Matrilin-3 Is Dispensable for Mouse Skeletal Growth and Development

REFERENCES

• Aszódi, A., Hauser N., Studer D., Paulsson M., Hiripi L., and Bösze Z.. 1996. Cloning, sequencing and expression analysis of mouse cartilage matrix protein cDNA. Eur. J. Biochem. 236:970–977.
   PubMedGoogle Scholar
• Aszódi, A., Chan D., Hunziker E., Bateman J. F., and Fässler R.. 1998. Collagen II is essential for the removal of the notochord and the formation of intervertebral discs. J. Cell Biol. 143:1399–1412.
   PubMed Web of Science ®Google Scholar
• Aszódi, A., Bateman J. F., Hirsch E., Baranyi M., Hunziker E. B., Hauser N., Bösze Z., and Fässler R.. 1999. Normal skeletal development of mice lacking matrilin 1: redundant function of matrilins in cartilage? Mol. Cell. Biol. 19:7841–7845.
   PubMedGoogle Scholar
• Brachtendorf, G., Kuhn A., Samulowitz U., Knorr R., Gustafsson E., Potocnik A. J., Fässler R., and Vestweber D.. 2001. Early expression of endomucin on endothelium of the mouse embryo and on putative hematopoietic clusters in the dorsal aorta. Dev. Dyn. 222:410–419.
   PubMedGoogle Scholar
• Brandau, O., Aszódi A., Hunziker E. B., Neame P. J., Vestweber D., and Fässler R.. 2002. Chondromodulin is dispensable during endochondral ossification and eye development. Mol. Cell. Biol. 22:6627–6635.
   PubMedGoogle Scholar
• Briggs, M. D., and Chapman K. L.. 2002. Pseudoachondroplasia and multiple epiphyseal dysplasia: mutation review, molecular interactions, and genotype to phenotype correlations. Hum. Mutat. 19:465–478.
   PubMed Web of Science ®Google Scholar
• Chapman, K. L., Mortier G. R., Chapman K., Loughlin J., Grant M. E., and Briggs M. D.. 2001. Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia. Nat. Genet. 28:393–396.
   PubMed Web of Science ®Google Scholar
• Chen, Q., Johnson D. M., Haudenschild D. R., Tondravi M. M., and Goetinck P. F.. 1995. Cartilage matrix protein forms a type II collagen-independent filamentous network: analysis in primary cell cultures with a retrovirus expression system. Mol. Biol. Cell 6:1743–1753.
   PubMedGoogle Scholar
• Chen, Q., Zhang Y., Johnson D. M., and Goetinck P. F.. 1999. Assembly of a novel cartilage matrix protein filamentous network: molecular basis of differential requirement of von Willebrand Factor A domains. Mol. Biol. Cell 10:2149–2162.
   PubMedGoogle Scholar
• Deák, F., Wagener R., Kiss I., and Paulsson M.. 1999. The matrilins: a novel family of oligomeric extracellular matrix proteins. Matrix Biol. 18:55–66.
   PubMedGoogle Scholar
• Dinser, R., Zaucke F., Kreppel F., Hultenby K., Kochanek S., Paulsson M., and Maurer P.. 2002. Pseudoachondroplasia is caused through both intra- and extracellular pathogenic pathways. J. Clin. Investig. 110:505–513.
   PubMedGoogle Scholar
• Farndale, R. W., Buttle D. J., and Barrett A. J.. 1986. Improved quantitation and discrimination of sulphated glycosaminoglycans by use of dimethylmethylene blue. Biochim. Biophys. Acta 883:173–177.
   PubMed Web of Science ®Google Scholar
• Hauser, N., and Paulsson M.. 1994. Native cartilage matrix protein (CMP). A compact trimer of subunits assembled via a coiled-coil α-helix. J. Biol. Chem. 269:25747–25753.
   PubMed Web of Science ®Google Scholar
• Hauser, N., Paulsson M., Heinegård D., and Mörgelin M.. 1996. Interaction of cartilage matrix protein (CMP) with aggrecan. Increased covalent crosslinking with maturation. J. Biol. Chem. 271:32247–32252.
   PubMedGoogle Scholar
• Huang, X., Birk D. E., and Goetinck P. F.. 1999. Mice lacking matrilin-1 (cartilage matrix protein) have alterations in type II collagen fibrillogenesis and fibril organization. Dev. Dyn. 216:434–441.
