Decorin

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]
End	91,182,824 bp[1]
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)[2]
End	97,518,143 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• collagen binding; • protein N-terminus binding; • protein kinase inhibitor activity; • glycosaminoglycan binding; • extracellular matrix binding; • GO:0001948 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; • 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; • placentation; • chondroitin sulfate biosynthetic process; • response to mechanical stimulus; • aging; • 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 from RNA polymerase II promoter; • negative regulation of JAK-STAT cascade;
	Sources:Amigo / QuickGO
Orthologs
	1634
	13179
	ENSG00000011465
	ENSMUSG00000019929
	P07585
	P28654
NM_001920; NM_133503; NM_133504; NM_133505; NM_133506;
	NM_133507
	NM_001190451; NM_007833
NP_001911; NP_598010; NP_598011; NP_598012; NP_598013;
	NP_598014
	NP_001177380; NP_031859
	Wikidata
View/Edit Human	View/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

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]

References

GRCh38: Ensembl release 89: ENSG00000011465 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000019929 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: DCN decorin".
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.
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.
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.
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.
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.
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.
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.
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.
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.
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. S2CID 20575381.
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. S2CID 32175802.
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.
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.
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.

External links

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

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000011465 - Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[Entrez-5] "Entrez Gene: DCN decorin".

[pmid23798385-6] 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.

[pmid9675033-14] 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.

[pmid12105206-15] 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. S2CID 20575381.

[pmid9988678-16] 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. S2CID 32175802.

[pmid8093006-17] 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.

[pmid7798269-18] 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.

[pmid22087031-19] 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.