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Immunolocalization of collagen Types II and III in single fibrils of human articular cartilage

Young, Robert David ORCID: https://orcid.org/0000-0002-8300-8002, Lawrence, Paul A., Duance, Victor Colin ORCID: https://orcid.org/0000-0002-7555-2016, Aigner, Thomas and Monaghan, Paul 2000. Immunolocalization of collagen Types II and III in single fibrils of human articular cartilage. Journal of Histochemistry and Cytochemistry 48 (3) , pp. 423-432. 10.1177/002215540004800312

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Abstract

Type II and III fibrillar collagens were localized by immunogold electron microscopy in resin sections of human femoral articular cartilage taken from the upper radial zone in specimens from patients with osteoarthritis. Tissue samples stabilized by high-pressure cryofixation were processed by freeze-substitution, either in acetone containing osmium or in methanol without chemical fixatives, before embedding in epoxy or Lowicryl resin, respectively. Ultrastructural preservation was superior with osmium-acetone, although it was not possible to localize collagens by this method. In contrast, in tissue prepared by low-temperature methods without chemical fixation, collagens were successfully localized with mono- or polyclonal antibodies to the helical (Types II and III) and amino-propeptide (Type III procollagen) domains of the molecule. Dual localization using secondary antibodies labeled with 5- or 10-nm gold particles demonstrated the presence of Types II and III collagen associated within single periodic banded fibrils. Collagen fibrils in articular cartilage are understood to be heteropolymers mainly of Types II, IX, and XI collagen. Our observations provide further evidence for the complexity of these assemblies, with the potential for interactions between at least 11 distinct collagen types as well as several non-collagenous components of the extracellular matrix.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Optometry and Vision Sciences
Neuroscience and Mental Health Research Institute (NMHRI)
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QR Microbiology > QR180 Immunology
Publisher: The Histochemical Society
ISSN: 0022-1554
Last Modified: 28 Oct 2022 08:29
URI: https://orca.cardiff.ac.uk/id/eprint/70991

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