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DCN  -  decorin

Homo sapiens

Synonyms: Bone proteoglycan II, CSCD, DSPG2, Decorin, PG-S2, ...
 
 
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Disease relevance of DCN

 

Psychiatry related information on DCN

  • Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease [5].
  • There is evidence indicating that these profibrotic factors interact with antifibrotic defense mechanisms, such as decrease of myofibroblast accumulation, elimination of reactive oxygen species by inducible nitric oxide synthase and neutralization of transforming-growth-factor beta1 by decorin, such that some plaques are in dynamic turnover [6].
 

High impact information on DCN

  • On the basis of our results, decorin may eventually prove to be clinically useful in diseases associated with overproduction of TGF-beta [7].
  • As transforming growth factor-beta induces synthesis of decorin in many cell types, our results suggest that decorin may be a component of a feedback system regulating cell growth [8].
  • In studying the functional role of an extracellular matrix proteoglycan, decorin, we have made observations that suggest a role for this proteoglycan in the control of cell proliferation [9].
  • The reduction in the saturation densities of the cell lines with the highest expression of decorin is more than 50% [9].
  • We report here that Chinese hamster ovary (CHO) cell lines expressing human decorin from a stably transfected complementary DNA construct form a more orderly monolayer and grow to a lower saturation density than control cells lacking decorin [9].
 

Chemical compound and disease context of DCN

 

Biological context of DCN

  • Regional localization of BGN to Xq13-qter and DCN to 12p12.1-qter was also obtained by examining hybrids containing spontaneous breaks or well-characterized translocations involving chromosomes X and 12 [15].
  • [125I]DCN poorly bound to subpeptide MKKTRG and did not bind at all to subpeptides VDAVRTEKGFLLLASLRQ and TLLALERKDHS, suggesting that heparin-binding sequence MKKTRG constituted a DCN binding site when flanked with peptides VDAVRTEKGFLLLASLRQ and TLLALERKDHS [16].
  • Overall, these data indicate that modulation by steric exclusion of cell adhesion to a KKTR-dependent cell adhesive site present within the N-terminal domain of TSP could explain the antiadhesive properties of DCN [16].
  • However, the mechanism by which decorin mediates its effect on cell proliferation is unclear [17].
  • The effects of decorin persisted in the absence of extracellular Ca2+ but were blocked by AG1478, an epidermal growth factor (EGF)-specific tyrosine kinase inhibitor, and by down-regulation of the EGF receptor [17].
 

Anatomical context of DCN

 

Associations of DCN with chemical compounds

  • Decorin (DCN) is a ubiquitous proteoglycan comprised of a core protein attached to a single dermatan/chondroitin sulphate glycosaminoglycan chain [21].
  • Northern blot analysis indicated that steady state messenger RNA (mRNA) concentration of DCN was increased by Dex in all of the HOB cultures and in seven of eight BMSC cultures analyzed [22].
  • In addition, heparan sulfate drastically inhibited [125I]DCN binding to solid-phase adsorbed TSP (80% inhibition), suggesting that DCN could bind to the N-terminal domain of TSP through interaction with heparin-binding sequences [16].
  • To address this question, a series of synthetic peptides, overlapping heparin-binding sequences ARKGSGRR (residues 22-29), KKTR (residues 80-83) and RLRIAKGGVNDN (residues 178-189), were synthesized and tested for their ability to interact with DCN [16].
  • Several independent lines of evidence have implicated decorin, a small leucine-rich proteoglycan, in the inhibition of cell proliferation [17].
 

Physical interactions of DCN

 

Enzymatic interactions of DCN

  • MMP-7 cleaves DCN into three major fragments which have the N-termini Asp1-Glu-Ala-Ser-Gly, Glu2-Ala-Ser-Gly-Ile and Leu244-His-Leu-Asp-Asn [21].
 

Regulatory relationships of DCN

 

Other interactions of DCN

  • Both biglycan and decorin bound to type V collagen in a saturable and specific manner [20].
  • Scatchard analysis showed that biglycan bound beta ig-h3 more avidly than decorin with Kd values estimated as 5.88 x 10(-8) and 1.02 x 10(-7) M, respectively [29].
  • A remarkable finding was the observation that there was a reduction not only in the total levels of collagen, but also in osteonectin and three proteoglycans (a large chondroitin sulfate proteoglycan, biglycan, and decorin) [30].
  • METHODS: Renal tissues from 18 patients with CGN were examined immunohistochemically for versican, decorin, biglycan and collagen type I, and were compared with morphologically normal tissues from six tumor nephrectomies [31].
  • MMP-2 and MMP-3 digest DCN into seven major fragments in a similar pattern [21].
 

