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Gene Review

BGN  -  biglycan

Bos taurus

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Disease relevance of BGN

  • Proteoglycans from bovine nasal septa and from the Swarm rat chondrosarcoma were isolated as aggregates (PGC) and as monomers (PGS) [1].
  • The inhibition of synthesis of biglycan and decorin by IL-1 might be important in the pathophysiology of cartilage destruction in rheumatic diseases [2].
  • No change was observed in molecular size of PGS, isolated chondroitin sulphates or keratan sulphate-protein cores in osteoarthrosis in comparison with non-osteoarthrotic cartilage from the same joint or from younger adult animals [3].

High impact information on BGN

  • Addition of small amounts of proteoglycan subunit (PGS) blocked platelet aggregation, whereas chondroitin sulfate, a major glycosaminoglycan component of cartilage matrix, impaired platelet aggregation only at concentrations which resulted in a marked increase in viscosity [4].
  • Moreover, PGS abolished aggregation of platelets by polylysine but did not prevent aggregation by ADP, suggesting that PGS may block strategically placed lysine sites on the collagen molecule [4].
  • Similar leucine rich repeats have been identified in a number of proteins including the small interstitial proteoglycans decorin and PG-S1 [5].
  • Crystal Structure of the Biglycan Dimer and Evidence That Dimerization Is Essential for Folding and Stability of Class I Small Leucine-rich Repeat Proteoglycans [6].
  • We used light scattering to show that biglycan is dimeric in solution and solved the crystal structure of the glycoprotein core of biglycan at 3.40-A resolution [6].

Biological context of BGN

  • The results indicate that CTGF suppresses the synthesis of biglycan but newly induced that of decorin in the cells when the cell density is low; in addition, no change was observed in the hydrodynamic size and the glycosaminoglycan chain length of these two small chondroitin/dermatan sulfate proteoglycans [7].
  • Two overlapping cDNA clones for core protein of a biglycan of bovine aorta were isolated from a pSPORT bovine aorta tissue cDNA library [8].
  • The nucleotide sequence of the protein core for bovine aortic smooth muscle cell biglycan was determined using recombinant DNA technology [9].
  • The bovine biglycan protein core has four potential O-linked and two potential N-linked glycosylation sites and is composed of 11 leucine-rich repeat units [9].
  • Analysis of the deduced amino acid sequence for bovine biglycan revealed a striking homology, 94.6% and 95.7%, to human and rat biglycan, respectively [9].

Anatomical context of BGN


Associations of BGN with chemical compounds


Regulatory relationships of BGN


Other interactions of BGN


Analytical, diagnostic and therapeutic context of BGN

  • This was demonstrated by electron microscopy after negative staining of gold-labeled biglycan in aggregation experiments with collagen VI [21].
  • Biglycan but not decorin mRNAs were detected by Northern analysis and by PCR [22].
  • It was previously concluded on the basis of immunodiffusion studies that GPL has two antigenic components, one in common with PGS and one specific for the link proteins [23].
  • Bovine nasal cartilage proteoglycan aggregates are dissociated and separated by density gradient centrifugation in 4 M guanidine into proteoglycan subunit (PGS) and glycoprotein link (GPL) fractions, the latter containing hyaluronic acid and "link proteins" responsible for aggregate formation [23].
  • This finding was consistent with Northern blot analysis which showed that steady-state biglycan mRNA levels increased significantly during the elastinogenic period [24].


