The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain.
Open accessAbstract
Synovial fluid was collected from patients with recent knee injury and from patients with early or late stage osteoarthritis. Chondroitin sulfate-substituted aggrecan fragments present in these fluids, and in normal bovine synovial fluid, were purified by cesium chloride gradient centrifugation, enzymically deglycosylated and fractionated by gel filtration on Superose-12. Each sample contained two major aggrecan core protein populations with apparent molecular masses of approximately 90 kD and 150 kD. For all samples, NH2-terminal analysis of both populations gave a single major sequence beginning ARGSV. This NH2 terminus results from cleavage of the human aggrecan core protein at the Glu 373-Ala 374 bond within the interglobular domain between the G1 and G2 domains. Cleavage at this site also occurs during control and interleukin-1 stimulated aggrecan catabolism in bovine cartilage explant cultures (Sandy, J., P. Neame, R. Boynton, and C. Flannery. 1991. J. Biol. Chem. 266:8683-8685). These results indicate that the major aggrecan fragments present in both osteoarthritic human synovial fluid and in normal bovine synovial fluid are large, being composed of a short NH2-terminal stretch of the interglobular domain, the G2 domain, the keratan sulfate domain, and variable lengths of the chondroitin sulfate domain(s). We conclude that the release of aggrecan fragments from articular cartilage into the synovial fluid seen at all stages of human osteoarthritis (Lohmander, L. S. 1991. Acta Orthop. Scand. 62:623-632) is promoted by the action of a normal cartilage proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain.
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Cites
A Direct Spectrophotometric Microassay for Sulfated Glycosaminoglycans in Cartilage Cultures
Farndale, R. W., Sayers, C. A., & Barrett, A. J. (1982) · Connective Tissue Research · doi:10.3109/03008208209160269 · Cited by 1,347
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Doege, K. J., Sasaki, M., Kimura, T., & Yamada, Y. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35257-2 · Cited by 446
MacNaul, K. L., Chartrain, N., Lark, M., Tocci, M. J., & Hutchinson, N. I. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44894-0 · Cited by 399
Lohmander, L. S., Hoerrner, L. A., & Lark, M. W. (1993) · Arthritis & Rheumatism · doi:10.1002/art.1780360207 · Cited by 339
Self-citationSandy, J. D., Neame, P. J., Boynton, R. E., & Flannery, C. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31499-6 · Cited by 284
Self-citationFlannery, C. R., Lark, M. W., & Sandy, J. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48387-1 · Cited by 270
Self-citationFirestein, G. S., Paine, M. M., & Littman, B. H. (1991) · Arthritis & Rheumatism · doi:10.1002/art.1780340905 · Cited by 257
Expression of Metalloproteinases and Metalloproteinase Inhibitor in Human Arthritic Synovium
Spence Mccachren, S. (1991) · Arthritis & Rheumatism · doi:10.1002/art.1780340904 · Cited by 210
Cited by
Matrix Metalloproteinases: Role In Arthritis
Burrage, P. (2006) · Frontiers in Bioscience · doi:10.2741/1817 · Cited by 1,292
Deletion of active ADAMTS5 prevents cartilage degradation in a murine model of osteoarthritis
Glasson, S. S., Askew, R., Sheppard, B., Carito, B., Blanchet, T., Ma, H.-L., Flannery, C. R., Peluso, D., Kanki, K., Yang, Z., et al. (2005) · Nature · doi:10.1038/nature03369 · Cited by 1,253
Self-citationOhuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M., & Okada, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2446 · Cited by 938
Structure and function of aggrecan
KIANI, C., CHEN, L., WU, Y. J., YEE, A. J., & YANG, B. B. (2002) · Cell Research · doi:10.1038/sj.cr.7290106 · Cited by 758
Purification and Cloning of Aggrecanase-1: A Member of the ADAMTS Family of Proteins
Tortorella, M. D., Burn, T. C., Pratta, M. A., Abbaszade, I., Hollis, J. M., Liu, R., Rosenfeld, S. A., Copeland, R. A., Decicco, C. P., Wynn, R., et al. (1999) · Science · doi:10.1126/science.284.5420.1664 · Cited by 686
Metadata
- Authors
- Sandy, J. D., Flannery, C. R., Neame, P. J., & Lohmander, L. S.
- Venue
- Journal of Clinical Investigation
- Published
- 1992-05-01
- Volume
- 89
- Issue
- 5
- Pages
- 1512-1516
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W2114769400
- Cited by
- 411
- References
- 21
- FWCI
- 15.81
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Sandy, J. D., Flannery, C. R., Neame, P. J., & Lohmander, L. S. (1992). The structure of aggrecan fragments in human synovial fluid. Evidence for the involvement in osteoarthritis of a novel proteinase which cleaves the Glu 373-Ala 374 bond of the interglobular domain. Journal of Clinical Investigation. https://doi.org/10.1172/jci115742
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