Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis

Jung Yoo, T. F. Kresina, C. J. Malemud, V. M. Goldberg

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. 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%) 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 chronic 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.

Original languageEnglish (US)
Pages (from-to)832-836
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number3
StatePublished - 1987

Fingerprint

Synovitis
Proteoglycans
Epitopes
Keratan Sulfate
Rabbits
Immunoglobulin G
Peptides
Monoclonal Antibodies
DEAE-Cellulose
Antibodies
Chondroitin Sulfates
Cartilage
Antibody Formation
Immune Sera
Anti-Idiotypic Antibodies
Pathology
Weights and Measures

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis. / Yoo, Jung; Kresina, T. F.; Malemud, C. J.; Goldberg, V. M.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, No. 3, 1987, p. 832-836.

Research output: Contribution to journalArticle

@article{d113474d24e4451a8337675f4bae3621,
title = "Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis",
abstract = "This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. 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{\%}) 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 chronic 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.",
author = "Jung Yoo and Kresina, {T. F.} and Malemud, {C. J.} and Goldberg, {V. M.}",
year = "1987",
language = "English (US)",
volume = "84",
pages = "832--836",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "3",

}

TY - JOUR

T1 - Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis

AU - Yoo, Jung

AU - Kresina, T. F.

AU - Malemud, C. J.

AU - Goldberg, V. M.

PY - 1987

Y1 - 1987

N2 - This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. 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%) 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 chronic 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.

AB - This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. 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%) 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 chronic 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.

UR - http://www.scopus.com/inward/record.url?scp=0023114810&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023114810&partnerID=8YFLogxK

M3 - Article

VL - 84

SP - 832

EP - 836

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 3

ER -