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Validated All-in-One™ qPCR Primer for DCN(NM_001920.4) Search again
Product ID:
HQP094486
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CSCD, DSPG2, PG40, PGII, PGS2, SLRR1B
Gene Description:
decorin
Target Gene Accession:
NM_001920.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is a small cellular or pericellular matrix proteoglycan that is closely related in structure to biglycan protein. The encoded protein 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. It contains one attached glycosaminoglycan chain. This protein is capable of suppressing the growth of various tumor cell lines. There are multiple alternatively spliced transcript variants known for this gene. This gene is a candidate gene for Marfan syndrome. [provided by RefSeq].
Gene References into function
- decorin can disrupt glucose and TGFbeta/Smad-dependent transcription in mesangial cells through a mechanism that involves an increase in Ca(2+) signalling, the activation of Ca(2+)/calmodulin-dependent protein kinase II and phosphorylation of Smad2
- has a GAG chain and affinity to collagen
- binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope
- decorin supports adhesion and activation of human platelets
- The 179 allele variant of the Decorin gene is related to a slower progression of diabetic nephropathy in type 1 diabetic patients with albuminuria and receiving antihypertensive therapy
- the glycosaminoglycan chains in decorin are chondroitin, chondroitin 4-sulfate or chondroitin 6-sulfate
- carbohydrate recognition domains of SP-D interact with the dermatan sulfate moiety of decorin via lectin activity and the core protein of decorin binds the collagen-like region of SP-D
- might play a pivotal role in tissue remodeling by acting on the balance between extracellular matrix synthesis and degradation
- Decorin expressed in oral cancer may have lost its ability to inhibit TGF-beta signaling and activate epidermal growth factor receptor signaling pathways because of aberrant nuclear localization.
- decorin is a monomer in solution and is a monovalent ligand for various extracellular matrix proteins, growth factors, and cell surface receptors
- Continuous infusion of recombinant human decorin into acute stab injuries of adult rat spinal cord results in major reduction in astrogliosis, macrophage accumulation and deposition of chondroitin sulfate proteoglycans within spinal cord scar tissue.
- IL-10 and IL-6 induce decorin mRNA transcription, but additional signals from the extracellular matrix are necessary for its translation.
- Clones derived from a fibrotic patient secreted 3-fold greater amounts of decorin than those from a control subject; furthermore, there was a negative correlation between proliferation and synthesis of decorin
- decorin secreted by MRC-5 cells is a dermatan sulfate proteoglycan; glycosaminoglycans from the purified protein were treated with chondroitinases and the resulting disaccharides were analyzed
- dynamically increased expression of decorin in the choriodecidual membrane during parturition may be a part of the uterine preparation for labor
- decorin not only can regulate collagen fibril formation but that it also can act as an intermediary between type I and type VI collagen
- Malignant cells can actively influence the composition of the extracellular matrix through TGFbeta1 and other soluble factors.
- investigates the complex composed of one decorin core protein and one collagen molecule in order to obtain their binding force and binding stiffness
- Subsequent sequencing of candidate genes revealed a frameshift mutation in the DCN gene (c.967delT) that encodes for decorin, predicting a C-terminal truncation of the decorin protein
- 505 transcripts are differentially expressed in the thyroid carcinoma cell lines.
- a novel collagen binding domain in decorin acts cooperatively with leucine-rich repeat 4 to mask the alpha2beta1 integrin-binding site on collagen, an important sequence for the phagocytosis of collagen fibrils
- decorin peptides from the leucine-rich repeat 5 region inhibit angiogenesis
- decorin is not required for cell survival
- Decorin causes EGFR internalization via caveolae
- decorin secretion regulation has several components, including appropriate substitution with N-linked oligosaccharides and factors involved in glycosaminoglycan synthesis
- beta ig-h3 can differentially modulate the aggregation of collagen VI with biglycan and decorin
- decorin is a potent trophic factor that protects neuronal progenitor cells and glioma cells from oxygen and glucose deprivation
- reduced galactosyltransferase I(beta4GalT-7)activity resulting in defective glycosylation of decorin and biglycan may be responsible for the complex molecular pathology in beta4GalT-7 deficient Ehlers-Danlos syndrome patients
- Data show that decorin protein core inhibits tumor xenograft growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation.
- hevin can modulate the structure of dermal extracellular matrix, specifically by its regulation of decorin levels and collagen fibril assembly
- This is the second family with congenital stromal corneal dystrophy of the cornea in which a frame shift mutation in the decorin gene has been detected.
- Decorin mRNA was expressed in patients with early B-cell CLL, low expression was found in advanced clinical stages a significant higher expression in patients with non-progressive CLL type.
- decorin and biglycan are increased in DMD skeletal muscle and may have a role in muscle response to dystrophic cell damage
- data demonstrate that decorin can regulate fibrin organization and reveal a novel mechanism by which extracellular matrix components can participate in hemostasis, thrombosis, and wound repair
- The purified recombinant human decorin (rhDecorin) significantly inhibited the proliferation of LX-2 cells, a human HSC cell line, stimulated by TGF-beta1.
- decorin in the umbilical cord vein wall is elevated in pre-eclampsia in comparison to the corresponding control vessels
- Altered expression of decorin mRNA in the different dermal strata and a decrease in the collagen-to-decorin ratio inflicted by both age and ultraviolet irradiation affect collagen bundle diameter and subsequently the mechanical properties of human skin.
- Decorin may play an important role in cases of vulvar lichen sclerosus
- decorin is taken up by more than one endocytic pathway; uptake depends on EGFR signaling rather than trafficking along the same pathway
- The results suggest that a high level of decorin mRNA might be associated with the reduced content of collagen type III, resulting in a less flexible form of extracellular matrix in the connective tissue in stress urinary incontinence and prolapse.
- analysis of distribution patterns of decorin and biglycan and their relation with collagen
- In addition, no pathogenic sequence variations were found in DCN, DSPG3, LUM, PITX2 and FOXC1, which have also been implicated in corneal and anterior segment dysgenesis.
- Data show that at early stages of fibrillogenesis, the glycosaminoglycan chain of decorin has a reducing effect on collagen fibril diameter.
- Forced expression of decorin was accompanied by a suppression of alpha-SMA expression, whereas knocking down of decorin expression by RNA interference increased the expression of alpha-SMA.
- The molecular mechanism of Leucine Rich Repeat 5 reveals that its anti-migratory effect on endothelial cells is mediated by inhibiting VEGF-stimulated endothelial nitric oxide synthase activation and nitric oxide release.
- induction of decorin expression in angiogenic, as opposed to quiescent, endothelial cells promotes a motile phenotype in an interstitial collagen I-rich environment by both signaling through IGF-IR and influencing alpha2beta1 integrin activity
- Decorin is likely to possess a suppressive effect on human tumor angiogenesis in vivo and certainly provides a usable biomarker for distinguishing between benign and malignant vascular tumors in patients.
- The antimyeloma effect of decorin involved direct induction of apoptosis and activation of p21(WAF).
- analysis of an exception to the decorin oncosuppression model using human osteosarcoma cells
- Functional analysis of human decorin promoter identified an imperfect inverted repeat DNA motif, IR8 (-2313TGGTCAtagtgtcaTGACCT-2294), as a likely FXR-responsive element that is involved in decorin regulation.
- Multiple core-protein species were detected for decorin, biglycan, lumican and keratocan in the degenerate osteoarthritic articular cartilage and menisci.
- study concludes expression of decorin may be involved in the differentiation of colonic polyps and reduced expression of decorin may abrogate the defensive potential of stromal tissue and promote the development of common types of colon carcinoma