PDB rendering based on 1xcd.
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 Q3TSV1
RefSeq (mRNA) NM_001920.3 NM_007833
RefSeq (protein) NP_001911.1 NP_031859
Location (UCSC) Chr 12:
91.54 – 91.58 Mb
Chr 10:
96.94 – 96.98 Mb
PubMed search [1] [2]

Decorin is a proteoglycan on average 90 - 140 kilodaltons (kD) in size.

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, and that it interacts with the "d" and "e" bands.


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).

In some publications, decorin has been shown to enhance the bioactivity of TGF-beta 1, in other publications, TGF-beta 1's bioactivity has been shown to be inhibited. Because of this, it is believed the primary function of decorin lies in certain aspects of regulation during the cell cycle.

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 Epidermal growth factor receptor[2][3] and TGF beta 1.[4][5][6]


  1. ^ a b "Entrez Gene: DCN decorin". 
  2. ^ Santra, Manoranjan; Reed Charles C, Iozzo Renato V (Sep. 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. (United States) 277 (38): 35671–81. doi:10.1074/jbc.M205317200. ISSN 0021-9258. PMID 12105206. 
  3. ^ Iozzo, R V; Moscatello D K, McQuillan D J, Eichstetter I (Feb. 1999). "Decorin is a biological ligand for the epidermal growth factor receptor". J. Biol. Chem. (UNITED STATES) 274 (8): 4489–92. doi:10.1074/jbc.274.8.4489. ISSN 0021-9258. PMID 9988678. 
  4. ^ Hildebrand, A; Romarís M, Rasmussen L M, Heinegård D, Twardzik D R, Border W A, Ruoslahti E (Sep. 1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta". Biochem. J. (ENGLAND) 302 ( Pt 2) (Pt 2): 527–34. ISSN 0264-6021. PMC 1137259. PMID 8093006. 
  5. ^ Schönherr, E; Broszat M, Brandan E, Bruckner P, Kresse H (Jul. 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. (UNITED STATES) 355 (2): 241–8. doi:10.1006/abbi.1998.0720. ISSN 0003-9861. PMID 9675033. 
  6. ^ Takeuchi, Y; Kodama Y, Matsumoto T (Dec. 1994). "Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity". J. Biol. Chem. (UNITED STATES) 269 (51): 32634–8. ISSN 0021-9258. PMID 7798269. 

Further reading

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