Aggrecan from bovine articular cartilage 

Major structural proteoglycan of cartilage extracellular matrix. Large proteoglycan with a molecular weight greater than 2,500 kDa. Approximately 100-150 glycosaminoglycan (GAG) chains are attached to the core protein (210-250 kDa). The majority of the GAG chains are chondroitin/dermatan sulfate with the remainder being keratan sulfate. This structural molecule produces a rigid, reversibly deformable gel that resists compression. It combines with hyaluronic acid to form very large macromolecular complexes. Addition of small amounts (0.1-2% w/w) of hyaluronic acid to an aggrecan solution (2mg/ml) results in the formation of a complex with an increased hydrodynamic volume and in a significant increase (30-40%) in the relative viscosity of the solution. Aggrecan is a critical component for cartilage structure and the function of joints. The synthesis and degradation of aggrecan are being investigated for their roles in cartilage deterioration during joint injury, disease, and aging. Contains three globular domains, G1, G2, and G3, that are involved in aggregation and hyaluronan binding, cell adhesion, and chondrocyte apoptosis.

Proteoglycans are extracted from articular cartilage with guanidine hydrochloride. Further purification includes gel filtration and ion exchange chromatography. The product is dialyzed against water and sterile-filtered prior to lyophilization.

lyophilized powder

salt, essentially free

white

H₂O: 2 mg/mL

cow ... AGC1(280985)

−20°C

Doege, K.J., Kreis, T., and Vale, R., ed. Guidebook to the Extracellular Matrix and Adhesion Proteins Oxford, UK , (1993), 17-18

Watanabe, H, et al., Identification of hyaluronan-binding domains of aggrecan. J. Biol. Chem. 272(44), 28057-28065, (1997)

Hardingham, TE, et al., The structure, function and turnover of aggrecan, the large aggregating proteoglycan from cartilage. Eur. J. Clin.Chem. Clin. Biochem. 32(4), 249-257, (1994)

Cao, L, et al., Expression of the G1 domain of aggrecan interferes with chondrocyte attachment and adhesion. Matrix Biol. 17(5), 379-392, (1998)

Ishiguro, et al., Relationship of matrix metalloproteinases and their inhibitors to cartilage proteoglycan and collagen turnover: analyses of synovial fluid from patients with osteoarthritis. Arthritis Rheum. 42, 129-136, (1999) abstract

Billington, C.J., et al., An aggrecan-degrading activity associated with chondrocyte membranes. Biochem. J. 336, 207-12, (1998) abstract

Arner, E.C., et al., Generation and Characterization of Aggrecanse A solublecartilage-derived aggrecan-degrading activity. J. Biol. Chem. 274, 6594-6601, (1999) abstract

Bolton, M.C., et al., Age-related changes in the synthesis of link protein and aggrecan in human articular cartilage: implications for aggregate stability. Biochem. J. 337, 77-82, (1999) abstract

Cao, L., and Yang, B.B., Chondrocyte apoptosis induced by aggrecan G1 domain as a result of decreased cell adhesion. Exp. Cell Res. 246, 527-537, (1999) abstract

Hedlund, H., et al., Association of the aggrecan keratan sulfate-rich region with collagen in bovine articular cartilage. J. Biol. Chem. 274, 5777-5781, (1999) abstract

Hardingham, T.E. and Muir, H. Biochim. Biophys. Acta 279, 401-405, (1972) abstract

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