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Cartilage: Biomimetic Study of the Extracellular Matrix

Published online by Cambridge University Press:  15 January 2014

Chinedu I. Anyaeji
Affiliation:
Section on Tissue Biophysics and Biomimetics, Program in Pediatric Imaging and Tissue Sciences, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
Peter J. Basser
Affiliation:
Section on Tissue Biophysics and Biomimetics, Program in Pediatric Imaging and Tissue Sciences, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
Ferenc Horkay
Affiliation:
Section on Tissue Biophysics and Biomimetics, Program in Pediatric Imaging and Tissue Sciences, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
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Abstract

Cartilage is a complex biological tissue that exhibits gel-like behavior. Its primary biological function is providing compressive resistance to external loading and nearly frictionless lubrication of joints. In this study, we model cartilage extracellular matrix using a biomimetic system. We demonstrate that poly(vinyl) alcohol (PVA) hydrogels are robust biomaterials exhibiting mechanical and swelling properties similar to that of cartilage extracellular matrix. A comparison is made between the macroscopic behavior of PVA gels and literature data reported for cartilage.

Type
Articles
Copyright
Copyright © Materials Research Society 2014 

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References

REFERENCES

Mow, V.C., Zhu, W. and Ratcliffe, A., Structure and function of articular cartilage and meniscus, in Basic Orthopedic Biomechanics, eds. Mow, V.C., and Hayes, W.C., Raven Press, New York, 1991.Google Scholar
Campbell, N.A., Reece, J.A. and Simon, E.J., Essential Biology with Physiology (2nd Edition), San Francisco: Jossey Bass, 2004.Google Scholar
Dijkgraaf, L.C., De Bont, L.G.M., Boering, G. and Liem, R.S.B., Normal cartilage structure, biochemistry, and metabolism. Journal of Oral and Maxilofacial Surgery 53, 924929 (1995).CrossRefGoogle ScholarPubMed
Hansson, T.. Öberg, T., Carlsson, G.E. and Kopp, S.: Thickness of the soft tissue layers and the articular disk in the temporomandibular joint. Acta Odontologica Scandinavica 35, 7783 (1977).CrossRefGoogle ScholarPubMed
Ogston, A.G., Intracellular Matrix: The Biological Functions of the Glycosaminoglycans (Andre, A. B., Ed.), Vol. 3, Academic Press, New York, 1970.Google Scholar
Van der Rest, M., and Mayne, R., Type IX collagen proteoglycan from cartilage is covalently cross-linked to type II collagen. J. Biot. Chem. 263, 16151618 (1988).Google ScholarPubMed
Poole, A.R., Pidoux, I., Reiner, A. and Rosenberg, L.. An immunoelectron microscope study of the organization of proteoglycan monomer, link protein, and collagen in the matrix of articular cartilage. J. Cell Biol. 93, 921937 (1982).CrossRefGoogle ScholarPubMed
Heinegard, D. and Hascall, V.C.. Aggregation of cartilage proteoglycans III. Characteristics of the proteins isolated from trypsin digest of aggregates. J. BioL. Chem. 249, 42504256 (1974).Google Scholar
Tang, L.H., Rosenberg, L., Reiner, A. and Poole, A.R., Proteoglycans from bovine nasal cartilage. Properties of a soluble form of link protein. J. Biol. Chem. 25, 1052310531 (1979).Google Scholar
Mow, V.C., Zhu, W., Lai, W.M., Hardingham, T.E., Hughes, C. and Muir, H., The influence of link protein stabilization on the viscometric properties of proteoglycan aggregate solutions. Biochim. Biophys. Acta 992, 201208 (1989).Google Scholar
Neame, P.J., Christner, J.E. and Baker, J.R., Cartilage proteoglycan aggregates. The link protein and proteoglycan amino-terminal globular domains have similar structures. J. BioL. Chem. 262, 1776817778 (1987).Google ScholarPubMed
Schinagl, R.M., Gurskis, D., Chen, A.C. and Sah, R.L., Depth-dependent confined compression modulus of full-thickness bovine articular cartilage. Journal of Orthopaedic Research 15, 499506 (1997).CrossRefGoogle ScholarPubMed
Bloebaum, R.D. and Wilson, A.S., The morphology of the surface of articular cartilage in adult rats. Journal of Anatomy 131, 333346 (1980).Google ScholarPubMed
Guilak, F., Ratcliffe, A., Lane, N., Rosenwassen, M. and Mow, V.C., Mechanical and biological changes in the superfacial zone of articular cartilage in canine experimental osteoarthritis. Journal of Orthopedic Research 12, 474484 (1994).CrossRefGoogle Scholar
Oka, M., Ushio, K. and Fujita, H., Development of artificial articular cartilage. Proceedings of the Institution of Mechanical Engineers, Part H: Journal of Engineering in Medicine 214, 5968 (2000).CrossRefGoogle ScholarPubMed
Gu, Z.Q., Xiao, J.M. and Zhang, X.H.. The development of artificial articular cartilage – PVA-hydrogel. Bio-Medical Materials and Engineering 8, 7581 (1998).Google ScholarPubMed
Ushio, K., Oka, M. and Nakamura, T., Attachment of articular cartilage to underlying bone. J. Biomed. Mater. 68B, 5968 (2003).CrossRefGoogle Scholar
Kobayashi, M., Toguchida, J. and Oka, M., Preliminary study of polyvinyl alcohol-hydrogel (PVA-H) artificial meniscus. Biomaterials 24, 639647 (2003).CrossRefGoogle ScholarPubMed
Kobayashi, M., A study of polyvinyl alcohol-hydrogel (PVA-H) artificial meniscus in vivo. Biomedical materials and engineering 14, 505515 (2004).Google ScholarPubMed
Hassan, C.M. and Peppas, N.A., Structure and applications of poly(vinyl alcohol) hydrogels produced by conventional crosslinking or by freezing/thawing methods. Adv. Polym. Sci. 153, 3765 (2000).CrossRefGoogle Scholar
Horkay, F., Basser, P.J., Hecht, A.M. and Geissler, E. E.: Hierarchical Organization of Cartilage Proteoglycans. Macromol. Symp. 306-307, 1117 (2011).CrossRefGoogle Scholar
Dimitriadis, E.K., Horkay, F., Maresca, J., Kachar, B. and Chadwick, R.S., Determination of elastic moduli of thin layers of soft material using the atomic force microscope. Biophysical Journal 82, 27982810 (2002).CrossRefGoogle ScholarPubMed
Horkay, F., Horkayne-Szakaly, I. and Basser, P.J., Measurement of the osmotic properties of thin polymer films and biological tissue samples. Biomacromolecules 6, 988993 (2005).CrossRefGoogle ScholarPubMed
Basser, P.J., Schneiderman, R., Bank, R.A., Wachtel, E. and Maroudas, A., Mechanical properties of the collagen network in human articular cartilage as measured by osmotic stress technique. Archives of Biochemistry and Biophysics 351, 207219 (1998).CrossRefGoogle ScholarPubMed
Horkay, F. and Lin, D.C., Mapping the local osmotic modulus of polymer gels. Langmuir 25, 87358741 (2009).CrossRefGoogle ScholarPubMed
Silva, C., Horkayne-Szakaly, I., Chandran, P., Dimitriadis, E.K., Lin, D.C., Papanicolas, C., Basser, P.J. and Horkay, F., Depth dependence of the mechanical and osmotic properties of cartilage. In Gels and Biomedical Materials (Eds. Horkay, F., Narayan, R., et al. .) Cambridge University Press, 2012.Google Scholar