Decorin

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

DCN
Identifiers
Aliases	DCN, Dcn, DC, DSPG2, PG40, PGII, PGS2, SLRR1B, mDcn, CSCD, decorin
External IDs	OMIM: 125255; MGI: 94872; HomoloGene: 22430; GeneCards: DCN; OMA:DCN - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q21.33 Start 91,140,484 bp End 91,183,217 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 C3|10 50.27 cM Start 97,315,471 bp End 97,354,005 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in decidua Achilles tendon synovial joint vena cava tendon of biceps brachii gallbladder pericardium tail of epididymis skin of hip stromal cell of endometrium Top expressed in sciatic nerve umbilical cord ankle efferent ductule iris vestibular membrane of cochlear duct cervix skin of external ear corneal stroma calvaria 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
Wikidata
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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.

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. Other angiogenic growth factors that decorin inhibits are angiopoietin, hepatocyte growth factor (HGF) and platelet-derived growth factor (PDGF).

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

Clinical significance

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

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. The decorin-deficient knockout mouse shows reduced inflammatory reactions during contact dermatitis due to a defect in leukocyte recruitment and altered interferon gamma function.

Interactions

Decorin has been shown to interact with:

• Collagen type I
• Epidermal growth factor receptor and
• TGF beta 1,
• TLR2, and
• TLR4.

Further reading

• Ständer M, Naumann U, Wick W, Weller M (May 1999). "Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth". Cell and Tissue Research. 296 (2): 221–7. doi:10.1007/s004410051283. PMID 10382266. S2CID 20282995.
• Fujisawa R (March 2002). "[Recent advances in research on bone matrix proteins]". Nihon Rinsho. Japanese Journal of Clinical Medicine. 60 (Suppl 3): 72–8. PMID 11979972.
• Krumdieck R, Höök M, Rosenberg LC, Volanakis JE (December 1992). "The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex". Journal of Immunology. 149 (11): 3695–701. doi:10.4049/jimmunol.149.11.3695. PMID 1431141. S2CID 23005992.
• Winnemöller M, Schön P, Vischer P, Kresse H (October 1992). "Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment". European Journal of Cell Biology. 59 (1): 47–55. PMID 1468447.
• Murphy-Ullrich JE, Schultz-Cherry S, Höök M (February 1992). "Transforming growth factor-beta complexes with thrombospondin". Molecular Biology of the 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)". Cytogenetics and Cell Genetics. 60 (2): 107–11. doi:10.1159/000133314. PMID 1611907.
• McBride OW, Fisher LW, Young MF (February 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, Jacobs L, Perlish JS, Termine JD (February 1991). "Decorin interacts with fibrillar collagen of embryonic and adult human skin". Journal of Structural Biology. 106 (1): 82–90. doi:10.1016/1047-8477(91)90065-5. PMID 2059554.
• Pulkkinen L, Kainulainen K, Krusius T, Mäkinen P, Schollin J, Gustavsson KH, Peltonen L (October 1990). "Deficient expression of the gene coding for decorin in a lethal form of Marfan syndrome". The Journal of Biological Chemistry. 265 (29): 17780–5. doi:10.1016/S0021-9258(18)38231-0. PMID 2211661.
• Yamaguchi Y, Mann DM, Ruoslahti E (July 1990). "Negative regulation of transforming growth factor-beta by the proteoglycan decorin". Nature. 346 (6281): 281–4. Bibcode:1990Natur.346..281Y. doi:10.1038/346281a0. PMID 2374594. S2CID 4272333.
• Greve H, Blumberg P, Schmidt G, Schlumberger W, Rauterberg J, Kresse H (July 1990). "Influence of collagen lattice on the metabolism of small proteoglycan II by cultured fibroblasts". The Biochemical Journal. 269 (1): 149–55. doi:10.1042/bj2690149. PMC 1131544. PMID 2375748.
• Roughley PJ, White RJ (September 1989). "Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II". The Biochemical Journal. 262 (3): 823–7. doi:10.1042/bj2620823. PMC 1133347. PMID 2590169.
• Fisher LW, Termine JD, Young MF (March 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". The Journal of Biological Chemistry. 264 (8): 4571–6. doi:10.1016/S0021-9258(18)83781-4. PMID 2647739.
• Yamaguchi Y, Ruoslahti E (November 1988). "Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation". Nature. 336 (6196): 244–6. Bibcode:1988Natur.336..244Y. doi:10.1038/336244a0. PMID 3194009. S2CID 4338095.
• Krusius T, Ruoslahti E (October 1986). "Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA". Proceedings of the National Academy of Sciences of the United States of America. 83 (20): 7683–7. Bibcode:1986PNAS...83.7683K. doi:10.1073/pnas.83.20.7683. PMC 386785. PMID 3484330.
• Fisher LW, Hawkins GR, Tuross N, Termine JD (July 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". The Journal of Biological Chemistry. 262 (20): 9702–8. doi:10.1016/S0021-9258(18)47991-4. PMID 3597437.
• Lysiak JJ, Hunt J, Pringle GA, Lala PK (April 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 (December 1994). "Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity". The Journal of Biological Chemistry. 269 (51): 32634–8. doi:10.1016/S0021-9258(18)31681-8. PMID 7798269.
• Scholzen T, Solursh M, Suzuki S, Reiter R, Morgan JL, Buchberg AM, et al. (November 1994). "The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation". The Journal of Biological Chemistry. 269 (45): 28270–81. doi:10.1016/S0021-9258(18)46924-4. PMID 7961765.
• Danielson KG, Fazzio A, Cohen I, Cannizzaro LA, Eichstetter I, Iozzo RV (January 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 (February 2005). "Congenital stromal dystrophy of the cornea caused by a mutation in the decorin gene". Investigative Ophthalmology & Visual Science. 46 (2): 420–6. doi:10.1167/iovs.04-0804. PMID 15671264.

External links

• GeneReviews/NCBI/NIH/UW entry on Congenital Stromal Corneal Dystrophy