Effect of Decorin and Dermatan Sulfate on the Mechanical Properties of a Neocartilage

REFERENCES

• Roughly, P.J. (2006). The structure and function of cartilage proteoglycans. Euro. Cells Mater., 12, 92–101.
   PubMed Web of Science ®Google Scholar
• Poole, A.R., Rosenberg, L.C., Reiner, A., Ionescu, M., Bogoch, E., and Roughley, P.J. (1996). Contents and distributions of the proteoglycans decorin and biglycan in normal and osteoarthritic human articular cartilage. J. Orthop. Res., 14(5), 681–689.
   PubMed Web of Science ®Google Scholar
• Scott, J.E. (1992). Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues. FASEB, 6, 2639–2645.
   PubMed Web of Science ®Google Scholar
• Moscatello, D.K., Santra, M., Mann, D.M., McQuillan, D.J., Wong, A.J., and Iozzo, R.V. (1998). Decorin suppresses tumor cell growth by activating the epidermal growth factor receptor. J. Clin. Invest., 101(2), 406–412.
   PubMed Web of Science ®Google Scholar
• Ferdous, Z., Wei, V.M., Iozzo, R., Hook, M., and Grande-Allen, K.J. (2007). Decorin-transforming growth factor-β interaction regulate matrix organization and mechanical characteristics of three-dimensional collagen matrices. J. Biol. Chem., 282(49), 35887–35898.
   PubMed Web of Science ®Google Scholar
• Kokenyesi, R., and Woessner, Jr, J.F. (1990). Relationship between dilatation of the rat uterine cervix and a small dermatan sulfate proteoglycan. Biol. Reprod., 42, 87–97.
   PubMed Web of Science ®Google Scholar
• Gotte, M., and Kresse, H. (2005). Defective glycosaminoglycan substitution of decorin in a patient with progeroid syndrome is a direct consequence of two point mutations in the galactosyltransferase I (β4GalT-7) gene. Biochem. Gen., 43(1), 65–77.
   PubMed Web of Science ®Google Scholar
• Seidler, D.G., (2006). Defective glycosylation of decorin and biglycan, altered collagen structure, and abnormal phenotype of the skin fibroblasts of an Ehlers-Danlos syndrome patient carrying the novel Arg270Cys substitution in galactosyltransferase I (β4GalT-7). J. Mol. Med., 84, 583–594.
   PubMed Web of Science ®Google Scholar
• Vogel, K.G., and Trotter, J.A. (1987). The effects of proteoglycans on the morphology of collagen fibrils formed in vitro. Collagen Rel. Res., 7, 105–114.
   PubMedGoogle Scholar
• Iwasaki, S., (2008). The modulation of collagen fibril assembly and its structure by decorin: an electron microscopic study. Arch. Histol. Cytol., 71(1), 37–44.
   PubMed Web of Science ®Google Scholar
• Ruhland, C., (2007). The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis. FEBS J., 274, 4246–4255.
   PubMed Web of Science ®Google Scholar
• Raspanti, M., Viola, M., Sonaggere, M., Tira, M.E., and Tenni, R. (2007). Collagen fibril structure is affected by collagen concentration and decorin. Biomacromolecules, 8, 2087–2091.
   PubMed Web of Science ®Google Scholar
• Zhang, G., (2006). Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development. J. Cell Biochem., 98, 1436–1449.
   PubMed Web of Science ®Google Scholar
• Nakamura, N., (2000). Decorin antisense gene therapy improves functional healing of early rabbit ligament scar with enhanced collagen fibrillogenesis in vivo. J. Orthop. Res., 18, 517–523.
   PubMed Web of Science ®Google Scholar
• Scott, J.E., and Stockwell, R.A. (2006). Cartilage elasticity resides in shape module decoran and aggrecan sumps of damping fluid: implications in osteoarthrosis. J. Physiol., 574, 643–650.
   PubMed Web of Science ®Google Scholar
• Redaelli, A., Vesentini, S., Soncini, M., Vena, P., Mantero, S., and Montevecchi, F.M. (2003). Possible role of decorin glycosaminoglycans in fibril to fibril force transfer in relative mature tendons—a computational study from molecular to microstructural level. J. Biomech., 36, 1555–1569.
   PubMed Web of Science ®Google Scholar
• Liu, X., Yeh M.-L., Lewis, J.L., and Luo, Z.-P. (2005). Direct measurement of the rupture force of single pair of decorin interactions. Biochem. Biophys. Res. Commun., 338, 1342–1345.
