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Decorin

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Template:PBB 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]

Naming

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

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 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

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

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. 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]

Interactions

Decorin has been shown to interact with:

References

  1. ^ a b "Entrez Gene: DCN decorin".
  2. ^ Buraschi S, Neill T, Goyal A, Poluzzi C, Smythies J, Owens RT, Schaefer L, Torres A, Iozzo RV (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. ^ Attention: This template ({{cite pmid}}) is deprecated. To cite the publication identified by PMID 25900252, please use {{cite journal}} with |pmid=25900252 instead.
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

Further reading


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