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Protein DCN PDB 1xcd.png
PDB rendering based on 1xcd.
Available structures
PDB Ortholog search: PDBe, RCSB
External IDs OMIM125255 MGI94872 HomoloGene22430 GeneCards: DCN Gene
RNA expression pattern
PBB GE DCN 201893 x at tn.png
PBB GE DCN 209335 at tn.png
PBB GE DCN 211813 x at tn.png
More reference expression data
Species Human Mouse
Entrez 1634 13179
Ensembl ENSG00000011465 ENSMUSG00000019929
UniProt P07585 P28654
RefSeq (mRNA) NM_001920 NM_001190451
RefSeq (protein) NP_001911 NP_001177380
Location (UCSC) Chr 12:
91.14 – 91.18 Mb
Chr 10:
97.48 – 97.52 Mb
PubMed search [1] [2]

Decorin is a protein that in humans is encoded by the DCN gene.

Decorin is a proteoglycan that is on average 90 - 140 kilodaltons (kD) in molecular weight. It belongs to the small leucine-rich proteoglycan (SLRP) family and consists of a protein core containing leucine repeats with a glycosaminoglycan (GAG) chain consisting of either chondroitin sulfate (CS) or dermatan sulfate (DS).

Decorin is a small cellular or pericellular matrix proteoglycan and is closely related in structure to biglycan protein. Decorin and biglycan are thought to be the result of a gene duplication. This protein is a component of connective tissue, binds to type I collagen fibrils, and plays a role in matrix assembly.[1]


Decorin's name is a derivative of both the fact that it "decorates" collagen type I, and that it interacts with the "d" and "e" bands of fibrils of this collagen.


Decorin appears to influence fibrillogenesis, and also interacts with fibronectin, thrombospondin, the complement component C1q, epidermal growth factor receptor (EGFR) and transforming growth factor-beta (TGF-beta).

Decorin has been shown to either enhance or inhibit the activity of TGF-beta 1. The primary function of decorin involves regulation during the cell cycle.

It has involved in the regulation of autophagy, of endothelial cell and inhibits angiogenesis. This process is mediated by a high-affinity interaction with VEGFR2 ( vascular endothelial growth factor receptor) which leads to increased levels of tumor suppressor gene called PEG3.[2] Other angiogenic growth factors that decorin inhibits are angiopoietin, hepatocyte growth factor (HGF) and platelet-derived growth factor (PDGF).[3]

Decorin has recently been established as a myokine. In this role, it promotes muscle hypertrophy by binding with myostatin.[4]

Clinical signifiance[edit]

Keloid scars have decreased decorin expression compared to healthy skin. [5]

Animal studies[edit]

Infusion of decorin into experimental rodent spinal cord injuries has been shown to suppress scar formation and promote axon growth.

Decorin has been shown to have anti-tumorigenic properties in an experimental murine tumor model and is capable of suppressing the growth of various tumor cell lines. There are multiple alternatively spliced transcript variants known for the decorin gene. Mutations in the decorin gene are associated with congenital stromal corneal dystrophy.[1]


Decorin has been shown to interact with:


  1. ^ a b "Entrez Gene: DCN decorin". 
  2. ^ Buraschi S, Neill T, Goyal A, Poluzzi C, Smythies J, Owens RT et al. (June 2013). "Decorin causes autophagy in endothelial cells via Peg3". Proc. Natl. Acad. Sci. U.S.A. 110 (28): E2582—91. doi:10.1073/pnas.1305732110. PMID 23798385. 
  3. ^ Järveläinen H, Sainio A, Wight TN (2015). "Pivotal role for decorin in angiogenesis". Matrix Biol. 43: 15—26. doi:10.1016/j.matbio.2015.01.023. PMID 25661523. 
  4. ^ Kanzleiter, T; Rath, M; Görgens, SW; Jensen, J; Tangen, DS; Kolnes, AJ; Kolnes, KJ; Lee, S; Eckel, J; Schürmann, A; Eckardt, K (2014). "The myokine decorin is regulated by contraction and involved in muscle hypertrophy". Biochem Biophys Res Commun 450: 1089–1094. doi:10.1016/j.bbrc.2014.06.123. 
  5. ^ Jumper, N; Paus, R; Bayat, A (2015). "Functional histopathology of keloid disease". Histology and histopathology: 11624. PMID 25900252.  edit
  6. ^ a b Schönherr E, Broszat M, Brandan E, Bruckner P, Kresse H (1998). "Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen". Arch. Biochem. Biophys. 355 (2): 241–8. doi:10.1006/abbi.1998.0720. PMID 9675033. 
  7. ^ Santra M, Reed CC, Iozzo RV (2002). "Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope". J. Biol. Chem. 277 (38): 35671–81. doi:10.1074/jbc.M205317200. PMID 12105206. 
  8. ^ Iozzo RV, Moscatello DK, McQuillan DJ, Eichstetter I (1999). "Decorin is a biological ligand for the epidermal growth factor receptor". J. Biol. Chem. 274 (8): 4489–92. doi:10.1074/jbc.274.8.4489. PMID 9988678. 
  9. ^ Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E (1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta". Biochem. J. 302 (2): 527–34. PMC 1137259. PMID 8093006. 
  10. ^ Takeuchi Y, Kodama Y, Matsumoto T (1994). "Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity". J. Biol. Chem. 269 (51): 32634–8. PMID 7798269. 
  11. ^ a b Merline R, Moreth K, Beckmann J, Nastase MV, Zeng-Brouwers J, Tralhão JG, Lemarchand P, Pfeilschifter J, Schaefer RM, Iozzo RV, Schaefer L (2011). "Signaling by the matrix proteoglycan decorin controls inflammation and cancer through PDCD4 and MicroRNA-21". Sci Signal 4 (199): ra75. doi:10.1126/scisignal.2001868. PMID 22087031. 

