I. The degradation of isotopically labeled bacteria by polymorphonuclear leucocytes and macrophages. J Exp Med. 1963 Jan 1;117:27–42. doi: 10.1084/jem.117.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cohn Z. A. The structure and function of monocytes and macrophages. Adv Immunol. 1968;9:163–214. doi: 10.1016/s0065-2776(08)60443-5. [DOI] [PubMed] [Google Scholar]
  5. Graham R. C., Jr, Karnovsky M. J., Shafer A. W., Glass E. A., Karnovsky M. L. Metabolic and morphological observations on the effect of surface-active agents of leukocytes. J Cell Biol. 1967 Mar;32(3):629–647. doi: 10.1083/jcb.32.3.629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Holland P., Holland N. H., Cohn Z. A. The selective inhibition of macrophage phagocytic receptors by anti-membrane antibodies. J Exp Med. 1972 Mar 1;135(3):458–475. doi: 10.1084/jem.135.3.458. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Huber H., Fudenberg H. H. Receptor sites of human monocytes for IgG. Int Arch Allergy Appl Immunol. 1968;34(1):18–31. doi: 10.1159/000230091. [DOI] [PubMed] [Google Scholar]
  8. Jones T. C., Hirsch J. G. The interaction in vitro of Mycoplasma pulmonis with mouse peritoneal macrophages and L-cells. J Exp Med. 1971 Feb 1;133(2):231–259. doi: 10.1084/jem.133.2.231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jones T. C., Yeh S., Hirsch J. G. Studies on attachment and ingestion phases of phagocytosis of Mycoplasma pulmonis by mouse peritoneal macrophages. Proc Soc Exp Biol Med. 1972 Feb;139(2):464–470. doi: 10.3181/00379727-139-36165. [DOI] [PubMed] [Google Scholar]
  10. LoBuglio A. F., Cotran R. S., Jandl J. H. Red cells coated with immunoglobulin G: binding and sphering by mononuclear cells in man. Science. 1967 Dec 22;158(3808):1582–1585. doi: 10.1126/science.158.3808.1582. [DOI] [PubMed] [Google Scholar]
  11. Mantovani B., Rabinovitch M., Nussenzweig V. Phagocytosis of immune complexes by macrophages. Different roles of the macrophage receptor sites for complement (C3) and for immunoglobulin (IgG). J Exp Med. 1972 Apr 1;135(4):780–792. doi: 10.1084/jem.135.4.780. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Michell R. H., Pancake S. J., Noseworthy J., Karnovsky M. L. Measurement of rates of phagocytosis: the use of cellular monolayers. J Cell Biol. 1969 Jan;40(1):216–224. doi: 10.1083/jcb.40.1.216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. OREN R., FARNHAM A. E., SAITO K., MILOFSKY E., KARNOVSKY M. L. Metabolic patterns in three types of phagocytizing cells. J Cell Biol. 1963 Jun;17:487–501. doi: 10.1083/jcb.17.3.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Rhodes J. Macrophage heterogeneity in receptor activity: the activation of macrophage Fc receptor function in vivo and in vitro. J Immunol. 1975 Mar;114(3):976–981. [PubMed] [Google Scholar]
  15. Stossel T. P. Quantitative studies of phagocytosis. Kinetic effects of cations and heat-labile opsonin. J Cell Biol. 1973 Aug;58(2):346–356. doi: 10.1083/jcb.58.2.346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Weisman R. A., Korn E. D. Phagocytosis of latex beads by Acanthamoeba. I. Biochemical properties. Biochemistry. 1967 Feb;6(2):485–497. doi: 10.1021/bi00854a017. [DOI] [PubMed] [Google Scholar]

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