Journal article
Comparative proteomic analysis of normal and collagen IX null mouse cartilage reveals altered extracellular matrix composition and novel components of the collagen IX interactome
B Brachvogel, F Zaucke, K Dave, EL Norris, J Stermann, M Dayakli, M Koch, JJ Gorman, JF Bateman, R Wilson
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2013
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.
Grants
Awarded by Deutsche Forschungsgemeinschaft
Funding Acknowledgements
[ "This work was supported by grants from the National Health and Medical Research Council of Australia, the Murdoch Childrens Research Institute, the Victorian Government's Operational Infrastructure Support Program, and Deutsche Forschungsgemeinschaft Grants BR2304/5-1, BR2304/7-1, and ZA561/2-1.", "We thank Mats Paulsson for critical reading of this manuscript and Paul O'Donnell (Bio21 institute, University of Melbourne) for assistance in analyzing excised proteins by mass spectrometry. Access to proteomic infrastructure funding in the QIMR Protein Discovery Centre was made possible through the Australian Government National Collaborative Infrastructure Scheme (NCRIS) provided via Bioplatforms Australia and the Queensland State Government." ]