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J Biol Chem, Vol. 274, Issue 14, 9636-9647, April 2, 1999
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From the Fibromodulin is a member of a family of
connective tissue glycoproteins/proteoglycans containing leucine-rich
repeat motifs. Several members of this gene family bind to fibrillar
collagens and are believed to function in the assembly of the collagen
network in connective tissues. Here we show that mice lacking a
functional fibromodulin gene exhibit an altered morphological phenotype
in tail tendon with fewer and abnormal collagen fiber bundles. In fibromodulin-null animals virtually all collagen fiber bundles are
disorganized and have an abnormal morphology. Also 10-20% of the
bundles in heterozygous mice are similar to the abnormal bundles in
fibromodulin-null tail tendon. Ultrastructural analysis of Achilles
tendon from fibromodulin-null mice show collagen fibrils with irregular
and rough outlines in cross-section. Morphometric analysis show that
fibromodulin-null mice have on the average thinner fibrils than wild
type animals as a result of a larger preponderance of very thin fibrils
in an overall similar range of fibril diameters. Protein and RNA
analyses show an approximately 4-fold increase in the content of
lumican in fibromodulin-null as compared with wild type tail tendon,
despite a decrease in lumican mRNA. These results demonstrate a
role for fibromodulin in collagen fibrillogenesis and suggest that the
orchestrated action of several leucine-rich repeat
glycoproteins/proteoglycans influence the architecture of collagen matrices.
Department of Cell and Molecular Biology,
University of Lund, P.O. Box 94, S-221 00 Lund, Sweden, the
§ Department of Experimental Pathology, University Hospital,
S-221 85 Lund, Sweden, and the ¶ Laboratory for Electron
microscopy, Department of Pathology, National Hospital,
0027 Oslo, Norway
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B. Mansson, C. Wenglen, M. Morgelin, T. Saxne, and D. Heinegard Association of Chondroadherin with Collagen Type II J. Biol. Chem., August 24, 2001; 276(35): 32883 - 32888. [Abstract] [Full Text] [PDF]
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