Results 211 to 220 of about 18,940 (249)
Some of the next articles are maybe not open access.

Decorin in the Tumor Microenvironment.

Advances in Experimental Medicine and Biology, 2020
The tumor microenvironment plays a determining role in cancer development through a plethora of interactions between the extracellular matrix and tumor cells. Decorin is a prototype member of the SLRP family found in a variety of tissues and is expressed in the stroma of various forms of cancer. Decorin has gained recognition for its essential roles in
Kornélia Baghy   +3 more
semanticscholar   +3 more sources

Selective inactivity of TGF-β/decorin complexes [PDF]

open access: yesFEBS Letters, 1994
Previous studies had shown that binding of TGF-β to the small proteoglycan decorin results in its inactivation. Indeed, in osteosarcoma cells the addition of decorin prevented the TGF-β1-mediated up-regulation of biglycan synthesis.
Andrej Hasilík   +2 more
exaly   +2 more sources

Decorin mediated biomimetic PCL-gelatin nano-framework to impede scarring.

International Journal of Biological Macromolecules, 2022
Scars occur as a result of fibrosis after tissue damage or surgery and reports suggest that excessive Transforming growth factor-β (TGF-β) activity during the process of wound healing leads to progressive fibrosis. Decorin is an extracellular matrix (ECM)
A. Vijayan   +6 more
semanticscholar   +1 more source

Biosynthesis of decorin and glypican

Matrix Biology, 2000
Decorin and glypican are two examples of exclusively chondroitin/dermatan sulfate and heparan sulfate-substituted proteoglycans, respectively. Decorin is a secretory product, whereas glypican is linked to membrane lipids via a glycosyl-phosphatidyl-inositol (GPI) anchor.
L A, Fransson   +5 more
openaire   +2 more sources

Effect of Exogenous Decorin on Cell Morphology and Attachment of Decorin-Deficient Fibroblasts

Journal of Biochemistry, 1996
We have reported deficient expression of decorin on skin fibroblasts from a patient with carbohydrate-deficient glycoprotein syndrome type I [Gu, J. and Wada, Y. (1995) J. Biochem. 117, 1276-1279]. The characteristics of fibroblasts from this patient included increased cell spreading and reduced proliferation.
J, Gu, Y, Wada
openaire   +2 more sources

Reconstruction of glycosaminoglycan chains in decorin

Biochemical and Biophysical Research Communications, 2002
The glycosaminoglycan chain of decorin from human spinal ligaments was digested using the hydrolysis of bovine testicular hyaluronidase. As a result, decorin with hexasaccharide, octasaccharide, and decasaccharide including the linkage region, GlcA-Gal-Gal-Xyl, was obtained.
Mito, Iwafune   +6 more
openaire   +2 more sources

Differential interactions of decorin and decorin mutants with type I and type VI collagens

FEBS Journal, 2004
The small leucine‐rich proteoglycan decorin can bind via its core protein to different types of collagens such as type I and type VI. To test whether decorin can act as a bridging molecule between these collagens, the binding properties of wild‐type decorin, two full‐length decorin species with single amino acid substitutions (DCN E180K, DCN E180Q ...
Gordon, Nareyeck   +5 more
exaly   +3 more sources

Small Leucine Rich Proteoglycans (decorin, biglycan and lumican) in cancer.

Clinica chimica acta; international journal of clinical chemistry, 2019
The extracellular matrix (ECM) prevents invasion of tumour cells and possesses an intrinsic mechanism to down-regulate signalling processes that promote cancer proliferation. Small Leucine Rich Proteoglycans (SLRPs) are ubiquitous ECM components involved
Sandeep Appunni   +5 more
semanticscholar   +1 more source

Home - About - Disclaimer - Privacy