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Gene Review

FMOD  -  fibromodulin

Bos taurus

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High impact information on FMOD

  • A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin) [1].
  • The cleavage product obtained after MMP-13 digestion was identical to that observed in cleaved fibromodulin from cartilage explant cultures stimulated with interleukin-1 [2].
  • Cleavage removes the tyrosine sulfate-rich region in the N terminus of fibromodulin [2].
  • Fibromodulin, a member of the leucine-rich repeat protein family, is one predominant protein in cartilage and is known for its roles in the formation of collagen fibrils and sustained interaction with these formed fibers [2].
  • The deduced keratocan amino acid sequence is unique but related to two other keratan sulfate-containing proteins, lumican (the 37B core protein) and fibromodulin [3].

Biological context of FMOD


Anatomical context of FMOD

  • The small keratan sulfate-substituted proteoglycan (fibromodulin) from articular cartilage was shown to contain keratan sulfate linked to the core protein through N-glycosidic linkages to residues Asn-109, Asn-147, Asn-182, and Asn-272 [8].
  • Biosynthetic experiments with articular chondrocytes in the presence of tunicamycin, an inhibitor of N-linked oligosaccharide synthesis, demonstrated a specific inhibition of [35S]SO4 incorporation into fibromodulin [8].
  • Thus fibromodulin from cartilage, tendon, and sclera contains N-glycosidically linked oligosaccharides, some of which are extended to keratan sulfate chains [4].
  • Among a large number of secreted fibroblast products, decorin and fibromodulin represented the vast majority of the collagen binding components [5].
  • The small proteoglycans, decorin, fibromodulin, biglycan, and lumican, represent a family of structurally related but genetically distinct molecules present in many types of connective tissues [5].

Associations of FMOD with chemical compounds


Other interactions of FMOD


Analytical, diagnostic and therapeutic context of FMOD


  1. A collagen-binding 59-kd protein (fibromodulin) is structurally related to the small interstitial proteoglycans PG-S1 and PG-S2 (decorin). Oldberg, A., Antonsson, P., Lindblom, K., Heinegård, D. EMBO J. (1989) [Pubmed]
  2. Cleavage of fibromodulin in cartilage explants involves removal of the N-terminal tyrosine sulfate-rich region by proteolysis at a site that is sensitive to matrix metalloproteinase-13. Heathfield, T.F., Onnerfjord, P., Dahlberg, L., Heinegård, D. J. Biol. Chem. (2004) [Pubmed]
  3. Molecular cloning and tissue distribution of keratocan. Bovine corneal keratan sulfate proteoglycan 37A. Corpuz, L.M., Funderburgh, J.L., Funderburgh, M.L., Bottomley, G.S., Prakash, S., Conrad, G.W. J. Biol. Chem. (1996) [Pubmed]
  4. Posttranslational modifications of fibromodulin. Antonsson, P., Heinegård, D., Oldberg, A. J. Biol. Chem. (1991) [Pubmed]
  5. Binding of fibromodulin and decorin to separate sites on fibrillar collagens. Hedbom, E., Heinegård, D. J. Biol. Chem. (1993) [Pubmed]
  6. Biosynthetic mechanisms for the addition of polylactosamine to chondrocyte fibromodulin. Plaas, A.H., Wong-Palms, S. J. Biol. Chem. (1993) [Pubmed]
  7. Differential distribution of lumican and fibromodulin in tooth cementum. Cheng, H., Caterson, B., Neame, P.J., Lester, G.E., Yamauchi, M. Connect. Tissue Res. (1996) [Pubmed]
  8. Identification of the keratan sulfate attachment sites on bovine fibromodulin. Plaas, A.H., Neame, P.J., Nivens, C.M., Reiss, L. J. Biol. Chem. (1990) [Pubmed]
  9. The structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage. Lauder, R.M., Huckerby, T.N., Nieduszynski, I.A. Eur. J. Biochem. (1996) [Pubmed]
  10. Age-related changes in the structure of the keratan sulphate chains attached to fibromodulin isolated from articular cartilage. Lauder, R.M., Huckerby, T.N., Nieduszynski, I.A., Plaas, A.H. Biochem. J. (1998) [Pubmed]
  11. Sequence and structural implications of a bovine corneal keratan sulfate proteoglycan core protein. Protein 37B represents bovine lumican and proteins 37A and 25 are unique. Funderburgh, J.L., Funderburgh, M.L., Brown, S.J., Vergnes, J.P., Hassell, J.R., Mann, M.M., Conrad, G.W. J. Biol. Chem. (1993) [Pubmed]
  12. Proteins in the tensile region of adult bovine deep flexor tendon. Vogel, K.G., Meyers, A.B. Clin. Orthop. Relat. Res. (1999) [Pubmed]
  13. Glycosaminoglycan addition to proteoglycans by articular chondrocytes--evidence for core protein-specific pathways. Wong-Palms, S., Plaas, A.H. Arch. Biochem. Biophys. (1995) [Pubmed]
  14. Characterization of fibromodulin isolated from bovine periodontal ligament. Watanabe, T., Kubota, T. J. Periodont. Res. (1998) [Pubmed]
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