Immunolocalization of type III collagen in human articular cartilage                prepared by high-pressure cryofixation, freeze-substitution, and low-temperature                embedding.

Young, Robert D.; Lawrence, Paul A.; Duance, VC; Aigner, Thomas; Monaghan, Paul

doi:10.1177/43.4.7897183

Cited by 23 publications

(18 citation statements)

References 22 publications

(30 reference statements)

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“…Both the collagen and the calcium metabolism are central aspects of cartilage physiology in development, growth, and adulthood. Collagen and calcium processing are altered in OA, contributing to degenerative processes and to pathological tissue remodeling, e.g., the formation of atypical ECM (collagen Types X and III, characteristic for fetal cartilage) and of osteophytes (Schmid and Linsenmayer 1987;Sandell et al 1991;von der Mark et al 1992;Young et al 1995;Vornehm et al 1996).…”

Section: Discussionmentioning

confidence: 99%

Expression of Anchorin CII (Cartilage Annexin V) in Human Young, Normal Adult, and Osteoarthritic Cartilage

Mollenhauer

Mok

King

et al. 1999

J Histochem Cytochem.

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SUMMARYIn its tissue-specific function as a collagen receptor of chondrocytes, cartilage annexin V (anchorin CII) occupies a key position in the organization of the cell-extracellular matrix (ECM) junction for the tissue. The general role of annexin V (Anx V) in other tissues suggests involvement in cellular secretory processes and in regulation of apoptosis. Immunohistochemical analysis of Anx V in growth plate cartilage, confirmed by in situ hybridization, suggests that Anx V is prominently expressed and forms a major constituent of growth plate chondrocytes. Anx V epitopes are also located in the pericellular matrix of hypertrophic cartilage. In adult articular cartilage the expression is downregulated, with the highest levels of immunostaining found in the upper third of the articular cartilage layers and almost no antigen found in the deep layers. Osteoarthritic (OA) cartilage is characterized by a significant upregulation of message and protein throughout the entire depth of the tissue, an accumulation of cytoplasmic annexin V epitopes, and a release of epitopes into the pericellular and interterritorial matrix, in part co-localized with granular structures. Therefore, Anx V expression and tissue distribution may serve as a histological marker for metabolic alterations and for changes in the cellular phenotype associated with OA.

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Section: Discussionmentioning

confidence: 99%

Expression of Anchorin CII (Cartilage Annexin V) in Human Young, Normal Adult, and Osteoarthritic Cartilage

Mollenhauer

Mok

King

et al. 1999

J Histochem Cytochem.

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“…Type III collagen has been consistently found in normal and osteoarthritic human articular cartilage (Wotton and Duance 1994; Young et al 1995), where it colocalizes in the same fibrils with type II collagen (Young et al 2000). Many other types of collagen have been described (at least 27, so far), some of them located in epiphyseal cartilage.…”

Section: Collagenmentioning

confidence: 98%

Biological Calcification

2007

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“…III collagen present as a minor component of articular cartilage (Wotton and Duance 1994;Young et al 1995). Type III collagen has usually been found associated with Type I collagen (Fleischmajer et al 1990).…”

Section: Figurementioning

confidence: 99%

Immunolocalization of Collagen Types II and III in Single Fibrils of Human Articular Cartilage

Young

Lawrence

Duance

et al. 2000

J Histochem Cytochem.

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S U M M A R Y 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 aminopropeptide (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 noncollagenous components of the extracellular matrix.

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Immunolocalization of type III collagen in human articular cartilage prepared by high-pressure cryofixation, freeze-substitution, and low-temperature embedding.

Cited by 23 publications

References 22 publications

Expression of Anchorin CII (Cartilage Annexin V) in Human Young, Normal Adult, and Osteoarthritic Cartilage

Expression of Anchorin CII (Cartilage Annexin V) in Human Young, Normal Adult, and Osteoarthritic Cartilage

Biological Calcification

Immunolocalization of Collagen Types II and III in Single Fibrils of Human Articular Cartilage

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