   PubMed Web of Science ®Google Scholar
• Elliott, D.M., Robinson, P.S., Gimbel, J.A., (2003). Effect of altered matrix proteins on quasilinear viscoelastic properties in transgenic mouse tail tendons. Ann. Biomed. Eng., 31, 599–605.
   PubMed Web of Science ®Google Scholar
• Robinson, P.S., Lin, T.W., Reynolds, P.R., Derwin, K.A., Iozzo, R.V., and Soslowsky, L.J. (2004). Strain rate sensitive mechanical properties of tendon fascicles from mice with genetically engineered alterations in collagen and decorin. J. Biomech. Engr., 126, 252–257.
   PubMed Web of Science ®Google Scholar
• Lujan, T.J., Underwood, C.J., Henninger, H.B., Thompson, B.M., and Weiss, J.A. (2007). Effect of dermatan sulfate glycosaminoglycans on the quasi-static material properties of the human medial collateral ligament. J. Orthop. Res., online pub DOI 10.1002/jor.20351.
   PubMed Web of Science ®Google Scholar
• Hall, M.L., Krawczak, D.A., Simha, N.K., and Lewis, J.L. (2008). Effect of dermatan sulfate on the indentation and tensile properties of articular cartilage. Osteoarthr. Cart., in press.
   Google Scholar
• Fedewa, M.M., Oegema, T.R., Jr, Schwartz, M.H., MacLeod, A., and Lewis, J.L. (1998). Chondrocytes in culture produce a mechanically functional tissue. J. Orthop. Res., 16, 227–236.
   PubMed Web of Science ®Google Scholar
• Masuda, K., Sah, R.L., Hejna, M.J., and Thonar, E.J. (2003). A novel two-step method for the formation of tissue-engineered cartilage by mature bovine chondrocytes: the alginate-recovered-chondrocyte (ARC) method. J. Orthop. Res., 21(1), 139–48.
   PubMed Web of Science ®Google Scholar
• Krusius, T., andRuoslahti, E. (1986). Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA. Proc. Nat. Acad. Sci. USA. 83, 7683–7687.
   PubMed Web of Science ®Google Scholar
• Schroeder, T.M., Kahler, R.A., Li, X., and Westendorf, J.J. (2004). Histone deacetylase 3 interacts with runx2 to repress the osteocalcin promoter and regulate osteoblast differentiation. J. Biol. Chem., 279, 41998–42007.
   PubMed Web of Science ®Google Scholar
• Kahler, R.A., and Westendorf, J.J. (2003). Lymphoid enhancer factor-1 and beta-catenin inhibit Runx2-dependent transcriptional activation of the osteocalcin promoter. J. Biol. Chem., 278, 11937–11944.
   PubMed Web of Science ®Google Scholar
• Chandrasekhar, S., Esterman, M., and Hoffman, H. (1987). Microdetermination of proteoglycans and glycosaminoglycans in the presence of guanidine hydrochloride. Anal. Biochem., 161, 103.
   PubMed Web of Science ®Google Scholar
• Labarca, C., and Paigen, K. (1980). A simple, rapid, and sensitive DNA assay procedure. Anal. Biochem., 102, 344.
   PubMed Web of Science ®Google Scholar
• Keane, M., Belperio, J., Arenberg, D., Burdick, M., Xu, Z., Xue, Y., and Strieter, R. (1999). IFN-gamma-inducible protein-10 attenuates bleomycin-induced pulmonary fibrosis via inhibition of angiogenesis. J. Immunol., 163, 5686.
   PubMed Web of Science ®Google Scholar
• Scott, P.G., Dodd, C.M., and Pringle, G.A. (1993). Mapping the locations of the epitopes of five monoclonal antibodies to the core protein of dermatan sulfate proteoglycan II (decorin). J. Biol. Chem., 268(16), 11558–11564.
   PubMed Web of Science ®Google Scholar
• Wardale, R., and Duance, V. (1993). Quantification and immunolocalisation of porcine articular and growth plate cartilage collagens. J. Cell Sci., 105, 975.
   PubMed Web of Science ®Google Scholar
• Reno, C., Marchuk, L., Sciore, P., Frank, C., and Hart, D. (1997). Rapid isolation of total RNA from small samples of hypocellular, dense connective tissues. Biotechniques, 22, 1082.
