DCN
Identifiers
Aliases	DCN, Dcn, DC, DSPG2, PG40, PGII, PGS2, SLRR1B, mDcn, CSCD, decorin
External IDs	OMIM: 125255 MGI: 94872 HomoloGene: 22430 GeneCards: DCN
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q21.33 Start 91,140,484 bp[1] End 91,183,217 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C3|10 50.27 cM Start 97,315,471 bp[2] End 97,354,005 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon synovial joint vena cava gallbladder pericardium stromal cell of endometrium gastric mucosa right coronary artery lactiferous duct left uterine tube Top expressed in sciatic nerve belly cord ankle iris cervix corneal stroma calvaria superior surface of tongue body of femur extensor digitorum longus muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function collagen binding protein N-terminus binding protein kinase inhibitor activity glycosaminoglycan binding extracellular matrix binding protein binding RNA binding extracellular matrix structural constituent conferring compression resistance Cellular component cytoplasm extracellular matrix lysosomal lumen Golgi lumen collagen type VI trimer extracellular space extracellular region collagen-containing extracellular matrix Biological process glycosaminoglycan metabolic process positive regulation of mitochondrial fission negative regulation of protein kinase activity positive regulation of autophagy kidney development cytokine-mediated signaling pathway placenta development chondroitin sulfate biosynthetic process response to mechanical stimulus human ageing extracellular matrix disassembly extracellular matrix organization wound healing negative regulation of endothelial cell migration positive regulation of macroautophagy response to lipopolysaccharide positive regulation of mitochondrial depolarization animal organ morphogenesis chondroitin sulfate catabolic process negative regulation of angiogenesis positive regulation of phosphatidylinositol 3-kinase signaling peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan negative regulation of vascular endothelial growth factor signaling pathway dermatan sulfate biosynthetic process skeletal muscle tissue development positive regulation of transcription by RNA polymerase II negative regulation of receptor signaling pathway via JAK-STAT Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1634 13179 Ensembl ENSG00000011465 ENSMUSG00000019929 UniProt P07585 P28654 RefSeq (mRNA) NM_001920 NM_133503 NM_133504 NM_133505 NM_133506 NM_133507 NM_001190451 NM_007833 RefSeq (protein) NP_001911 NP_598010 NP_598011 NP_598012 NP_598013 NP_598014 NP_001177380 NP_031859 Location (UCSC) Chr 12: 91.14 – 91.18 Mb Chr 10: 97.32 – 97.35 Mb PubMed search [3] [4]
Wikidata
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Decorin is a protein that in humans is encoded by the DCN gene.

Decorin is a proteoglycan that is on average 90 - 140 kilodaltons (kDa) 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.^[5]

Naming

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.

Function

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 been 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.^[6] Other angiogenic growth factors that decorin inhibits are angiopoietin, hepatocyte growth factor (HGF) and platelet-derived growth factor (PDGF).^[7]

Decorin has recently been established as a myokine. In this role, it promotes muscle hypertrophy by binding with myostatin.^[8]

Clinical significance

Keloid scars have decreased decorin expression compared to healthy skin.^[9] Development of congenital stromal corneal dystrophy is dependent on export and extracellular deposition of truncated decorin. ^[10]

Animal studies

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. ^[11] The decorin-deficient knockout mouse shows reduced inflammatory reactions during contact dermatitis due to a defect in leukocyte recruitment and altered interferon gamma function. ^{[12] [13]}

Interactions

Decorin has been shown to interact with:

• Collagen type I^[14]
• Epidermal growth factor receptor^[15][16] and
• TGF beta 1,^[14][17][18]
• TLR2,^[19] and
• TLR4.^[19]