Disease relevance of DCN

• The avian low score normal muscle weakness alters decorin expression and collagen crosslinking [1].
• Cardiac decorin and Type I collagen expression and collagen fibrosis were examined in a chicken line exhibiting the low score normal (LSN) genetic muscle weakness and compared to normal cardiac muscle at 14 and 20 d of embryonic development and at 1 and 6 wk posthatch [2].
• Loss of decorin from the surface zone of articular cartilage in a chick model of osteoarthritis [3].

High impact information on DCN

• DCN II was found to contain two dermatan sulfate chains, whereas DCN I had a single dermatan sulfate chain [4].
• Decorin, a member of a family of proteins with leucine-rich repeat motifs, is a widely distributed extracellular matrix proteoglycan that is thought to be responsible for the structure, tissue organization, and surface properties of fibrils [4].
• Isolation and partial characterization of lumican and decorin from adult chicken corneas. A keratan sulfate-containing isoform of decorin is developmentally regulated [5].
• The results of this study suggest that adult chick corneas contain two isoforms of decorin: one containing C/DS side chains and the other, a hybrid, containing both C/DS and KS side chains [5].
• These results suggest that different post-translational modifications occur to the decorin gene product during corneal development and maturation [5].

Chemical compound and disease context of DCN

• In the current study, chicken myogenic satellite cells isolated from the pectoralis major muscle from the chicken genetic muscle weakness, low score normal (LSN), and normal pectoralis major muscle were used to investigate TGF-beta expression as it relates to decorin and beta1 integrin mRNA expression [6].

Biological context of DCN

• Comparison of deduced amino acid sequences shows that two of five amino acid differences in the mature protein between quail and chick decorin, and two of three for lumican, are non-conservative [7].
• These data suggest that the increase in decorin expression may be associated with a modification in a TGF-beta signal transduction pathway [8].
• In the avian genetic muscle weakness, low score normal (LSN), satellite cell proliferation and differentiation rates are significantly lower than that observed in normal chicken satellite cells, which may be attributed to a late embryonic increase in the expression of decorin [9].
• Decorin and collagen type I gene expression in avian low score normal pectoral muscle [10].
• Effect of transforming growth factor-beta on decorin and beta1 integrin expression during muscle development in chickens [6].

Anatomical context of DCN

• The effects of beta-D-xyloside on the synthesis of proteoglycans by skeletal muscle: lack of effect on decorin and differential polymerization of core protein-bound and xyloside-linked chondroitin sulfate [11].
• Decorin is highly expressed in sclera and sternum, whereas lumican is expressed in these tissues, as well as in liver, at very low levels [7].
• Exercise led to an increase in the size of the tendons, the content of hyaluronic acid, and the level of decorin [12].
• Immunolocalization of these proteoglycans shows that versican is initially present in pericellular locations around developing myotubes, whereas decorin is observed in the epimysium early in development, and then its distribution gradually spreads to also include the perimysium and endomysium [13].
• Based on the reported functions of decorin as a regulator of cell proliferation and collagen fibril organization, it is possible that the late embryonic increase in decorin may be influencing the alterations in LSN sarcomere and collagen organization [14].

Associations of DCN with chemical compounds

• cDNA clone to chick corneal chondroitin/dermatan sulfate proteoglycan reveals identity to decorin [15].
• Chick decorin contains three variations of this sequence that are tandemly linked to form a unit and three units tandemly linked to form the leucine-rich region [15].
• Similarly, EDTA selectively removed decorin compared with HCl, formic, acetic, or citric acids [16].
• The addition of exogenous TGF-beta decreased decorin expression during differentiation and reduced beta1 integrin expression at 24 and 48 h of differentiation [6].
• Monoclonal antibodies 6D6, CS-56 and AH12 specific to dermatan sulphate proteoglycan (decorin), chondroitin sulphate and keratan sulphate, respectively, were used [17].

Other interactions of DCN

• A 19-amino-acid match with sequence from the N-terminus of core protein from the corneal chondroitin/dermatan sulfate proteoglycan confirmed the clone as a corneal proteoglycan and the homology with human and bovine decorin confirmed its identity as decorin [15].
• SDS-PAGE indicated that decorin was present in all regions and fibromodulin was mainly observed in the tensile region [18].
• The LSN condition has elevated expression of TGF-beta2 and TGF-beta4 with increased expression of decorin and decreased beta1 integrin during myogenic satellite cell proliferation and differentiation [6].
• Compared to normal skeletal muscle, LSN muscle has normal myosin isoform switching and cell-cell recognition, elevated glycosaminoglycan and decorin levels at embryonic Day 20, and a large increase in collagen crosslinking at 6 wk posthatch [10].

Analytical, diagnostic and therapeutic context of DCN

• When fractionated on Sepharose CL-4B, scleral proteoglycans were resolved into two peaks which were identified by Western blot analysis as aggrecan (cartilage proteoglycan) and decorin [19].
• Molecular cloning and relative tissue expression of decorin and lumican in embryonic quail cornea [7].
• Normal satellite cell cultures were treated with the addition of exogenous TGF-beta during differentiation to determine if the altered expression of LSN decorin and beta1 integrin was associated with TGF-beta expression [6].
• Immunoblotting of these proteins was positive for the small proteoglycans fibromodulin and decorin, respectively [20].

References