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. 1982 Jul;35(7):723–727. doi: 10.1136/jcp.35.7.723

Fibronectin in exudative pleural effusions.

M Klockars, T Pettersson, T Vartio, H Riska, A Vaheri
PMCID: PMC497764  PMID: 7096593

Abstract

Fibronectin is a glycoprotein found in body fluids, loose connective tissue matrix and in basement membranes. Fibronectin in pleural effusion was found to be immunologically indistinguishable from the plasma form, as shown by double-diffusion analysis. Fibronectin isolated from pleural fluid by affinity chromatography on gelatin-Sepharose had a polypeptide pattern similar to that of plasma fibronectin in SDS-polyacrylamide gel electrophoresis. In 28 patients with infectious or non-specific pleural effusion fibronectin concentrations in pleural fluid were 335 +/- 104 micrograms/ml (mean +/- SD), in 15 patients with malignant disease the concentrations were 369 +/- 173 micrograms/ml and in 26 patients with tuberculosis 441 +/- 103 micrograms/ml. The highest concentrations, 605 +/- 252 micrograms/ml, of fibronectin in pleural fluid were detected in 14 patients with connective tissue diseases. The results suggest that increased fibronectin concentrations reflect the presence of a pleurisy due to connective tissue disease or tuberculosis rather than other infectious or malignant disease.

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Selected References

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  1. ABRAMS L. D. A pleural-biopsy punch. Lancet. 1958 Jan 4;1(7010):30–31. doi: 10.1016/s0140-6736(58)92521-2. [DOI] [PubMed] [Google Scholar]
  2. Blumenstock F. A., Saba T. M., Weber P., Laffin R. Biochemical and immunological characterization of human opsonic alpha2SB glycoprotein: its identity with cold-insoluble globulin. J Biol Chem. 1978 Jun 25;253(12):4287–4291. [PubMed] [Google Scholar]
  3. Engvall E., Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer. 1977 Jul 15;20(1):1–5. doi: 10.1002/ijc.2910200102. [DOI] [PubMed] [Google Scholar]
  4. Engvall E., Ruoslahti E., Miller E. J. Affinity of fibronectin to collagens of different genetic types and to fibrinogen. J Exp Med. 1978 Jun 1;147(6):1584–1595. doi: 10.1084/jem.147.6.1584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  6. Fyrand O., Munthe E., Solum N. O. Studies on cold insoluble globulin. I Concentrations in citrated plasma in rheumatic disorders. Ann Rheum Dis. 1978 Aug;37(4):347–350. doi: 10.1136/ard.37.4.347. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gudewicz P. W., Molnar J., Lai M. Z., Beezhold D. W., Siefring G. E., Jr, Credo R. B., Lorand L. Fibronectin-mediated uptake of gelatin-coated latex particles by peritoneal macrophages. J Cell Biol. 1980 Nov;87(2 Pt 1):427–433. doi: 10.1083/jcb.87.2.427. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Harris E. D., Jr, Krane S. M. Collagenases (third of three parts). N Engl J Med. 1974 Sep 26;291(13):652–661. doi: 10.1056/NEJM197409262911305. [DOI] [PubMed] [Google Scholar]
  9. Kurkinen M., Vaheri A., Roberts P. J., Stenman S. Sequential appearance of fibronectin and collagen in experimental granulation tissue. Lab Invest. 1980 Jul;43(1):47–51. [PubMed] [Google Scholar]
  10. Kuusela P. Fibronectin binds to Staphylococcus aureus. Nature. 1978 Dec 14;276(5689):718–720. doi: 10.1038/276718a0. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Mosesson M. W. Cold-insoluble globulin (CIg), a circulating cell surface protein. Thromb Haemost. 1977 Dec 15;38(4):742–750. [PubMed] [Google Scholar]
  13. 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]
  14. OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. Prog Allergy. 1958;5:1–78. [PubMed] [Google Scholar]
  15. Stathakis N. E., Mosesson M. W. Interactions among heparin, cold-insoluble globulin, and fibrinogen in formation of the heparin-precipitable fraction of plasma. J Clin Invest. 1977 Oct;60(4):855–865. doi: 10.1172/JCI108840. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. Tsukamoto Y., Helsel W. E., Wahl S. M. Macrophage production of fibronectin, a chemoattractant for fibroblasts. J Immunol. 1981 Aug;127(2):673–678. [PubMed] [Google Scholar]
  18. Vaheri A., Mosher D. F. High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochim Biophys Acta. 1978 Sep 18;516(1):1–25. doi: 10.1016/0304-419x(78)90002-1. [DOI] [PubMed] [Google Scholar]
  19. Vartio T., Vaheri A., Von Essen R., Isomäki H., Stenman S. Fibronectin in synovial fluid and tissue in rheumatoid arthritis. Eur J Clin Invest. 1981 Jun;11(3):207–212. doi: 10.1111/j.1365-2362.1981.tb01842.x. [DOI] [PubMed] [Google Scholar]
  20. Vuento M., Vaheri A. Purification of fibronectin from human plasma by affinity chromatography under non-denaturing conditions. Biochem J. 1979 Nov 1;183(2):331–337. doi: 10.1042/bj1830331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yamada K. M., Olden K. Fibronectins--adhesive glycoproteins of cell surface and blood. Nature. 1978 Sep 21;275(5677):179–184. doi: 10.1038/275179a0. [DOI] [PubMed] [Google Scholar]

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