   PubMed Web of Science ®Google Scholar
• Lewis, J.L., Johnson, S.L., and Oegema, Jr, T.R. (2002). Interfibrillar collagen binding exists in matrix produced by chondrocytes in culture: evidence by electron microscopy. Tissue Eng., 8, 989–995.
   PubMedGoogle Scholar
• Hayes, W.C., Keer, L.M., Hermann, G., and Mockros, L.F. (1972). A mathematical analysis for indentation tests of articular cartilage. J. Biomech., 5, 541–551.
   PubMed Web of Science ®Google Scholar
• Chiravarambath, S., Simha, N.K., Namani, R., and Lewis, J.L. (2008). Poroviscoelastic cartilage properties in the mouse from indentation. J. Biomech. Engr., in press.
   Web of Science ®Google Scholar
• Scott, J.E. (2003). Elasticity in extracellular matrix ‘shape modules’ of tendon, cartilage etc. A sliding proteoglycan-filament model. J. Physiol., 553, 335–343.
   PubMed Web of Science ®Google Scholar
• Pins, G.D., Christiansen, D.L., Patel, R., and Silver, F.H. (1997). Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophys. J., 73, 2164–2172.
   PubMed Web of Science ®Google Scholar
• Vogel, K.G., Paulsson, M., andHeinegard, D. (1984). Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem. J., 223, 587–597.
   PubMed Web of Science ®Google Scholar
• Kempson, B.E., Tuke, M.A., Dingle, J.T., Barrett, A.J., and Horsfield, P.H. (1976). The effects of proteolytic enzymes on the mechanical properties of adult human articular cartilage. Biochi. Biophy. Acta, 428, 741–760.
   PubMed Web of Science ®Google Scholar
• DiSilvestro, M.R., and Suh, J.-K.F. (2002). Biphasic poroviscoelastic characteristics of proteoglycan-depleted articular cartilage: simulation of degeneration. Anals Biomed. Engr., 30, 792–800.
   PubMed Web of Science ®Google Scholar
• Laasanen, M.S., (2003). Biomechanical properties of knee articular cartilage. Biorheology, 40, 133–140.
   PubMed Web of Science ®Google Scholar
• Simha, N.K., Fedewa, M., Leo, P.H., Lewis, J.L., and Oegema T. (1999). A composites theory predicts the dependence of stiffness of cartilage culture tissues on collagen volume fraction. J. Biomech., 32, 503–509.
   PubMed Web of Science ®Google Scholar
• Danielson, K.G., Baribault, H., Holmes, D.F., Graham, H., Kadler, K.E., and Iozzo, R.V. (1997). Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol., 136, 729–743.
   PubMed Web of Science ®Google Scholar
• Galois, L., (2006). Bovine chondrocyte behavior in three-dimensional type I collagen gel in terms of gel contraction, proliferation and gene expression. Biomaterials, 27, 79–90.
   PubMed Web of Science ®Google Scholar
• Budde, M., (2005). Altered integration of Matrilin-3 into cartilage extracellular matrix in the absence of collagen IX. Mol. Cell Biol., 25(23), 10465–10478.
   PubMed Web of Science ®Google Scholar
• Sandell, L.J., Heinegard, D., and Hering, T.M. (2007). Cell biology, biochemistry, and molecular biology of articular cartilage in osteoarthritis. In Osteoarthritis. 4th ed., Moskowitz, R.W., Altman, R.D., Hochberg, M.C., Buckwalter, J.A., and Goldberg, V.M. ( eds.) pp. 73–106. Lippincott Williams and Wilkins, Philadelphia.
   Google Scholar
• Witsch-Prehm, P., Miehlke, R., and Kresse, H. (1992). Presence of small proteoglycan fragments in normal and arthritic human cartilage. Arth. Rheum., 35(9), 1042–1052.
   PubMed Web of Science ®Google Scholar
• Cs-Szabo, G., Roughley, P.J., Plass, A.H.K., and Glant, T.T. (1995). Large and small proteoglycans of osteoarthritic and rheumatoid articular cartilage. Arth. Rheum., 38, 660–668.
   PubMed Web of Science ®Google Scholar
• Robinson, P.S., Huang, T.-F., Kazam, E., Iozzo, R.V., Birk, D.E., and Soslowsky, L.J. (2005). Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice. J. Biomech. Engr., 127, 181–185.
   PubMed Web of Science ®Google Scholar