  1. Role of proteoglycans in endochondral ossification: inhibition of calcification. Dziewiatkowski, D.D., Majznerski, L.L. Calcif. Tissue Int. (1985) [Pubmed]
  2. Interleukin-1 reversibly inhibits the synthesis of biglycan and decorin in intact articular cartilage in culture. von den Hoff, H., de Koning, M., van Kampen, J., van der Korst, J. J. Rheumatol. (1995) [Pubmed]
  3. Proteoglycan structure of bovine articular cartilage. Variation with age and in osteoarthrosis. Axelsson, I., Bjelle, A. Scand. J. Rheumatol. (1979) [Pubmed]
  4. Platelet interaction with modified articular cartilage. Its possible relevance to joint repair. Zucker-Franklin, D., Drosenberg, L. J. Clin. Invest. (1977) [Pubmed]
  5. 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]
  6. Crystal Structure of the Biglycan Dimer and Evidence That Dimerization Is Essential for Folding and Stability of Class I Small Leucine-rich Repeat Proteoglycans. Scott, P.G., Dodd, C.M., Bergmann, E.M., Sheehan, J.K., Bishop, P.N. J. Biol. Chem. (2006) [Pubmed]
  7. Differential regulation of biglycan and decorin synthesis by connective tissue growth factor in cultured vascular endothelial cells. Kaji, T., Yamamoto, C., Oh-i, M., Nishida, T., Takigawa, M. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  8. Primary structure of bovine aorta biglycan core protein deduced from cloned CDNA. Xu, J.H., Radhakrishnamurthy, B., Srinivasan, S.R., Berenson, G.S. Biochem. Mol. Biol. Int. (1995) [Pubmed]
  9. cDNA sequence for bovine biglycan (PGI) protein core. Torok, M.A., Evans, S.A., Marcum, J.A. Biochim. Biophys. Acta (1993) [Pubmed]
  10. Molecular interactions of biglycan and decorin with elastic fiber components: biglycan forms a ternary complex with tropoelastin and microfibril-associated glycoprotein 1. Reinboth, B., Hanssen, E., Cleary, E.G., Gibson, M.A. J. Biol. Chem. (2002) [Pubmed]
  11. Biglycan and decorin induce morphological and cytoskeletal changes involving signalling by the small GTPases RhoA and Rac1 resulting in lung fibroblast migration. Tufvesson, E., Westergren-Thorsson, G. J. Cell. Sci. (2003) [Pubmed]
  12. The self-association of biglycan from bovine articular cartilage. Liu, J., Laue, T.M., Choi, H.U., Tang, L.H., Rosenberg, L. J. Biol. Chem. (1994) [Pubmed]
  13. Differential regulation of biglycan and decorin by retinoic acid in bovine chondrocytes. Pearson, D., Sasse, J. J. Biol. Chem. (1992) [Pubmed]
  14. Cell density-dependent regulation of proteoglycan synthesis by transforming growth factor-beta(1) in cultured bovine aortic endothelial cells. Kaji, T., Yamada, A., Miyajima, S., Yamamoto, C., Fujiwara, Y., Wight, T.N., Kinsella, M.G. J. Biol. Chem. (2000) [Pubmed]
  15. The effects of transforming growth factor-beta and serum on proteoglycan synthesis by tendon fibrocartilage. Vogel, K.G., Hernandez, D.J. Eur. J. Cell Biol. (1992) [Pubmed]
  16. Polymorphonuclear leukocyte adhesion to articular cartilage is inhibited by cartilage surface macromolecules. Mitani, Y., Honda, A., Jasin, H.E. Rheumatol. Int. (2001) [Pubmed]
  17. Assignment of chromosome rearrangements between X chromosomes of human and cattle by laser microdissection and Zoo-FISH. Rubes, J., Kubickova, S., Musilova, P., Amaral, M.E., Brunner, R.M., Goldammer, T. Chromosome Res. (2005) [Pubmed]
  18. 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]
  19. Characterization of epiphycan, a small proteoglycan with a leucine-rich repeat core protein. Johnson, H.J., Rosenberg, L., Choi, H.U., Garza, S., Höök, M., Neame, P.J. J. Biol. Chem. (1997) [Pubmed]
  20. Keratocyte phenotype mediates proteoglycan structure: a role for fibroblasts in corneal fibrosis. Funderburgh, J.L., Mann, M.M., Funderburgh, M.L. J. Biol. Chem. (2003) [Pubmed]
  21. Biglycan organizes collagen VI into hexagonal-like networks resembling tissue structures. Wiberg, C., Heinegård, D., Wenglén, C., Timpl, R., Mörgelin, M. J. Biol. Chem. (2002) [Pubmed]
  22. Proteoglycan synthesis by bovine myocardial endothelial cells is increased by long-term exposure to high concentrations of glucose. Klein, D.J., Cohen, R.M., Rymaszewski, Z. J. Cell. Physiol. (1995) [Pubmed]
  23. Immunological studies of bovine nasal cartilage proteoglycan "link proteins". Keiser, H. Biochemistry (1975) [Pubmed]
  24. Developmental expression of dermatan sulfate proteoglycans in the elastic bovine nuchal ligament. Reinboth, B.J., Finnis, M.L., Gibson, M.A., Sandberg, L.B., Cleary, E.G. Matrix Biol. (2000) [Pubmed]
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