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Enhanced Expression of a Peanut Agglutinin Reactive O Linked Oligosaccharide on Fibronectins from the Synovial Fluid of Patients with Rheumatic Disease: Quantitation, Domain Localization, and Functional Significance
STEVEN CARSONS
ABSTRACT.
Methods. Identification and localization of the O linked oligosaccharide was performed by limited digestion of isolated SF Fn with a series of proteolytic enzymes followed by Western blotting with peroxidase labeled peanut agglutinin. Binding affinity to denatured collagen was performed utilizing a solid phase gelatin-binding assay. Quantitation was performed by measuring purified Fn in an antibody-lectin sandwich binding assay. Results. A desialyated O linked oligosaccharide was identified on the C-terminal 18 kDa segment of the SF Fn collagen-binding domain. These SF collagen-binding Fn fragments were more basic and had higher gelatin-binding affinities than corresponding plasma fibronectin fragments. Expression of this O linked oligosaccharide was highest on Fn isolated from osteoarthritic SF, followed by Fn isolated from rheumatoid arthritis SF, and finally normal human plasma. Conclusion. Fn isolated from SF have glycosylation alterations that may influence their biologic properties in the diseased joint. (J Rheumatol 2002;29:896-902) Key Indexing Terms:
SYNOVIAL FLUID
From the Division of Rheumatology, Allergy and Clinical Immunology, Winthrop-University Hospital, Mineola, and Department of Medicine, State University of New York at Stony Brook, Stony Brook, New York, USA. S.E. Carsons, MD, Chief, Division of Rheumatology, Allergy and Clinical Immunology, Winthrop-University Hospital, Associate Professor of Medicine, SUNY Stony Brook. Address reprint requests to Dr. S. Carsons, Division of Rheumatology, Winthrop-University Hospital, 222 Station Plaza North, Room 430, Mineola, NY 11501. E-mail: scarsons@winthrop.org Submitted May 31, 2001; revision accepted November 26, 2001. |