Type III collagen in normal human articular cartilage

Wotton, S. F.; Duance, Victor Colin

doi:10.1007/bf00160053

Cited by 52 publications

(41 citation statements)

References 19 publications

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“…Collagen type III is consistently detected by immunofluorescence in samples of normal and osteoarthritic human articular cartilage (Aigner et al, 1993;Wotton and Duance, 1994; Fig. 3).…”

Section: Deposition Of Type III Collagen Cross-linked To Type Ii Colmentioning

confidence: 90%

Articular cartilage collagen: an irreplaceable framework?

Eyre

Weis

2006

eCM

235

151

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Adult articular cartilage by dry weight is two-thirds collagen. The collagen has a unique molecular phenotype. The nascent type II collagen fibril is a heteropolymer, with collagen IX molecules covalently linked to the surface and collagen XI forming the filamentous template of the fibril as a whole. The functions of collagens IX and XI in the heteropolymer are far from clear but, evidently, they are critically important since mutations in COLIX and COLXI genes can result in chondrodysplasia syndromes. Here we review what is known of the collagen assembly and present new evidence that collagen type III becomes covalently added to the polymeric fabric of adult human articular cartilage, perhaps as part of a matrix repair or remodelling process.

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“…Collagen type III is consistently detected by immunofluorescence in samples of normal and osteoarthritic human articular cartilage (Aigner et al, 1993;Wotton and Duance, 1994; Fig. 3).…”

Section: Deposition Of Type III Collagen Cross-linked To Type Ii Colmentioning

confidence: 90%

Articular cartilage collagen: an irreplaceable framework?

Eyre

Weis

2006

eCM

235

151

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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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“…In a recent resurgence of interest in the occurrence of Type 111 collagen in cartilage, Wotton and Duance (1994) showed Type I11 also to be a minor component of normal tissue. In osteoarthritis, increased expression of Type 111 collagen, in association with Type I1 collagen biosynthesis but independent of Type I collagen production, was demonstrated by in situ hybridization studies (Aigner et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

“…The major fibrillar component of cartilage is known to be Type I1 collagen. In view of the very small amounts of Type 111 collagen found in cartilage (Wotton and Duance, 1994), the presence of gold labeling on the major interstitial fibrils indicates that, in addition to Types M and XI collagen (Mendler et al, 1989) Type I11 also appears to be a component of the Type I1 fibrils. Further confirmation of this possibility awaits the results of experiments in progress to perform dual immunolocalitation of collagen types on sections of low-temperature processed cartilage specimens.…”

Section: Discussionmentioning

confidence: 99%

“…Sections were treated with bovine testicular hyaluronidase (Sigma Chemicals; Poole, UK) (2 mg/ml) in PBS at 37°C for 1 hr before exposure to primary antibodies diluted in PBS/l% bovine serum albumin (BSA) and either (a) a rabbit polyclonal antibody to pN collagen Type 111, diluted 1:500, or (b) a polyclonal antibody raised in goat to the pepsin-extracted (triple-helical) domain of human Type I11 collagen, at a dilution of 1:lOO. These antibodies are the same as those used previously (Wotton and Duance, 1994;Aigner et al, 1993), and have been extensively characterized by ELISA and Western blotting for crossreactivity to other collagen types and fragments (see Wotton and Duance, 1994;Nowack et al, 1976). Control sections were incubated with PBS/l% BSA alone.…”

Section: Methodsmentioning

confidence: 99%

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