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The Different Roles of Aggrecan Interaction Domains [PDF]
Journal of Histochemistry and Cytochemistry, 2012 The aggregating proteoglycans of the lectican family are important components of extracellular matrices. Aggrecan is the most well studied of these and is central to cartilage biomechanical properties and skeletal development. Key to its biological function is the fixed charge of the many glycosaminoglycan chains, that provide the basis for the ...
Anders Aspberg
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Matrix Biology, 1994
Large proteoglycans were purified by ion-exchange chromatography, gel filtration and CsCl gradient centrifugation from the compressed and tensional regions of adult bovine deep flexor tendon. Tryptic peptide maps of proteoglycan from the compressed region were very similar to maps of aggrecan from bovine articular cartilage, with evidence for the ...
K G, Vogel +3 more
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Large proteoglycans were purified by ion-exchange chromatography, gel filtration and CsCl gradient centrifugation from the compressed and tensional regions of adult bovine deep flexor tendon. Tryptic peptide maps of proteoglycan from the compressed region were very similar to maps of aggrecan from bovine articular cartilage, with evidence for the ...
K G, Vogel +3 more
openaire +2 more sources
Aggrecanase and Aggrecan Degradation in Osteoarthritis: A Review
Journal of International Medical Research, 2008 Aggrecanase-mediated aggrecan degradation is a significant event in early-stage osteoarthritis (OA). Aggrecanases belonging to the ‘A Disintegrin And Metalloproteinase with ThromboSpondin motifs’ (ADAMTS) family of proteinases play a significant role in aggrecan depletion in osteoarthritic cartilage.
K, Huang, L D, Wu
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Journal of Bone and Mineral Metabolism, 2000
terminal globular (G)1 domain and a C-terminal G3 domain that are joined by intervening nonglobular sequences of lengths characteristic for each core protein. In addition, the aggrecan core protein has a G2 domain. The G1, G2, and G3 domains each contain distinctive motifs, with each motif having its own folded structure (Fig. 1).
W, Luo +6 more
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terminal globular (G)1 domain and a C-terminal G3 domain that are joined by intervening nonglobular sequences of lengths characteristic for each core protein. In addition, the aggrecan core protein has a G2 domain. The G1, G2, and G3 domains each contain distinctive motifs, with each motif having its own folded structure (Fig. 1).
W, Luo +6 more
openaire +2 more sources
Aggrecan: Beyond cartilage and into the brain
The International Journal of Biochemistry & Cell Biology, 2012Aggrecan is well-studied in cartilage but its expression and function in the central nervous system has only recently begun to be appreciated. Aggrecan plays an important role in the organization of the neural extracellular space by binding and organizing hyaluronan to the cell surface through interactions with link protein and tenascins forming a ...
Morawski, M. +3 more
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Synthesis and characterization of an aggrecan mimic
Acta Biomaterialia, 2012Aggrecan (AGG) is a large, aggregating proteoglycan present throughout the body, but predominantly found in articular cartilage. The principle features of AGG, its hyaluronan (HA) binding domain and its abundance of covalently attached glycosaminoglycans (GAGs), make it an essential component of the functional ability of articular cartilage.
Jonathan C, Bernhard, Alyssa, Panitch
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Compressive nanomechanics of opposing aggrecan macromolecules
Journal of Biomechanics, 2006In this study, we have measured the nanoscale compressive interactions between opposing aggrecan macromolecules in near-physiological conditions, in order to elucidate the molecular origins of tissue-level cartilage biomechanical behavior. Aggrecan molecules from fetal bovine epiphyseal cartilage were chemically end-grafted to planar substrates ...
Delphine Dean, Lin Han, Christine Ortiz
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