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. 1986 Nov;125(2):349–357.

Response of pulmonary macrophages to hyperoxic pulmonary injury. Acquisition of surface fibronectin and fibrin/ogen and enhanced expression of a fibronectin receptor.

R L Kradin, Y Zhu, C A Hales, C Bianco, R B Colvin
PMCID: PMC1888255  PMID: 2947472

Abstract

The in vivo acquisition of coagulation plasma proteins on the surface of pulmonary macrophages was studied in guinea pigs breathing 95% oxygen. Fibrin/ogen and fibronectin appeared rapidly and concurrently on the surfaces of macrophages in the bronchoalveolar lavage fluid, which was judged by immunohistologic examination and flow cytometry. Pulmonary macrophages showed a parallel increase in the expression of a surface fibronectin receptor. Hyperoxic lung injury was accompanied by deposition of an extravascular pulmonary matrix of fibronectin and fibrin/ogen and depressed plasma levels of fibronectin. Binding to clot matrix proteins may lead to aggregation and retention of macrophages at sites of acute lung injury as well as alteration of cell function.

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Selected References

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  1. Alitalo K., Hovi T., Vaheri A. Fibronectin is produced by human macrophages. J Exp Med. 1980 Mar 1;151(3):602–613. doi: 10.1084/jem.151.3.602. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bachofen M., Weibel E. R. Alterations of the gas exchange apparatus in adult respiratory insufficiency associated with septicemia. Am Rev Respir Dis. 1977 Oct;116(4):589–615. doi: 10.1164/arrd.1977.116.4.589. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Bhan A. K., Reinherz E. L., Poppema S., McCluskey R. T., Schlossman S. F. Location of T cell and major histocompatibility complex antigens in the human thymus. J Exp Med. 1980 Oct 1;152(4):771–782. doi: 10.1084/jem.152.4.771. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bianco C. Fibrin, fibronectin, and macrophages. Ann N Y Acad Sci. 1983 Jun 27;408:602–609. doi: 10.1111/j.1749-6632.1983.tb23277.x. [DOI] [PubMed] [Google Scholar]
  6. Burrell R., Anderson M. The induction of fibrogenesis by silica-treated alveolar macrophages. Environ Res. 1973 Dec;6(4):389–394. doi: 10.1016/0013-9351(73)90054-6. [DOI] [PubMed] [Google Scholar]
  7. Clark R. A., Dvorak H. F., Colvin R. B. Fibronectin in delayed-type hypersensitivity skin reactions: associations with vessel permeability and endothelial cell activation. J Immunol. 1981 Feb;126(2):787–793. [PubMed] [Google Scholar]
  8. Colvin R. B. Fibrinogen-fibrin interactions with fibroblasts and macrophages. Ann N Y Acad Sci. 1983 Jun 27;408:621–633. doi: 10.1111/j.1749-6632.1983.tb23279.x. [DOI] [PubMed] [Google Scholar]
  9. Colvin R. B., Gardner P. I., Roblin R. O., Verderber E. L., Lanigan J. M., Mosesson M. W. Cell surface fibrinogen-fibrin receptors on cultured human fibroblasts. Association with fibronectin (cold insoluble globulin, LETS protein) and loss in SV40 transformed cells. Lab Invest. 1979 Nov;41(5):464–473. [PubMed] [Google Scholar]
  10. 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]
  11. Deno D. C., McCafferty M. H., Saba T. M., Blumenstock F. A. Mechanism of acute depletion of plasma fibronectin following thermal injury in rats. Appearance of a gelatinlike ligand in plasma. J Clin Invest. 1984 Jan;73(1):20–34. doi: 10.1172/JCI111191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Engvall E. Enzyme immunoassay ELISA and EMIT. Methods Enzymol. 1980;70(A):419–439. doi: 10.1016/s0076-6879(80)70067-8. [DOI] [PubMed] [Google Scholar]
  13. Fujikawa L. S., Foster C. S., Harrist T. J., Lanigan J. M., Colvin R. B. Fibronectin in healing rabbit corneal wounds. Lab Invest. 1981 Aug;45(2):120–129. [PubMed] [Google Scholar]
  14. Godfrey H. P., Angadi C. V., Wolstencroft R. A., Bianco C. Localization of macrophage agglutination factor activity to the gelatin-binding domain of fibronectin. J Immunol. 1984 Sep;133(3):1417–1423. [PubMed] [Google Scholar]
