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Molecular and Cellular Biology, December 2005, p. 10465-10478, Vol. 25, No. 23
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.23.10465-10478.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Altered Integration of Matrilin-3 into Cartilage Extracellular Matrix in the Absence of Collagen IX

Institute for Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany,¹ Center for Biochemistry,² Center for Molecular Medicine, Medical Faculty, University of Cologne, Cologne, Germany,⁵ Biocenter and Department of Medical Biochemistry and Molecular Biology, University of Oulu, Oulu, Finland,³ Department of Orthopaedics, University of Regensburg, Bad Abbach, Germany⁴

Received 17 August 2005/ Accepted 8 September 2005

The matrilins are a family of four noncollagenous oligomeric extracellular matrix proteins with a modular structure. Matrilins can act as adapters which bridge different macromolecular networks. We therefore investigated the effect of collagen IX deficiency on matrilin-3 integration into cartilage tissues. Mice harboring a deleted Col9a1 gene lack synthesis of a functional protein and produce cartilage fibrils completely devoid of collagen IX. Newborn collagen IX knockout mice exhibited significantly decreased matrilin-3 and cartilage oligomeric matrix protein (COMP) signals, particularly in the cartilage primordium of vertebral bodies and ribs. In the absence of collagen IX, a substantial amount of matrilin-3 is released into the medium of cultured chondrocytes instead of being integrated into the cell layer as in wild-type and COMP-deficient cells. Gene expression of matrilin-3 is not affected in the absence of collagen IX, but protein extraction from cartilage is greatly facilitated. Matrilin-3 interacts with collagen IX-containing cartilage fibrils, while fibrils from collagen IX knockout mice lack matrilin-3, and COMP-deficient fibrils exhibit an intermediate integration. In summary, the integration of matrilin-3 into cartilage fibrils occurs both by a direct interaction with collagen IX and indirectly with COMP serving as an adapter. Matrilin-3 can be considered as an interface component, capable of interconnecting macromolecular networks and mediating interactions between cartilage fibrils and the extrafibrillar matrix.

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