Chondrocyte heterogeneity: immunohistologically defined variation of integrin expression at different sites in human fetal kneesDM Salter, JL Godolphin and MS Gourlay Edinburgh University Department of Pathology, UK. During development and at maturity different forms of cartilage vary in morphology and macromolecular content. This reflects heterogeneity of chondrocyte activity, in part involving differential interactions with the adjacent extracellular matrix via specialized cell surface receptors such as integrins. We undertook an immunohistological study on a series of human fetal knee joints to assess variation in the expression of integrins by chondrocytes and potential matrix ligands in articular, epiphyseal, growth plate, and meniscal cartilage. The results show that articular chondrocytes (beta 1+, beta 5 alpha V+, alpha 1+, alpha 2+/-, alpha 5+, weakly alpha 6+, alpha V+) differed from epiphyseal (beta 1+, beta 5 alpha V+, alpha 1+/-, alpha 2+/-, alpha 5+, alpha 6+, alpha V+) growth plate (beta 1+, beta 5 alpha V+, alpha 1-, alpha 2-, alpha 5+, alpha 6+, alpha V+), and meniscal cells (beta 1+, beta 5 alpha V+, alpha 1+, strongly alpha 2+, alpha 5+, alpha 6+, alpha V+ in expression of integrin subunits. There was no expression of beta 3, beta 4, beta 6, or alpha 3 by chondrocytes. These results differ from previous reports on the expression of integrins by adult articular cartilage, where alpha 2 and alpha 6 are not seen. Variation in distribution of matrix ligands was also seen. Fibronectin, laminin and Type VI collagen were expressed in all cartilages but there was restricted expression of tenascin, ED-A and ED-B fibronectin isoforms (articular cartilage and meniscus), and vitronectin (absent from growth plate cartilage). Regulated expression of integrins by chondrocytes, associated with changes in the pericellular matrix composition, is of potential importance in control of cartilage differentiation and function in health and disease.
Volume 43,
Issue 4,
pp. 447-457,
04/01/1995
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F. H. Chen, A. O. Thomas, J. T. Hecht, M. B. Goldring, and J. Lawler Cartilage Oligomeric Matrix Protein/Thrombospondin 5 Supports Chondrocyte Attachment through Interaction with Integrins J. Biol. Chem., September 23, 2005; 280(38): 32655 - 32661. [Abstract] [Full Text] [PDF] |
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E. Ekholm, K. D. Hankenson, H. Uusitalo, A. Hiltunen, H. Gardner, J. Heino, and R. Penttinen Diminished Callus Size and Cartilage Synthesis in {alpha}1{beta}1 Integrin-Deficient Mice during Bone Fracture Healing Am. J. Pathol., May 1, 2002; 160(5): 1779 - 1785. [Abstract] [Full Text] [PDF] |
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M. G. Attur, M. N. Dave, R. M. Clancy, I. R. Patel, S. B. Abramson, and A. R. Amin Functional Genomic Analysis in Arthritis-Affected Cartilage: Yin-Yang Regulation of Inflammatory Mediators by {alpha}5{beta}1 and {alpha}V{beta}3 Integrins J. Immunol., March 1, 2000; 164(5): 2684 - 2691. [Abstract] [Full Text] [PDF] |
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J. Kapyla, J. Ivaska, R. Riikonen, P. Nykvist, O. Pentikainen, M. Johnson, and J. Heino Integrin alpha 2I Domain Recognizes Type I and Type IV Collagens by Different Mechanisms J. Biol. Chem., February 4, 2000; 275(5): 3348 - 3354. [Abstract] [Full Text] [PDF] |
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S. Makihira, W. Yan, S. Ohno, T. Kawamoto, K. Fujimoto, A. Okimura, E. Yoshida, M. Noshiro, T. Hamada, and Y. Kato Enhancement of Cell Adhesion and Spreading by a Cartilage-specific Noncollagenous Protein, Cartilage Matrix Protein (CMP/Matrilin-1), via Integrin alpha 1beta 1 J. Biol. Chem., April 16, 1999; 274(16): 11417 - 11423. [Abstract] [Full Text] [PDF] |
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K. Ostergaard, D. M Salter, J. Petersen, K. Bendtzen, J. Hvolris, and C. B Andersen Expression of alpha and beta subunits of the integrin superfamily in articular cartilage from macroscopically normal and osteoarthritic human femoral heads Ann Rheum Dis, May 1, 1998; 57(5): 303 - 308. [Abstract] [Full Text] |
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