Decorin

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DCN
Protein DCN PDB 1xcd.png
Identifiers
AliasesDCN, Dcn, DC, DSPG2, PG40, PGII, PGS2, SLRR1B, mDcn, CSCD, decorin
External IDsOMIM: 125255 MGI: 94872 HomoloGene: 22430 GeneCards: DCN
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for DCN
Genomic location for DCN
Band12q21.33Start91,140,484 bp[1]
End91,182,824 bp[1]
RNA expression pattern
PBB GE DCN 201893 x at fs.png

PBB GE DCN 211813 x at fs.png

PBB GE DCN 209335 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001190451
NM_007833

RefSeq (protein)

NP_001177380
NP_031859

Location (UCSC)Chr 12: 91.14 – 91.18 MbChr 10: 97.48 – 97.52 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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[edit]

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[edit]

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 signifiance[edit]

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[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. [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[edit]

Decorin has been shown to interact with:

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000011465 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019929 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: DCN decorin".
  6. ^ Buraschi S, Neill T, Goyal A, Poluzzi C, Smythies J, Owens RT, et al. (July 2013). "Decorin causes autophagy in endothelial cells via Peg3". Proceedings of the National Academy of Sciences of the United States of America. 110 (28): E2582–91. Bibcode:2013PNAS..110E2582B. doi:10.1073/pnas.1305732110. PMC 3710796. PMID 23798385.
  7. ^ Järveläinen H, Sainio A, Wight TN (April 2015). "Pivotal role for decorin in angiogenesis". Matrix Biology. 43: 15–26. doi:10.1016/j.matbio.2015.01.023. PMC 4560244. PMID 25661523.
  8. ^ Kanzleiter T, Rath M, Görgens SW, Jensen J, Tangen DS, Kolnes AJ, et al. (July 2014). "The myokine decorin is regulated by contraction and involved in muscle hypertrophy". Biochemical and Biophysical Research Communications. 450 (2): 1089–94. doi:10.1016/j.bbrc.2014.06.123. PMID 24996176.
  9. ^ Jumper N, Paus R, Bayat A (September 2015). "Functional histopathology of keloid disease". Histology and Histopathology. 30 (9): 1033–57. doi:10.14670/HH-11-624. PMID 25900252.
  10. ^ Mellgren AE, Bruland O, Vedeler A, Saraste J, Schönheit J, Bredrup C, et al. (May 2015). "Development of congenital stromal corneal dystrophy is dependent on export and extracellular deposition of truncated decorin". Investigative Ophthalmology & Visual Science. 56 (5): 2909–15. doi:10.1167/iovs.14-16014. PMID 26029887.
  11. ^ Sofeu Feugaing DD, Götte M, Viola M (January 2013). "More than matrix: the multifaceted role of decorin in cancer". European Journal of Cell Biology. 92 (1): 1–11. doi:10.1016/j.ejcb.2012.08.004. PMID 23058688.
  12. ^ Seidler DG, Mohamed NA, Bocian C, Stadtmann A, Hermann S, Schäfers K, et al. (December 2011). "The role for decorin in delayed-type hypersensitivity". Journal of Immunology. 187 (11): 6108–19. doi:10.4049/jimmunol.1100373. PMC 5070385. PMID 22043007.
  13. ^ Bocian C, Urbanowitz AK, Owens RT, Iozzo RV, Götte M, Seidler DG (May 2013). "Decorin potentiates interferon-γ activity in a model of allergic inflammation". The Journal of Biological Chemistry. 288 (18): 12699–711. doi:10.1074/jbc.M112.419366. PMC 3642316. PMID 23460644.
  14. ^ a b Schönherr E, Broszat M, Brandan E, Bruckner P, Kresse H (July 1998). "Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen". Archives of Biochemistry and Biophysics. 355 (2): 241–8. doi:10.1006/abbi.1998.0720. PMID 9675033.
  15. ^ Santra M, Reed CC, Iozzo RV (September 2002). "Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope". The Journal of Biological Chemistry. 277 (38): 35671–81. doi:10.1074/jbc.M205317200. PMID 12105206.
  16. ^ Iozzo RV, Moscatello DK, McQuillan DJ, Eichstetter I (February 1999). "Decorin is a biological ligand for the epidermal growth factor receptor". The Journal of Biological Chemistry. 274 (8): 4489–92. doi:10.1074/jbc.274.8.4489. PMID 9988678.
  17. ^ Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E (September 1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta". The Biochemical Journal. 302 ( Pt 2) (2): 527–34. doi:10.1042/bj3020527. PMC 1137259. PMID 8093006.
  18. ^ 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. PMID 7798269.
  19. ^ a b Merline R, Moreth K, Beckmann J, Nastase MV, Zeng-Brouwers J, Tralhão JG, et al. (November 2011). "Signaling by the matrix proteoglycan decorin controls inflammation and cancer through PDCD4 and MicroRNA-21". Science Signaling. 4 (199): ra75. doi:10.1126/scisignal.2001868. PMC 5029092. PMID 22087031.

Further reading[edit]

External links[edit]