Analytical, diagnostic and therapeutic context of DCN

References

  1. Decorin, versican, and biglycan gene expression by keloid and normal dermal fibroblasts: differential regulation by basic fibroblast growth factor. Tan, E.M., Hoffren, J., Rouda, S., Greenbaum, S., Fox, J.W., Moore, J.H., Dodge, G.R. Exp. Cell Res. (1993) [Pubmed]
  2. Expression of decorin, biglycan, and collagen type I in human renal fibrosing disease. Stokes, M.B., Holler, S., Cui, Y., Hudkins, K.L., Eitner, F., Fogo, A., Alpers, C.E. Kidney Int. (2000) [Pubmed]
  3. Small proteoglycans of normal adult human kidney: distinct expression patterns of decorin, biglycan, fibromodulin, and lumican. Schaefer, L., Gröne, H.J., Raslik, I., Robenek, H., Ugorcakova, J., Budny, S., Schaefer, R.M., Kresse, H. Kidney Int. (2000) [Pubmed]
  4. Delayed appearance of decorin in healing burn scars. Sayani, K., Dodd, C.M., Nedelec, B., Shen, Y.J., Ghahary, A., Tredget, E.E., Scott, P.G. Histopathology (2000) [Pubmed]
  5. Peripheral distribution of dermatan sulfate proteoglycans (decorin) in amyloid-containing plaques and their presence in neurofibrillary tangles of Alzheimer's disease. Snow, A.D., Mar, H., Nochlin, D., Kresse, H., Wight, T.N. J. Histochem. Cytochem. (1992) [Pubmed]
  6. Mechanisms of Disease: new insights into the cellular and molecular pathology of Peyronie's disease. Gonzalez-Cadavid, N.F., Rajfer, J. Nature clinical practice. Urology. (2005) [Pubmed]
  7. Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Border, W.A., Noble, N.A., Yamamoto, T., Harper, J.R., Yamaguchi, Y., Pierschbacher, M.D., Ruoslahti, E. Nature (1992) [Pubmed]
  8. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Yamaguchi, Y., Mann, D.M., Ruoslahti, E. Nature (1990) [Pubmed]
  9. Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation. Yamaguchi, Y., Ruoslahti, E. Nature (1988) [Pubmed]
  10. Localization of a binding site for the proteoglycan decorin on collagen XIV (undulin). Ehnis, T., Dieterich, W., Bauer, M., Kresse, H., Schuppan, D. J. Biol. Chem. (1997) [Pubmed]
  11. Decorin core protein secretion is regulated by N-linked oligosaccharide and glycosaminoglycan additions. Seo, N.S., Hocking, A.M., Höök, M., McQuillan, D.J. J. Biol. Chem. (2005) [Pubmed]
  12. Decorin gene transfer-mediated suppression of TGF-beta synthesis abrogates experimental malignant glioma growth in vivo. Ständer, M., Naumann, U., Dumitrescu, L., Heneka, M., Löschmann, P., Gulbins, E., Dichgans, J., Weller, M. Gene Ther. (1998) [Pubmed]
  13. Fibroblasts from post-burn hypertrophic scar tissue synthesize less decorin than normal dermal fibroblasts. Scott, P.G., Dodd, C.M., Ghahary, A., Shen, Y.J., Tredget, E.E. Clin. Sci. (1998) [Pubmed]
  14. Central role of TGF-beta in the pathogenesis of diabetic nephropathy and macrovascular complications: a hypothesis. Yokoyama, H., Deckert, T. Diabet. Med. (1996) [Pubmed]
  15. Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively. McBride, O.W., Fisher, L.W., Young, M.F. Genomics (1990) [Pubmed]
  16. Decorin inhibits cell attachment to thrombospondin-1 by binding to a KKTR-dependent cell adhesive site present within the N-terminal domain of thrombospondin-1. Merle, B., Malaval, L., Lawler, J., Delmas, P., Clezardin, P. J. Cell. Biochem. (1997) [Pubmed]
  17. Decorin activates the epidermal growth factor receptor and elevates cytosolic Ca2+ in A431 carcinoma cells. Patel, S., Santra, M., McQuillan, D.J., Iozzo, R.V., Thomas, A.P. J. Biol. Chem. (1998) [Pubmed]
