Abstract
Quantitative immunoassays have been developed to measure the content, degradation, and synthesis of types II and IX collagens in hyaline cartilages. Some of these assays and their applications are described in this chapter. These and other assays are commercially available. The applications of these assays are discussed with examples from recent publications.
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References
Billinghurst, R. C., Dahlberg, L., Ionescu, M. et al. (1997) Enhanced cleavage of type II collagen by collagenases in osteoarthritic articular cartilage. J. Clin. Invest. 99, 1534–1545.
Hollander, A. P., Heathfield, T. F., Webber, C., et al. (1994) Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay. J. Clin. Invest. 93, 1722–1732.
Nelson F, Dahlberg L, Laverty, S., Reiner et al. (1998) Evidence for altered synthesis of type II collagen in patients with osteoarthritis. J. Clin. Invest. 102, 2115–2125.
Mwale, F., Billinghurst, C., Wu, W., et al. (2000) Selective assembly and remodelling of collagens II and IX associated with expression of the chondrocyte hypertrophic phenotype. Dev. Dyn. 218, 648–662.
Billinghurst, R. C., Buxton, E. M., Edwards, M. G., McGraw, M. S., and McIlwraith, C. W. (2001) Use of an antineoepitope antibody for identification of type-II collagen degradation in equine articular cartilage. Am. J. Vet. Res. 62, 1031–1039.
Dahlberg, L., Billinghurst, R. C., Manner, P., et al. (2000) Selective enhancement of collagenase-mediated cleavage of resident type II collagen in cultured osteoarthritic cartilage and arrest with a synthetic inhibitor that spares collagenase 1 (matrix metalloproteinase 1). Arthritis Rheum. 43, 673–682.
Billinghurst, R. C., O’Brien, K., Poole, A. R., and McIlwraith, C. W. (1999) Inhibition of articular cartilage degradation in culture by a novel nonpeptidic matrix metalloproteinase inhibitor. N. Y. Acad. Sci. 878, 594–597.
Billinghurst, R. C., Wu, W., Ionescu, M., et al. (2000) Comparison of the degradation of type II collagen and proteoglycan in nasal and articular cartilages by interleukin-1 and the selective inhibition of type II collagen cleavage by collagenase. Arthritis Rheum. 43, 664–672.
Laverty, S., O’Kouneff, S., Ionescu, M., et al. (2002) Excessive degradation of type II collagen in articular cartilage in equine osteochondrosis. J. Orthop. Res. 20, 1282–1289.
Hollander, A. P., Heathfield, T. F., Liu, J. J., et al. (1996) Enhanced denaturation of the α1(II) chains of type-II collagen in normal adult human intervertebral discs compared with femoral articular cartilage. J. Orthop. Res. 14, 61–66.
Antoniou, J., Steffen, T., Nelson, F., et al. (1996) The human intervertebral disc. Evidence for changes in the biosynthesis and denaturation of the extracellular matrix with growth, maturation, ageing and degeneration. J. Clin. Invest. 98, 996–1003.
Squires, G., Okouneff, S., Ionescu, M., and Poole, A. R. (2003) Pathobiology of focal lesion development in aging human articular cartilage reveals molecular matrix changes characteristic of osteoarthritis. Arthritis Rheum. 48, 1261–1270.
Miller, E. J. (1971) Isolation and characterization of a collagen from chick cartilage containing three identical achains. Biochemistry 10, 1652–1659.
ChandraRajan, J. (1978) Separation of type III collagen from type I collagen and pepsin by differential denaturation and renaturation. Biochem. Biophys. Res. Commun. 83, 180–186.
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© 2004 Humana Press Inc., Totowa, NJ
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Billinghurst, R.C., Mwale, F., Hollander, A., Ionescu, M., Poole, A.R. (2004). Immunoassays for Collagens in Chondrocyte and Cartilage Explant Cultures. In: Sabatini, M., Pastoureau, P., De Ceuninck, F. (eds) Cartilage and Osteoarthritis. Methods in Molecular Medicine™, vol 100. Humana Press. https://doi.org/10.1385/1-59259-810-2:251
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DOI: https://doi.org/10.1385/1-59259-810-2:251
Publisher Name: Humana Press
Print ISBN: 978-1-58829-247-6
Online ISBN: 978-1-59259-810-6
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