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Gene Review

Bgn  -  biglycan

Rattus norvegicus

Synonyms: Biglycan, Bone/cartilage proteoglycan I, PG-S1
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Disease relevance of Bgn


High impact information on Bgn


Chemical compound and disease context of Bgn


Biological context of Bgn


Anatomical context of Bgn

  • Tissue sections were incubated with antibodies to the small, leucine-rich PG, decorin, and biglycan and collagen type I. Airways were classified according to basement membrane perimeter length (< or =0.99, 1-2.99, and > or =3 mm) [10].
  • Biglycan, a nitric oxide-regulated gene, affects adhesion, growth, and survival of mesangial cells [1].
  • Vascular smooth muscle biglycan represents a highly conserved proteoglycan within the arterial wall [9].
  • A marked increase in biglycan mRNA signal expression was also observed in endothelial cells and smooth muscle cells of the thickened myocardial capillary wall [2].
  • Transiently acidified (but not native) conditioned media from Kupffer cells and myofibroblastlike cells and transforming growth factor-beta 1 enhanced the relative abundances of biglycan and decorin messenger RNAs up to five times in primary-cultured fat-storing cells [7].

Associations of Bgn with chemical compounds

  • Employing this approach, biglycan expression turned out to be down-regulated time- and dose-dependently either by interleukin-1beta-stimulated endogenous nitric oxide production or by direct application of the exogenous nitric oxide donor, diethylenetriamine nitric oxide [1].
  • Biglycan expression could be normalized, both in vitro and in vivo, by using a specific inhibitor of the inducible nitric-oxide synthase, l-N6-(l-iminoethyl)-l-lysine dihydrochloride [1].
  • The expression of genes encoding the core proteins of the novel small chondroitin/dermatan sulfate proteoglycans decorin and biglycan was studied in the livers of normal rats and in liver tissue during fibrogenesis induced by prolonged bile-duct ligation and thioacetamide poisoning [7].
  • Specifically, the synthesis of the small soluble PG, biglycan, was decreased by exposure to 50% O2 [11].
  • Levels of mRNA for the proteoglycan, biglycan (as assessed by Northern blot analysis), also were comparable between the standard and elevated glucose conditions [12].

Other interactions of Bgn

  • Whereas biglycan was readily detected within the ASM, decorin and collagen were detected outside the ASM and especially in the adventitial layer [10].
  • AngII treatment also resulted in significant increases in the mRNA of the core proteins, versican, biglycan, and perlecan [13].
  • Northern blot, RT-PCR, Western blot, and promoter activity assays revealed that HGF caused a significant increase in decorin mRNA and protein, as well as in biglycan mRNA, protein, and promoter activity, suggesting transcriptional control of gene expression [14].
  • RT-PCR analysis showed that versican mRNA was highly expressed at P1 but was little expressed at P42. mRNAs for other chondroitin sulfate proteoglycans including biglycan, aggrecan, and decorin did not change much between P1 and P42 [15].
  • Alkaline phosphatase (AP), osteocalcin (OC), metalloproteinases (MMP-2 and -14), procollagenase C (BMP-1), biglycan (BG) and integrin 1 are expressed at higher levels in FMS*-treated osteoblasts than in control cultures [16].

Analytical, diagnostic and therapeutic context of Bgn

  • The Northern blot analysis demonstrated that expression of biglycan mRNA in the pressure-overloaded hearts on days 2, 7, 14 and 28 was 2.88 +/- 0.89, 2.32 +/- 0.49, 2.17 +/- 0.57 and 1.81 +/- 0.46-fold higher, respectively, than that in the sham-operated hearts [2].
  • In situ hybridization showed an increased density of biglycan mRNA signal-positive cells in the pressure-overloaded hearts [2].
  • The main induced proteoglycans were identified as biglycan and decorin by immunoprecipitation with antiserum made against synthetic peptides from the proteoglycan core proteins [17].
  • Immunocytochemistry showed intense immunostaining of biglycan and fibromodulin in the areas of injured lung tissue from rats 14 and 28 d after BM administration [18].
  • Microarray analysis revealed that many proteoglycan core proteins change during kidney development (syndecan-1,2,4, glypican-1,2,3, versican, decorin, biglycan) [19].