  18. Glycosaminoglycans and proteoglycans in the skin of aneuploid fetuses with increased nuchal translucency. von Kaisenberg, C.S., Prols, F., Nicolaides, K.H., Maass, N., Meinhold-Heerlein, I., Brand-Saberi, B. Hum. Reprod. (2003) [Pubmed]
  19. Interleukin (IL)-6 and IL-10 induce decorin mRNA in endothelial cells, but interaction with fibrillar collagen is essential for its translation. Strazynski, M., Eble, J.A., Kresse, H., Schönherr, E. J. Biol. Chem. (2004) [Pubmed]
  20. Interaction of heparin cofactor II with biglycan and decorin. Whinna, H.C., Choi, H.U., Rosenberg, L.C., Church, F.C. J. Biol. Chem. (1993) [Pubmed]
  21. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Imai, K., Hiramatsu, A., Fukushima, D., Pierschbacher, M.D., Okada, Y. Biochem. J. (1997) [Pubmed]
  22. The effect of glucocorticoid on the synthesis of biglycan and decorin in human osteoblasts and bone marrow stromal cells. Kimoto, S., Cheng, S.L., Zhang, S.F., Avioli, L.V. Endocrinology (1994) [Pubmed]
  23. Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen. Schönherr, E., Broszat, M., Brandan, E., Bruckner, P., Kresse, H. Arch. Biochem. Biophys. (1998) [Pubmed]
  24. Leucine-rich repeat region of decorin binds to filamin-A. Yoshida, K., Suzuki, Y., Honda, E., Amemiya, K., Nakatani, T., Ebina, M., Narumi, K., Satoh, K., Munakata, H. Biochimie (2002) [Pubmed]
  25. Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis. Zhu, J.X., Goldoni, S., Bix, G., Owens, R.T., McQuillan, D.J., Reed, C.C., Iozzo, R.V. J. Biol. Chem. (2005) [Pubmed]
  26. Effects of rhDecorin on TGF-beta1 induced human hepatic stellate cells LX-2 activation. Shi, Y.F., Zhang, Q., Cheung, P.Y., Shi, L., Fong, C.C., Zhang, Y., Tzang, C.H., Chan, B.P., Fong, W.F., Chun, J., Kung, H.F., Yang, M. Biochim. Biophys. Acta (2006) [Pubmed]
  27. Isolation and characterization of fibroblasts derived from regenerating human periodontal defects. Ivanovski, S., Haase, H.R., Bartold, P.M. Arch. Oral Biol. (2001) [Pubmed]
  28. Effect of interleukin-10 on the gene expression of type I collagen, fibronectin, and decorin in human skin fibroblasts: differential regulation by transforming growth factor-beta and monocyte chemoattractant protein-1. Yamamoto, T., Eckes, B., Krieg, T. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  29. Beta ig-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation, and participates in ternary complexing with these macromolecules. Reinboth, B., Thomas, J., Hanssen, E., Gibson, M.A. J. Biol. Chem. (2006) [Pubmed]
  30. Extracellular matrix stoichiometry in osteoblasts from patients with osteogenesis imperfecta. Fedarko, N.S., Robey, P.G., Vetter, U.K. J. Bone Miner. Res. (1995) [Pubmed]
  31. Up-regulation of extracellular matrix proteoglycans and collagen type I in human crescentic glomerulonephritis. Stokes, M.B., Hudkins, K.L., Zaharia, V., Taneda, S., Alpers, C.E. Kidney Int. (2001) [Pubmed]
  32. Differential regulation of extracellular matrix proteoglycan (PG) gene expression. Transforming growth factor-beta 1 up-regulates biglycan (PGI), and versican (large fibroblast PG) but down-regulates decorin (PGII) mRNA levels in human fibroblasts in culture. Kähäri, V.M., Larjava, H., Uitto, J. J. Biol. Chem. (1991) [Pubmed]
  33. Expression of extracellular matrix molecules in human mesangial cells in response to prolonged hyperglycaemia. Wahab, N.A., Harper, K., Mason, R.M. Biochem. J. (1996) [Pubmed]
 
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