Enhanced denaturation of the α1(II) chains of type‐II collagen in normal adult human intervertebral discs compared with femoral articular cartilage
- 1 January 1996
- journal article
- research article
- Published by Wiley in Journal of Orthopaedic Research
- Vol. 14 (1) , 61-66
- https://doi.org/10.1002/jor.1100140111
Abstract
The mechanical strength of connective tissues is dependent on the integrity of their fibrillar collagen frameworks. The objective of the present study was to assess type‐II collagen damage (denaturation) in the adult human intervertebral disc compared with articular cartilage, in order to determine whether damage to this molecule may vary in different anatomical sites in the same person. A new immunochemical assay was used to measure the amounts of denatured and total type‐II collagen in the annulus fibrosus and nucleus pulposus of the L5‐S1 disc and in cartilage from the femoral condyles of the same individuals (n = 7). Denaturation of type‐II collagen was significantly higher in both the annulus fibrosus and the nucleus pulposus than in articular cartilage. Such increased damage to type‐II collagen in the adult disc may have relevance to the more pronounced degenerative changes observed in this tissue compared with articular cartilage.Keywords
This publication has 17 references indexed in Scilit:
- Increased damage to type II collagen in osteoarthritic articular cartilage detected by a new immunoassay.Journal of Clinical Investigation, 1994
- 1991 Volvo Award in Basic SciencesSpine, 1991
- Age Changes to the Anulus Fibrosus in Human Intervertebral DiscsSpine, 1991
- Human cartilage is degraded by rheumatoid arthritis synovial fluid but not by recombinant cytokines in vitroClinical and Experimental Immunology, 1991
- Preliminary Evaluation of a Scheme for Grading the Gross Morphology of the Human Intervertebral DiscSpine, 1990
- Immunohistochemical detection and immunochemical analysis of type II collagen degradation in human normal, rheumatoid, and osteoarthritic articular cartilages and in explants of bovine articular cartilage cultured with interleukin 1.Journal of Clinical Investigation, 1989
- Copper-H2O2 oxidation strikingly improves silver intensification of the nickel-diaminobenzidine (Ni-DAB) end-product of the peroxidase reaction.Journal of Histochemistry & Cytochemistry, 1988
- Human intervertebral disc: Structure and functionThe Anatomical Record, 1988
- Degeneration and the chemical composition of the human lumbar intervertebral discJournal of Orthopaedic Research, 1987
- Localization of proteoglycan monomer and link protein in the matrix of bovine articular cartilage: An immunohistochemical study.Journal of Histochemistry & Cytochemistry, 1980