Comparative proteomic analysis of normal and collagen IX null mouse cartilage reveals altered extracellular matrix composition and novel components of the collagen IX interactome

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Abstract

Background: Collagen IX is an integral cartilage extracellular matrix component important in skeletal development and joint function. Results: Proteomic analysis and validation studies revealed novel alterations in collagen IX null cartilage. Conclusion: Matrilin-4, collagen XII, thrombospondin-4, fibronectin, βig-h3, and epiphycan are components of the in vivo collagen IX interactome. Significance: We applied a proteomics approach to advance our understanding of collagen IX ablation in cartilage. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Brachvogel, B., Zaucke, F., Dave, K., Norris, E. L., Stermann, J., Dayakli, M., … Wilson, R. (2013). Comparative proteomic analysis of normal and collagen IX null mouse cartilage reveals altered extracellular matrix composition and novel components of the collagen IX interactome. Journal of Biological Chemistry, 288(19), 13481–13492. https://doi.org/10.1074/jbc.M112.444810

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