Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis
This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. With the use of radioimmunoassay, antibodies reactive with purified rabbit proteoglycan monomer were observed in nine of nine rabbits with immune synovitis. IgG-immunized but nonsynovitic control animals with no pathology showed no antibody response. A panel of murine monoclonal antibodies with defined specificity towards rabbit proteoglycan were utilized to characterize the epitope specificity of the immune synovitis polyclonal anti-proteoglycan response. One murine monoclonal antibody, 6C11, inhibited the binding of the polyclonal antisera to proteoglycan in all nine animals with significant (>40/sup 5/) inhibition in six of nine rabbits. Further inhibition studies utilizing DEAE-cellulose-resolved proteoglycan tryptic peptides revealed that peptides poor in chondroitin sulfate were strong inhibitors of binding of the polyclonal antibodies to the proteoglycan substrate. In particular, keratan sulfate-containing tryptic peptides were most inhibitory on a per weight basis. These results indicate that, in chromic IgG-induced immune synovitis, anti-proteoglycan antibodies elicited are heterogeneous with regard to specificity, but a relatively large proportion predominantly recognized a portion of the proteoglycan molecule containing core protein and associated keratan sulfate.
- Research Organization:
- Case Western Reserve Univ., Cleveland, OH
- OSTI ID:
- 6021511
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 84:3
- Country of Publication:
- United States
- Language:
- English
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ANIMALS
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550601* - Medicine- Unsealed Radionuclides in Diagnostics