   PubMedGoogle Scholar
• Klatt, A. R., Nitsche P. D., Kobbe B., Mörgelin M., Paulsson M., and Wagener R.. 2000. Molecular structure and tissue distribution of matrilin-3, a filament-forming extracellular matrix protein expressed during skeletal development. J. Biol. Chem. 275:3999–4006.
   PubMed Web of Science ®Google Scholar
• Klatt, A. R., Nitsche D. P., Kobbe B., Macht M., Paulsson M., and Wagener R.. 2001. Molecular structure, processing, and tissue distribution of matrilin-4. J. Biol. Chem. 276:17267–17275.
   PubMedGoogle Scholar
• Klatt, A. R., Paulsson M., and Wagener R.. 2002. Expression of matrilins during maturation of mouse skeletal tissues. Matrix Biol. 21:289–296.
   PubMedGoogle Scholar
• Kleemann-Fischer, D., Kleemann G. R., Engel D., Yates III J. R., Wu J. J., and Eyre D. R.. 2001. Molecular properties of matrilin-3 isolated from human growth cartilage. Arch. Biochem. Biophys. 387:209–215.
   PubMedGoogle Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
   PubMed Web of Science ®Google Scholar
• Miosge, N., Klenczar C., Herken R., Willem M., and Mayer U.. 1999. Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin. Lab. Investig. 79:1591–1599.
   PubMedGoogle Scholar
• Mostert, A. K., Dijkstra P. F., Jansen B. R. H., van Horn J. R., de Graaf B., Heutink P., and Lindhout D.. 2003. Familial multiple epiphyseal dysplasia due to a matrilin-3 mutation: further delineation of the phenotype including 40 years follow-up. Am. J. Med. Genet. 120A:490–497.
   PubMedGoogle Scholar
• Piecha, D., Muratoglu S., Mörgelin M., Hauser N., Studer D., Kiss I., Paulsson M., and Deak F.. 1999. Matrilin-2, a large, oligomeric matrix protein, is expressed by a great variety of cells and forms fibrillar networks. J. Biol. Chem. 274:13353–13361.
   PubMedGoogle Scholar
• Pullig, O., Weseloh G., Klatt A. R., Wagener R., and Swoboda B.. 2002. Matrilin-3 in human articular cartilage: increased expression in osteoarthritis. Osteoarthritis Cartilage 10:253–263.
   PubMed Web of Science ®Google Scholar
• Stefansson, S. E., Jonsson H., Ingvarsson T., Manolescu I., Jonsson H. H., Olafsdottir G., Palsdottir E., Stefansdottir G., Sveinbjornsdottir G., Frigge M. L., Kong A., Gulcher J. R., and Stefansson K.. 2003. Genomewide scan for hand osteoarthritis: a novel mutation in matrilin-3. Am. J. Hum. Genet. 72:1448–1459.
   PubMed Web of Science ®Google Scholar
• Svensson, L., Aszódi A., Heinegard D., Hunziker E., Reinholt F. P., Fässler R., and Oldberg A.. 2002. Cartilage oligomeric matrix protein-deficient mice have normal skeletal development. Mol. Cell. Biol. 22:4366–4371.
   PubMed Web of Science ®Google Scholar
• Wagener, R., Kobbe B., and Paulsson M.. 1997. Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor. FEBS Lett. 413:129–134.
   PubMedGoogle Scholar
• Wagener, R., Kobbe B., and Paulsson M.. 1998. Matrilin-4, a new member of the matrilin family of extracellular matrix proteins. FEBS Lett. 436:123–127.
   PubMedGoogle Scholar
• Wagener, R., Kobbe B., Aszódi A., Liu Z., Beier D. R., and Paulsson M.. 2000. Structure and mapping of the mouse matrilin-3 gene (Matn3), a member of a gene family containing a U12-type AT-AC intron. Mamm. Genome 11:85–90.
   PubMedGoogle Scholar
• Wiberg, C., Klatt A. R., Wagener R., Paulsson M., Bateman J. F., Heinegård D., and Mörgelin M.. 2003. Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan. J. Biol. Chem. 278:37698–37704.
   PubMed Web of Science ®Google Scholar
• Winterbottom, N., Tondravi M. M., Harrington T. L., Klier F. G., Vertel B. M., and Goetinck P. F.. 1992. Cartilage matrix protein is a component of the collagen fibril of cartilage. Dev. Dyn. 193:266–276.
   PubMed Web of Science ®Google Scholar
• Wu, J. J., and Eyre D. R.. 1998. Matrilin-3 forms disulfide-linked oligomers with matrilin-1 in bovine epiphyseal cartilage. J. Biol. Chem. 273:17433–17438.
   PubMedGoogle Scholar