Skip to main content
British Journal of Experimental Pathology logoLink to British Journal of Experimental Pathology
. 1981 Aug;62(4):362–368.

The distribution of fibronectin in the pannus in rheumatoid arthritis.

D L Scott, J P Delamere, K W Walton
PMCID: PMC2041679  PMID: 7028072

Abstract

Fibronectin is an adhesive glycoprotein synthesized by mesenchymal cells. Its distribution in the rheumatoid pannus has been studied by immunofluorescence using a monospecific antiserum. All areas of the pannus contained immunoreactive fibronectin, including its junctions with synovium, ligaments, bone and cartilage. It formed a coarse extracellular meshwork which surrounded the inflammatory cells infiltrating the pannus and which codistributed with reticulin and "immature" collagen. The proliferative cellular areas of the pannus showed marked reactivity for fibronectin. Although fibronectin was present at the pannus-cartilage junction, it was not otherwise found in articular cartilage. Fibronectin in the pannus did not have any relationship to the distribution of immunoglobulins or complement. Fibronectin is a structural component of the rheumatoid pannus and may play a role in the pathogenesis of rheumatoid synovitis.

Full text

PDF
364

Images in this article

Selected References

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

  1. Cooke T. D., Hurd E. R., Jasin H. E., Bienenstock J., Ziff M. Identification of immunoglobulins and complement in rheumatoid articular collagenous tissues. Arthritis Rheum. 1975 Nov-Dec;18(6):541–551. doi: 10.1002/art.1780180603. [DOI] [PubMed] [Google Scholar]
  2. Cooper S. M., Keyser A. J., Beaulieu A. D., Ruoslahti E., Nimni M. E., Quismorio F. P., Jr Increase in fibronectin in the deep dermis of involved skin in progressive systemic sclerosis. Arthritis Rheum. 1979 Sep;22(9):983–987. doi: 10.1002/art.1780220906. [DOI] [PubMed] [Google Scholar]
  3. Dessau W., Adelmann B. C., Timpl R. Identification of the sites in collagen alpha-chains that bind serum anti-gelatin factor (cold-insoluble globulin). Biochem J. 1978 Jan 1;169(1):55–59. doi: 10.1042/bj1690055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dessau W., Sasse J., Timpl R., von der Mark K. Role of fibronectin and collagen types I and II in chondrocytic differentiation in vitro. Ann N Y Acad Sci. 1978 Jun 20;312:404–405. doi: 10.1111/j.1749-6632.1978.tb16819.x. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Gay S., Balleisen L., Remberger K., Fietzek P. P., Adelmann B. C., Kühn K. Immunohistochemical evidence for the presence of collagen type III in human arterial walls, arterial thrombi, and in leukocytes, incubated with collagen in vitro. Klin Wochenschr. 1975 Oct 1;53(19):899–902. doi: 10.1007/BF01468981. [DOI] [PubMed] [Google Scholar]
  7. Gordon H., Sweets H. H. A Simple Method for the Silver Impregnation of Reticulum. Am J Pathol. 1936 Jul;12(4):545–552.1. [PMC free article] [PubMed] [Google Scholar]
  8. HEROVICI C. [Picropolychrome: histological staining technic intended for the study of normal and pathological connective tissue]. Rev Fr Etud Clin Biol. 1963 Jan;8:88–89. [PubMed] [Google Scholar]
  9. Hahn E., Wick G., Pencev D., Timpl R. Distribution of basement membrane proteins in normal and fibrotic human liver: collagen type IV, laminin, and fibronectin. Gut. 1980 Jan;21(1):63–71. doi: 10.1136/gut.21.1.63. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LENDRUM A. C., FRASER D. S., SLIDDERS W., HENDERSON R. Studies on the character and staining of fibrin. J Clin Pathol. 1962 Sep;15:401–413. doi: 10.1136/jcp.15.5.401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Linder E., Stenman S., Lehto V. P., Vaheri A. Distribution of fibronectin in human tissues and relationship to other connective tissue components. Ann N Y Acad Sci. 1978 Jun 20;312:151–159. doi: 10.1111/j.1749-6632.1978.tb16800.x. [DOI] [PubMed] [Google Scholar]
  12. Pras M., Glynn L. E. Isolation of a non-collagenous reticulin component and its primary characterization. Br J Exp Pathol. 1973 Aug;54(4):449–456. [PMC free article] [PubMed] [Google Scholar]
  13. SOOTHILL J. F. Estimation of eight serum proteins by a gel diffusion precipitin technique. J Lab Clin Med. 1962 May;59:859–870. [PubMed] [Google Scholar]
  14. Scott D. L., Wainwright A. C., Walton K. W., Williamson N. Significance of fibronectin in rheumatoid arthritis and osteoarthrosis. Ann Rheum Dis. 1981 Apr;40(2):142–153. doi: 10.1136/ard.40.2.142. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Shiozawa S., Jasin H. E., Ziff M. Absence of immunoglobulins in rheumatoid cartilage-pannus junctions. Arthritis Rheum. 1980 Jul;23(7):816–821. doi: 10.1002/art.1780230707. [DOI] [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. Valente A. J., Walton K. W. Studies on increased vascular permeability in the pathogenesis of lesions of connective tissue diseases: I. Experimental hyperlipidaemia and immune arthropathy. Ann Rheum Dis. 1980 Oct;39(5):490–499. doi: 10.1136/ard.39.5.490. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Walton K. W., Williamson N. Histological and immunofluorescent studies on the evolution of the human atheromatous plaque. J Atheroscler Res. 1968 Jul-Aug;8(4):599–624. doi: 10.1016/s0368-1319(68)80020-1. [DOI] [PubMed] [Google Scholar]
  19. Yamada K. M., Kennedy D. W. Fibroblast cellular and plasma fibronectins are similar but not identical. J Cell Biol. 1979 Feb;80(2):492–498. doi: 10.1083/jcb.80.2.492. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]

Articles from British journal of experimental pathology are provided here courtesy of Wiley

RESOURCES