  1. Biglycan, a nitric oxide-regulated gene, affects adhesion, growth, and survival of mesangial cells. Schaefer, L., Beck, K.F., Raslik, I., Walpen, S., Mihalik, D., Micegova, M., Macakova, K., Schonherr, E., Seidler, D.G., Varga, G., Schaefer, R.M., Kresse, H., Pfeilschifter, J. J. Biol. Chem. (2003) [Pubmed]
  2. Increased expression of biglycan mRNA in pressure-overloaded rat heart. Ayada, Y., Kusachi, S., Murakami, T., Hirohata, S., Takemoto, S., Komatsubara, I., Hayashi, J., Iwabu, A., Ninomiya, Y., Tsuji, T. Clin. Exp. Hypertens. (2001) [Pubmed]
  3. Altered expression of small proteoglycans, collagen, and transforming growth factor-beta 1 in developing bleomycin-induced pulmonary fibrosis in rats. Westergren-Thorsson, G., Hernnäs, J., Särnstrand, B., Oldberg, A., Heinegård, D., Malmström, A. J. Clin. Invest. (1993) [Pubmed]
  4. Spatial and temporal patterns of gene expression for the proteoglycans biglycan and decorin and for transforming growth factor-beta 1 revealed by in situ hybridization during experimentally induced liver fibrosis in the rat. Krull, N.B., Zimmermann, T., Gressner, A.M. Hepatology (1993) [Pubmed]
  5. Decorin, biglycan and their endocytosis receptor in rat renal cortex. Schaefer, L., Hausser, H., Altenburger, M., Ugorcakova, J., August, C., Fisher, L.W., Schaefer, R.M., Kresse, H. Kidney Int. (1998) [Pubmed]
  6. Angiotensin II stimulates extracellular matrix protein synthesis through induction of transforming growth factor-beta expression in rat glomerular mesangial cells. Kagami, S., Border, W.A., Miller, D.E., Noble, N.A. J. Clin. Invest. (1994) [Pubmed]
  7. Biglycan and decorin gene expression in normal and fibrotic rat liver: cellular localization and regulatory factors. Meyer, D.H., Krull, N., Dreher, K.L., Gressner, A.M. Hepatology (1992) [Pubmed]
  8. Kinetics of biglycan, decorin and thrombospondin-1 in mercuric chloride-induced renal tubulointerstitial fibrosis. Suzuki, K., Wang, R., Kubota, H., Shibuya, H., Saegusa, J., Sato, T. Exp. Mol. Pathol. (2005) [Pubmed]
  9. Vascular smooth muscle biglycan represents a highly conserved proteoglycan within the arterial wall. Dreher, K.L., Asundi, V., Matzura, D., Cowan, K. Eur. J. Cell Biol. (1990) [Pubmed]
  10. Airway remodeling in allergen-challenged Brown Norway rats: distribution of proteoglycans. Pini, L., Torregiani, C., Martin, J.G., Hamid, Q., Ludwig, M.S. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) [Pubmed]
  11. Fetal lung fibroblasts selectively down-regulate proteoglycan synthesis in response to elevated oxygen. Caniggia, I., Liu, J., Kuliszewski, M., Tanswell, A.K., Post, M. J. Biol. Chem. (1996) [Pubmed]
  12. The effect of glucose on proteoglycans produced by cultured mesangial cells. Silbiger, S., Schlondorff, D., Crowley, S., Rosenberg, L., Choi, H., Hatcher, V., Gordon, P. Diabetes (1993) [Pubmed]
  13. Regulation of vascular proteoglycan synthesis by angiotensin II type 1 and type 2 receptors. Shimizu-Hirota, R., Sasamura, H., Mifune, M., Nakaya, H., Kuroda, M., Hayashi, M., Saruta, T. J. Am. Soc. Nephrol. (2001) [Pubmed]
  14. Hepatocyte growth factor regulates proteoglycan synthesis in interstitial fibroblasts. Kobayashi, E., Sasamura, H., Mifune, M., Shimizu-Hirota, R., Kuroda, M., Hayashi, M., Saruta, T. Kidney Int. (2003) [Pubmed]
  15. Expression of a chondroitin sulfate proteoglycan, versican (PG-M), during development of rat cornea. Koga, T., Inatani, M., Hirata, A., Inomata, Y., Zako, M., Kimata, K., Oohira, A., Gotoh, T., Mori, M., Tanihara, H. Curr. Eye Res. (2005) [Pubmed]
  16. FMS*Calciumfluor specifically increases mRNA levels and induces signaling via MAPK 42,44 and not FAK in differentiating rat osteoblasts. Manduca, P., Marchisio, S., Astigiano, S., Zanotti, S., Galmozzi, F., Palermo, C., Palmieri, D. Cell Biol. Int. (2005) [Pubmed]
  17. Elevated expression of transforming growth factor-beta and proteoglycan production in experimental glomerulonephritis. Possible role in expansion of the mesangial extracellular matrix. Okuda, S., Languino, L.R., Ruoslahti, E., Border, W.A. J. Clin. Invest. (1990) [Pubmed]
  18. Alterations in large and small proteoglycans in bleomycin-induced pulmonary fibrosis in rats. Venkatesan, N., Ebihara, T., Roughley, P.J., Ludwig, M.S. Am. J. Respir. Crit. Care Med. (2000) [Pubmed]
  19. Regulation of ureteric bud branching morphogenesis by sulfated proteoglycans in the developing kidney. Steer, D.L., Shah, M.M., Bush, K.T., Stuart, R.O., Sampogna, R.V., Meyer, T.N., Schwesinger, C., Bai, X., Esko, J.D., Nigam, S.K. Dev. Biol. (2004) [Pubmed]
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