[go: up one dir, main page]
More Web Proxy on the site http://driver.im/ Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1983 Jun 1;157(6):1844–1854. doi: 10.1084/jem.157.6.1844

Plasma fibronectin enhances phagocytosis of opsonized particles by human peripheral blood monocytes

PMCID: PMC2187060  PMID: 6854210

Abstract

We have investigated the effect of plasma fibronectin (Fn) on binding and phagocytosis of sheep erythrocytes (E) by human peripheral blood monocytes. Unopsonized E were not phagocytosed in the absence or presence of Fn, but Fn enhanced the phagocytosis of E bearing IgG. Sheep erythrocytes sensitized with IgM and C3b were ingested only when monocytes were exposed to Fn. The Fn enhancement of phagocytosis occurred for both fluid-phase and glass-adherent monocytes. Experiments in which Fn was washed out before mixing monocytes with opsonized E demonstrated that the Fn effect occurred because of interaction with the monocytes and not the opsonized particles. Chromatography of the Fn on Biogel A 1.5m showed that the phagocytosis-enhancing activity exactly co-chromatographed with the Fn protein. Fn did not increase the number of monocyte membrane receptors for the Fc fragment of monomeric IgG. We conclude that Fn enhances monocyte phagocytosis, not by binding to particles as a conventional opsonin, but by stimulating monocytes to ingest already opsonized particles more avidly.

Full Text

The Full Text of this article is available as a PDF (809.0 KB).

Selected References

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

  1. Berger M., Gaither T. A., Hammer C. H., Frank M. M. Lack of binding of human C3, in its native state, to C3b receptors. J Immunol. 1981 Oct;127(4):1329–1334. [PubMed] [Google Scholar]
  2. Bevilacqua M. P., Amrani D., Mosesson M. W., Bianco C. Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes. J Exp Med. 1981 Jan 1;153(1):42–60. doi: 10.1084/jem.153.1.42. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Blumenstock F., Saba T. M., Weber P., Cho E. Purification and biochemical characterization of a macrophage stimulating alpha-2-globulin opsonic protein. J Reticuloendothel Soc. 1976 Mar;19(3):157–172. [PubMed] [Google Scholar]
  4. Czop J. K., Austen K. F. Augmentation of phagocytosis by a specific fibronectin fragment that links particulate activators to the fibronectin adherence receptor of human monocytes. J Immunol. 1982 Dec;129(6):2678–2681. [PubMed] [Google Scholar]
  5. Czop J. K., Kadish J. L., Austen K. F. Augmentation of human monocyte opsonin-independent phagocytosis by fragments of human plasma fibronectin. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3649–3653. doi: 10.1073/pnas.78.6.3649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Czop J. K., Kadish J. L., Austen K. F. Purification and characterization of a protein with fibronectin determinants and phagocytosis-enhancing activity. J Immunol. 1982 Jul;129(1):163–167. [PubMed] [Google Scholar]
  7. Doran J. E., Mansberger A. R., Reese A. C. Cold insoluble globulin-enhanced phagocytosis of gelatinized targets by macrophage monolayers: a model system. J Reticuloendothel Soc. 1980 May;27(5):471–483. [PubMed] [Google Scholar]
  8. Ehlenberger A. G., Nussenzweig V. The role of membrane receptors for C3b and C3d in phagocytosis. J Exp Med. 1977 Feb 1;145(2):357–371. doi: 10.1084/jem.145.2.357. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fries L. F., Hall R. P., Lawley T. J., Crabtree G. R., Frank M. M. Monocyte receptors for the Fc portion of IgG studies with monomeric human IgG1: normal in vitro expression of Fc gamma receptors in HLA-B8/Drw3 subjects with defective Fc gamma-mediated in vivo clearance. J Immunol. 1982 Sep;129(3):1041–1049. [PubMed] [Google Scholar]
  10. Gaither T. A., Hammer C. H., Frank M. M. Studies of the molecular mechanisms of C3b inactivation and a simplified assay of beta 1H and the C3b inactivator (C3bINA). J Immunol. 1979 Sep;123(3):1195–1204. [PubMed] [Google Scholar]
  11. Griffin F. M., Jr, Mullinax P. J. Augmentation of macrophage complement receptor function in vitro. III. C3b receptors that promote phagocytosis migrate within the plane of the macrophage plasma membrane. J Exp Med. 1981 Aug 1;154(2):291–305. doi: 10.1084/jem.154.2.291. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hammer C. H., Wirtz G. H., Renfer L., Gresham H. D., Tack B. F. Large scale isolation of functionally active components of the human complement system. J Biol Chem. 1981 Apr 25;256(8):3995–4006. [PubMed] [Google Scholar]
  13. Marquette D., Molnar J., Yamada K., Schlesinger D., Darby S., Van Alten P. Phagocytosis-promoting activity of avian plasma and fibroblastic cell surface fibronectins. Mol Cell Biochem. 1981 May 26;36(3):147–155. doi: 10.1007/BF02357031. [DOI] [PubMed] [Google Scholar]
  14. Mosesson M. W., Umfleet R. A. The cold-insoluble globulin of human plasma. I. Purification, primary characterization, and relationship to fibrinogen and other cold-insoluble fraction components. J Biol Chem. 1970 Nov 10;245(21):5728–5736. [PubMed] [Google Scholar]
  15. Niehaus G. D., Dillon B. C., Schumacker P. T., Saba T. M. Influence of gelatin on bioassayable and immunoreactive opsonic fibronectin. Proc Soc Exp Biol Med. 1981 Oct;168(1):15–23. doi: 10.3181/00379727-168-41228. [DOI] [PubMed] [Google Scholar]
  16. Norris D. A., Clark R. A., Swigart L. M., Huff J. C., Weston W. L., Howell S. E. Fibronectin fragment(s) are chemotactic for human peripheral blood monocytes. J Immunol. 1982 Oct;129(4):1612–1618. [PubMed] [Google Scholar]
  17. Saba T. M., Blumenstock F. A., Weber P., Kaplan J. E. Physiologic role of cold-insoluble globulin in systemic host defense: implications of its characterization as the opsonic alpha 2-surface-binding glycoprotein. Ann N Y Acad Sci. 1978 Jun 20;312:43–55. doi: 10.1111/j.1749-6632.1978.tb16792.x. [DOI] [PubMed] [Google Scholar]
  18. Saba T. M., Di Luzio N. R. Reticuloendothelial blockade and recovery as a function of opsonic activity. Am J Physiol. 1969 Jan;216(1):197–205. doi: 10.1152/ajplegacy.1969.216.1.197. [DOI] [PubMed] [Google Scholar]
  19. Verbrugh H. A., Peterson P. K., Smith D. E., Nguyen B. Y., Hoidal J. R., Wilkinson B. J., Verhoef J., Furcht L. T. Human fibronectin binding to staphylococcal surface protein and its relative inefficiency in promoting phagocytosis by human polymorphonuclear leukocytes, monocytes, and alveolar macrophages. Infect Immun. 1981 Sep;33(3):811–819. doi: 10.1128/iai.33.3.811-819.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Yamada K. M., Hahn L. H., Olden K. Structure and function of the fibronectins. Prog Clin Biol Res. 1980;41:797–819. [PubMed] [Google Scholar]

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

RESOURCES