Proteoglycan Association with Collagen<i>d</i>Band in Hyaline Articular Cartilage

Orford, C R; Gardner, D L

doi:10.3109/03008208409013696

Cited by 29 publications

(9 citation statements)

References 23 publications

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“…Evidence in favor of a strong interaction between these two matrix molecules comes from histological, biophysical, and biomechanical experiments. For example, electron microscopy studies, using cationic dyes (36) and immunoassay (37) techniques, have directly observed PG contact points on the collagen fibers. Further support for PG interacting with collagen came from in vitro biomechanical studies by Zhu et al (38).…”

Section: Discussionmentioning

confidence: 99%

Macromolecule and water magnetization exchange modeling in articular cartilage

et al. 2000

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Section: Discussionmentioning

confidence: 99%

Macromolecule and water magnetization exchange modeling in articular cartilage

et al. 2000

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“…While the molecular components of the tissue have been well characterised and many of the collagen-collagen and collagen-proteoglycan interactions described under in vivo and in vitro conditions (Hendrix et al, 1982;Bayliss et al, 1983;Broom and Poole, 1983;Orford and Gardner, 1984;Müller-Glauser et al, 1986;Mendler et al, 1989;Furuto et al, 1991;Poole et al, 1992;Wu et al, 1992;Hagiwara et al, 1993;Hedbom and Heinegárd, 1993;Wotton and Duance, 1994;Weber et al, 1996;Danielson et al, 1997;Hagg et al, 1998), the three dimensional structure of AC is still controversial, due to the variation in preparation methods, imaging techniques and the variety of species in which AC has been studied.…”

Section: The Ultrastructure Of Mouse Articular Cartilage: Collagen Ormentioning

confidence: 99%

“…The main deformation that occurs in the deep zone is in the interterritorial matrix (IM), allowing the cellular columns to slide over and with respect to one another. the region of the tidemark, the weakest point of the cartilage (Fawns and Landells, 1953;Otterness et al, 1999).…”

Section: A Model Of Mouse Acmentioning

confidence: 99%

The ultrastructure of mouse articular cartilage: Collagen orientation and implications for tissue functionality. A polarised light and scanning electron microscope study and review.

Hughes

Archer²,

Gwynn³

2005

eCM

127

120

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Abstract.Adult mouse articular cartilage (AC) has not been thoroughly described using high resolution imaging techniques, despite the fact that the availability of knockout mice with specific extracellular matrix (ECM) mutations have renewed interest in using the mouse as a model for a variety of different human conditions. With osteoarthritis affecting millions of people worldwide, investigations into the structure and, therefore, the ability of AC to act as a load-bearing tissue, are crucial for developing treatments and prevention techniques to limit the degree of severity in this condition. Cryofixation and formaldehyde fixation as well as chemical digestion of the uncalcified regions of AC were used in combination with bright field light, polarised light and scanning electron microscopy to image the structure of adult mouse AC. Chemical digestion of the tissue revealed unique insights into the structure of mouse AC and the high cellular density of the tissue. Tightly packed sheets of collagen fibrils formed the territorial matrix (TM) of the deep zone. These were observed closely surrounding the chondrons, after applying both chemical and cryofixation techniques. The interterritorial matrix (IM), in contrast, was more isotropically arranged. The results of the study have implications for the interpretation of biomechanical functionality of mouse AC with probable applications to other species.

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“…DISCUSSION Previous histochemical studies have indicated a close spatial relationship between proteoglycans and collagen in soft tissues, e.g. in tendon and annulus fibrosus (21) and in articular cartilage (22). Immunohistochemical examination has shown that the small dermatan sulfate proteoglycan decorin is associated with fibrils in tendon (23) and dermis (24), apparently because of interactions between the core protein and collagen.…”

Section: Figmentioning

confidence: 99%

Association of the Aggrecan Keratan Sulfate-rich Region with Collagen in Bovine Articular Cartilage

Hedlund¹,

Hedbom²,

Heinegård³

et al. 1999

Journal of Biological Chemistry

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Aggrecan, the predominant large proteoglycan of cartilage, is a multidomain macromolecule with each domain contributing specific functional properties. One of the domains contains the majority of the keratan sulfate (KS) chain substituents and a protein segment with a proline-rich hexapeptide repeat sequence. The function of this domain is unknown but the primary structure suggests a potential for binding to collagen fibrils. We have examined binding of aggrecan fragments encompassing the KS-rich region in a solid-phase assay. A moderate affinity (apparent K d ‫؍‬ 1.1 M) for isolated collagen II, as well as collagen I, was demonstrated. Enzymatic digestion of the KS chains did not alter the capacity of the peptide to bind to collagen, whereas cleavage of the protein core abolished the interaction. The distribution of the aggrecan KS-rich region in bovine tarsometatarsal joint cartilage was investigated using immunoelectron microscopy. Immunoreactivity was relatively low in the superficial zone and higher in the intermediate and deep zones of the uncalcified cartilage. Within the pericellular and territorial matrix compartments the epitopes representing the aggrecan KSrich region were detected preferentially near or at collagen fibrils. Along the fibrils, epitope reactivity was non-randomly distributed, showing preference for the gap region within the D-period. Our data suggest that collagen fibrils interact with the KS-rich regions of several aggrecan monomers aligned within a proteoglycan aggregate. The fibril could therefore serve as a backbone in at least some of the aggrecan complexes.Articular cartilage matrix can be regarded as a fiber-reinforced composite material (1), where aggrecan complexes are entangled within a network of collagen fibrils. The aggrecan complexes, constituting about 90% of the proteoglycan content (2), endow the matrix with high osmotic pressure, compressive stiffness, and resilience, whereas collagen is essential for the tensile strength of the tissue (3). Different mechanical properties of the composite depend on these major constituents and how they are assembled and stabilized by intermolecular interactions. The capacity of cartilage to withstand mechanical stress depends upon its structural integrity and, hence, numerous interactions between the matrix components. Indeed, the molecules are so tightly associated that most of the tissue constituents require denaturing solvents or proteases for extraction. This has hampered studies of molecular function. To gain insight into the physiology of articular cartilage, it is necessary to identify and characterize interactions between the matrix constituents, particularly those involving the collagen.In the present study we focused on a domain of the aggrecan molecule containing the majority of the keratan sulfate (KS) 1 chain substituents and a protein segment with a hexapeptide repeat sequence (4). The second globular domain (G2) is localized adjacent to this KS-rich region, on the N-terminal side. The first globular domain (G1), which r...

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Proteoglycan Association with CollagendBand in Hyaline Articular Cartilage

Cited by 29 publications

References 23 publications

Macromolecule and water magnetization exchange modeling in articular cartilage

Macromolecule and water magnetization exchange modeling in articular cartilage

The ultrastructure of mouse articular cartilage: Collagen orientation and implications for tissue functionality. A polarised light and scanning electron microscope study and review.

Association of the Aggrecan Keratan Sulfate-rich Region with Collagen in Bovine Articular Cartilage

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