Original article| Volume 102, ISSUE 5, P722-731, November 1983

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Factors influencing the incorporation of fibronectin into synovial fluid cryoprotein

  • Steven Carsons
    Reprint requests: Steven Carsons, M.D., Department of Medicine, Long Island Jewish-Hillside Medical Center, New Hyde Park, N. Y. 11042.
    From the Section of Rheumatic Diseases, Department of Medicine, S.U.N.Y. Downstate Medical Center Brooklyn, N. Y., USA
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  • Beverly B. Lavietes
    From the Section of Rheumatic Diseases, Department of Medicine, S.U.N.Y. Downstate Medical Center Brooklyn, N. Y., USA
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  • Herbert S. Diamond
    From the Section of Rheumatic Diseases, Department of Medicine, S.U.N.Y. Downstate Medical Center Brooklyn, N. Y., USA
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  • Author Footnotes
    ∗ Present address: Department of Medicine, Long Island Jewish-Hillside Medical Center, New Hyde Park, N. Y. 11042.
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      Methods of synovial fluid collection and processing known to affect cryoprotein formation were examined to investigate the proposed role of fibronectin in synovial fluid cryoprecipitation. Fibronectin, a nonimmunoglobulin, noncomplement synovial fluid protein was present in all resolubilized synovial fluid cryoproteins studied. Radiolabeled fibronectin was precipitated from rheumatoid synovial fluid to a significantly greater extent (10%) than from noninflammatory (osteoarthritic) synovial fluid (2.8%), normal plasma (1.3%), or normal serum (0.5%) (p < 0.01). Clotting of synovial fluid reduced fibronectin concentration 44% and resulted in a reduction in the amount and percent incorporation of fibronectin into cryoprotein, whereas heparinization and hyaluronidase treatment increased cryoprecipitable fibronectin. Affinity depletion of synovial fluid fibronectin resulted in loss of C1q and reduction in IgG in the cryoprotein; however, fibronectin, C1q, and IgG could not be co-eluted from affinity matrices of gelatin and protein A-Sepharose. Cryoprotein formation from pathologic synovial fluid depends in part on fibronectin and appears to involve interactions between fibronectin and fibrinogen as well as immunoglobulin complexes and complement components.


      (Fn) (fibronectin), (SDS-PAGE) (sodium dodecyl sulfate-polyacrylamide gel electrophoresis), (Kd) (kilodalton), (PBS) (phosphate-buffered saune), (RA) (rheumatoid arthritis), (OA) (osteoarthritis), (EDTA) (ethylenediamine tetraacetic acid), (DTT) (dithiothreitol)
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