  15. Green G. M. The J. Burns Amberson Lecture--in defense of the lung. Am Rev Respir Dis. 1970 Nov;102(5):691–703. doi: 10.1164/arrd.1970.102.5.691. [DOI] [PubMed] [Google Scholar]
  16. Hoffman R. A., Kung P. C., Hansen W. P., Goldstein G. Simple and rapid measurement of human T lymphocytes and their subclasses in peripheral blood. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4914–4917. doi: 10.1073/pnas.77.8.4914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Hosein B., Bianco C. Monocyte receptors for fibronectin characterized by a monoclonal antibody that interferes with receptor activity. J Exp Med. 1985 Jul 1;162(1):157–170. doi: 10.1084/jem.162.1.157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Hynes R. O. The role of fibronectin in cellular behavior. Results Probl Cell Differ. 1980;11:112–123. doi: 10.1007/978-3-540-38267-6_15. [DOI] [PubMed] [Google Scholar]
  19. Kleinman H. K., Wilkes C. M., Martin G. R. Interaction of fibronectin with collagen fibrils. Biochemistry. 1981 Apr 14;20(8):2325–2330. doi: 10.1021/bi00511a039. [DOI] [PubMed] [Google Scholar]
  20. Köhler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975 Aug 7;256(5517):495–497. doi: 10.1038/256495a0. [DOI] [PubMed] [Google Scholar]
  21. Lipscomb M. F., Toews G. B., Lyons C. R., Uhr J. W. Antigen presentation by guinea pig alveolar macrophages. J Immunol. 1981 Jan;126(1):286–291. [PubMed] [Google Scholar]
  22. Moscicki R. A., Amento E. P., Krane S. M., Kurnick J. T., Colvin R. B. Modulation of surface antigens of a human monocyte cell line, U937, during incubation with T lymphocyte-conditioned medium: detection of T4 antigen and its presence on normal blood monocytes. J Immunol. 1983 Aug;131(2):743–748. [PubMed] [Google Scholar]
  23. Mosher D. F. Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem. 1975 Aug 25;250(16):6614–6621. [PubMed] [Google Scholar]
  24. Mosher D. F. Fibronectin. Prog Hemost Thromb. 1980;5:111–151. [PubMed] [Google Scholar]
  25. Murphy G. F., Bhan A. K., Harrist T. J., Mihm M. C., Jr In situ identification of T6-positive cells in normal human dermis by immunoelectron microscopy. Br J Dermatol. 1983 Apr;108(4):423–431. doi: 10.1111/j.1365-2133.1983.tb04594.x. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. Pettersson E. E., Colvin R. B. Cold-insoluble globulin (fibronectin, LETS protein) in normal and diseased human glomeruli: papain-sensitive attachment to normal glomeruli and deposition in crescents. Clin Immunol Immunopathol. 1978 Dec;11(4):425–436. doi: 10.1016/0090-1229(78)90170-8. [DOI] [PubMed] [Google Scholar]
  28. Pommier C. G., O'Shea J., Chused T., Yancey K., Frank M. M., Takahashi T., Brown E. J. Studies on the fibronectin receptors of human peripheral blood leukocytes. Morphologic and functional characterization. J Exp Med. 1984 Jan 1;159(1):137–151. doi: 10.1084/jem.159.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Remold H. G., Shaw J. E., David J. R. A macrophage surface component related to fibronectin is involved in the response to migration inhibitory factor. Cell Immunol. 1981 Feb;58(1):175–187. doi: 10.1016/0008-8749(81)90159-3. [DOI] [PubMed] [Google Scholar]
  30. Ruoslahti E., Hayman E. G., Kuusela P., Shively J. E., Engvall E. Isolation of a tryptic fragment containing the collagen-binding site of plasma fibronectin. J Biol Chem. 1979 Jul 10;254(13):6054–6059. [PubMed] [Google Scholar]
  31. 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]
  32. Stenman S., Vaheri A. Distribution of a major connective tissue protein, fibronectin, in normal human tissues. J Exp Med. 1978 Apr 1;147(4):1054–1064. doi: 10.1084/jem.147.4.1054. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Yamada K. M., Akiyama S. K., Hayashi M. Fibronectin structure and function, and its interactions with glycosaminoglycans. Biochem Soc Trans. 1981 Dec;9(6):506–508. doi: 10.1042/bst0090506. [DOI] [PubMed] [Google Scholar]

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