Further reading[edit]

  • Ständer M, Naumann U, Wick W, Weller M (1999). "Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth". Cell Tissue Res. 296 (2): 221–7. doi:10.1007/s004410051283. PMID 10382266. 
  • Fujisawa R (2002). "[Recent advances in research on bone matrix proteins]". Nippon Rinsho. 60 Suppl 3: 72–8. PMID 11979972. 
  • Krumdieck R, Höök M, Rosenberg LC, Volanakis JE (1992). "The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex". J. Immunol. 149 (11): 3695–701. PMID 1431141. 
  • Winnemöller M, Schön P, Vischer P, Kresse H (1993). "Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment". Eur. J. Cell Biol. 59 (1): 47–55. PMID 1468447. 
  • Murphy-Ullrich JE, Schultz-Cherry S, Höök M (1992). "Transforming growth factor-beta complexes with thrombospondin". Mol. Biol. Cell 3 (2): 181–8. doi:10.1091/mbc.3.2.181. PMC 275517. PMID 1550960. 
  • Pulkkinen L, Alitalo T, Krusius T, Peltonen L (1992). "Expression of decorin in human tissues and cell lines and defined chromosomal assignment of the gene locus (DCN)". Cytogenet. Cell Genet. 60 (2): 107–11. doi:10.1159/000133314. PMID 1611907. 
  • McBride OW, Fisher LW, Young MF (1990). "Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively". Genomics 6 (2): 219–25. doi:10.1016/0888-7543(90)90560-H. PMID 1968422. 
  • Fleischmajer R, Fisher LW, MacDonald ED et al. (1991). "Decorin interacts with fibrillar collagen of embryonic and adult human skin". J. Struct. Biol. 106 (1): 82–90. doi:10.1016/1047-8477(91)90065-5. PMID 2059554. 
  • Pulkkinen L, Kainulainen K, Krusius T et al. (1990). "Deficient expression of the gene coding for decorin in a lethal form of Marfan syndrome". J. Biol. Chem. 265 (29): 17780–5. PMID 2211661. 
  • Yamaguchi Y, Mann DM, Ruoslahti E (1990). "Negative regulation of transforming growth factor-beta by the proteoglycan decorin". Nature 346 (6281): 281–4. doi:10.1038/346281a0. PMID 2374594. 
  • Greve H, Blumberg P, Schmidt G et al. (1990). "Influence of collagen lattice on the metabolism of small proteoglycan II by cultured fibroblasts". Biochem. J. 269 (1): 149–55. PMC 1131544. PMID 2375748. 
  • Roughley PJ, White RJ (1990). "Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II". Biochem. J. 262 (3): 823–7. PMC 1133347. PMID 2590169. 
  • Fisher LW, Termine JD, Young MF (1989). "Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species". J. Biol. Chem. 264 (8): 4571–6. PMID 2647739. 
  • Yamaguchi Y, Ruoslahti E (1988). "Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation". Nature 336 (6196): 244–6. doi:10.1038/336244a0. PMID 3194009. 
  • Krusius T, Ruoslahti E (1986). "Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA". Proc. Natl. Acad. Sci. U.S.A. 83 (20): 7683–7. doi:10.1073/pnas.83.20.7683. PMC 386785. PMID 3484330. 
  • Fisher LW, Hawkins GR, Tuross N, Termine JD (1987). "Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone". J. Biol. Chem. 262 (20): 9702–8. PMID 3597437. 
  • Lysiak JJ, Hunt J, Pringle GA, Lala PK (1995). "Localization of transforming growth factor beta and its natural inhibitor decorin in the human placenta and decidua throughout gestation". Placenta 16 (3): 221–31. doi:10.1016/0143-4004(95)90110-8. PMID 7638106. 
  • Takeuchi Y, Kodama Y, Matsumoto T (1995). "Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity". J. Biol. Chem. 269 (51): 32634–8. PMID 7798269. 
  • Scholzen T, Solursh M, Suzuki S et al. (1994). "The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation". J. Biol. Chem. 269 (45): 28270–81. PMID 7961765. 
  • Danielson KG, Fazzio A, Cohen I et al. (1993). "The human decorin gene: intron-exon organization, discovery of two alternatively spliced exons in the 5' untranslated region, and mapping of the gene to chromosome 12q23". Genomics 15 (1): 146–60. doi:10.1006/geno.1993.1022. PMID 8432526. 
  • Bredrup C, Knappskog PM, Majewski J, Rødahl E, Boman H (2005). "Congenital stromal dystrophy of the cornea caused by a mutation in the decorin gene". Invest. Ophthalmol. Vis. Sci. 46 (2): 420–6. doi:10.1167/iovs.04-0804. PMID 15671264. 

External links[edit]