Summary
The distribution of fibronectin in the lining layer of inflamed rheumatoid arthritis (RA) synovium has been ultrastructurally investigated using an anti-human plasma fibronectin antibody.
The hyperplasia of lining cells was prominent in the lining layer of the inflamed RA synovium. A high level of fibronectin was localized in this region. Ultrastructurally the fibronectin was observed on the surface of both type A (type M) and type B (type F) cells, and in the extracellular fibrin-like material. This glycoprotein was detectable in rough endoplasmic reticulum (RER), some Golgi apparatus, and peripheral vesicles of type B cells. On the other hand, RER and Golgi apparatus of type A cells failed to be immunostained with the antibody. Type A cells occasionally contacted each other with interdigitation of cytoplasmic processes, and a high amount of fibronectin was localized in this region.
These findings indicate that fibronectin is synthesized along the classic secretory pathway through RER and Golgi apparatus of type B cells. On the contrary, type A cells seem not to be associated with the local synthesis of the glycoprotein. Fibronectin may play a structural role in organizing these proliferated lining cells by promoting cell adhesion. The synthesis of fibronectin by proliferated type B cells may be responsible in part for the local increase of this glycoprotein in the lining layer of RA synovium.
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References
Mosesson MW, Amrani DL (1980) The structure and biologic activities of plasma fibronectin. Blood 56:145–158
Vaheri A, Mosher DF (1978) High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochim Biophys Acta 516:1–25
Yamada KM, Olden K (1978) Fibronectins — adhesive glycoproteins of cell surface and blood. Nature 275:179–184
Engvall E, Ruoslahti E, Miller EJ (1978) Affinity of fibronectin to collagens of different genetic types and to fibrinogen. J Exp Med 147:1584–1595
Mosher D (1975) Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem 250:6614–6621
Yamada KW, Kennedy DW, Kimata K, Pratt RM (1980) Characterization of fibronectin interactions with glycosaminoglycans and identification of active proteolytic fragments. J Biol Chem 255:6055–6063
Kurkinen M, Vaheri A, Roberts PJ, Stenman S (1980) Sequential appearance of fibronectin and collagen in experimental granulation tissue. Lab Invest 43:47–51
Scott DL, Delamere JP, Walton KW (1981) The distribution of fibronectin in the pannus in rheumatoid arthritis. Br J Exp Pathol 62:362–368
Scott DL, Wainwright AC, Walton KW, Williamson N (1981) Significance of fibronectin in rheumatoid arthritis and osteoarthrosis. Ann Rheum Dis 40:142–153
Vartio T, Vaheri A, Von Essen R, Isomäki H, Stenman S (1981) Fibronectin in synovial fluid and tissue in rheumatoid arthritis. Eur J Clin Invest 11:207–212
Carson S, Natarajan C, Drew H, Diamond H (1980) Fibronectin in human synovial fluid. Arthritis Rheum 23:661
Clemmensen I, Anderson RB (1982) Different molecular forms of fibronectin in rheumatoid synovial fluid. Arthritis Rheum 25:25–31
Immartino AJ, Anderson B, Donakowski C, Schmit FR (1980) Detection of fibronectin in rheumatoid and non-rheumatoid synovial fluids and cryoproteins. Arthritis Rheum 23:694
Barland P, Novikoff AB, Hamerman D (1962) Electron microscopy of the human synovial membrane. J Cell Biol 14:207–220
Hirohata K, Kobayashi I (1964) Fine structures of the synovial tissues in rheumatoid arthritis. Kobe J Med Sci 10: 195–225
McLean IW, Nakane PK (1974) Periodate-lysine-paraformaldehyde fixative: A new fixative for immunoelectron microscopy. J Histochem Cytochem 22:1077–1083
Graham RC Jr, Karnovsky MJ (1966) The early stages of absorption of injected horseradish peroxidase in the proximal tubules of mouse kidneys: Ultrastructural cytochemistry by a new technique. J Histochem Cytochem 14:291–298
Allen C, Saba, T, Molnar J (1973) Isolation, purification and characterization of opsonic protein. J Reticuloendothel Soc 13:410–423
Blumenstock F, Saba T, Weber P, Cho E (1976) Purification and biochemical characterization of a macrophage stimulating α2-globulin opsonin protein. J Reticuloendothel Soc 19:157–172
Hedman K (1980) Intracellular localization of fibronectin using immunoperoxidase cytochemistry in light and electron microscopy. J Histochem Cytochem 28:1233–1241
Zvaifler NJ (1973) The immunopathology of joint inflammation in rheumatoid arthritis. Adv Immunol 16:265–336
Clemmensen I, Donde R, Anderson RB (1977) The primary plasmin inhibitor in rheumatoid synovial fluid. Arthritis Rheum 20:1354–1358
McDonald J, Baum BJ, Rosenberg DM, Kelman JA, Brin SC, Crystal RG (1979) Destruction of a major extracellular adhesive glycoprotein (fibronectin) of human fibroblasts by neutral proteases from polymorphonuclear leukocyte granules. Lab Invest 40:350–357
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Matsubara, T., Spycher, M.A., Rüttner, J.R. et al. The ultrastructural localization of fibronectin in the lining layer of rheumatoid arthritis synovium: The synthesis of fibronectin by type B lining cells. Rheumatol Int 3, 75–79 (1983). https://doi.org/10.1007/BF00541148
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DOI: https://doi.org/10.1007/BF00541148