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Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan.
Open accessAbstract
Monoclonal antibodies were raised against proteoglycan core protein isolated after chondroitinase ABC digestion of human articular cartilage proteoglycan monomer. Characterization of one of the monoclonal antibodies (1/20/5-D-4) indicated that it specifically recognized an antigenic determinant in the polysaccharide structure of both corneal and skeletal keratan sulfate. Enzyme immunoassay analyses indicated that the mouse monoclonal IgG1 recognized keratan sulfate in native proteoglycan aggregate and proteoglycan monomer preparations isolated from hyaline cartilages of a wide variety of animal species (human, monkey, cow, sheep, chicken, and shark cartilage). The 1/20/5-D-4 monoclonal antibody did not recognize antigenic determinants on proteoglycan isolated from Swarm rat chondrosarcoma. This finding is consistent with several biochemical analyses showing the absence of keratan sulfate in proteoglycan synthesised by this tissue. A variety of substructures isolated after selective cleavage of bovine nasal cartilage proteoglycan (Heinegård, D., and Axelsson, J. (1977) J. Biol. Chem. 252, 1971-1979) were used as competing antigens in radioimmunoassays to characterize the specificity of the 1/20/5-D-4 immunoglobulin. Substructures derived from the keratan sulfate attachment region of the proteoglycan (keratan sulfate peptides) showed the strongest inhibition. Both corneal and skeletal keratan sulfate peptides as competing antigens in radioimmunoassays showed similar inhibition when compared on the basis of their glucosamine content. Therefore, the 1/20/5-D-4 monoclonal antibody appears to recognize a common determinant in their polysaccharide moieties. Chemical desulfation of the keratan sulfate reduced the antigenicity of the glycosaminoglycan. The antibody did not recognize determinants present in dermatan sulfate, heparin, heparin sulfate, or hyaluronic acid.
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Cited by
Developmental changes in heparan sulfate expression: in situ detection with mAbs.
David, G., Bai, X. M., Van der Schueren, B., Cassiman, J. J., & Van den Berghe, H. (1992) · The Journal of cell biology · doi:10.1083/jcb.119.4.961 · Cited by 477
Snow, D. M., Steindler, D. A., & Silver, J. (1990) · Developmental Biology · doi:10.1016/0012-1606(90)90203-u · Cited by 386
Implications of the serine protease HtrA1 in amyloid precursor protein processing
Grau, S., Baldi, A., Bussani, R., Tian, X., Stefanescu, R., Przybylski, M., Richards, P., Jones, S. A., Shridhar, V., Clausen, T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501823102 · Cited by 215
Metadata
- Authors
- Caterson, B., Christner, J. E., & Baker, J. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1983-07
- Volume
- 258
- Issue
- 14
- Pages
- 8848-8854
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1533521663
- Cited by
- 409
- References
- 0
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan. https://app.cochat.ai/papers/10.1016/s0021-9258(18)32133-1
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- Caterson, B., Christner, J. E., & Baker, J. R. (1983). Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibodies to cartilage proteoglycan. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)32133-1
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