Disease relevance of Bgn

• In vivo, in a model of mesangioproliferative glomerulonephritis up-regulation of inducible nitric-oxide synthase mRNA was associated with reduced expression of biglycan in isolated glomeruli [1].
• Biglycan mRNA expression in rat myocardium after abdominal aortic banding with renal ischemia was examined [2].
• The marked alterations of biglycan and decorin during the development of fibrosis suggests that these proteoglycans have a regulating role in this process [3].
• Expression of the proteoglycans biglycan and decorin and of transforming growth factor-beta 1 at various stages of liver fibrosis induced experimentally in rats by oral administration of thioacetamide was examined [4].
• In the tubulointerstitium of diseased kidneys (polycystic kidneys, 5/6-nephrectomy, kidneys from the Milan normotensive strain) there was a general up-regulation of decorin expression, while biglycan was localized only in distinct foci of fibrotic lesions [5].

High impact information on Bgn

• Ang II treatment of rat mesangial cells in culture increased TGF-beta and matrix components biglycan, fibronectin, and collagen type I at both the mRNA and protein levels in a time- and dose-dependent manner [6].
• Decorin mRNA, in contrast to biglycan decreased and reached 20% of control on day 10 [3].
• After the increase of TGF-beta 1 mRNA the messages for biglycan and collagen III steadily increased to reach a maximum 10 d after bleomycin instillation [3].
• Biglycan gene expression levels coincided tightly with the activity and extent of fibrosis, fat-storing cells and their transformed form, the myofibroblast-like cells, being the major contributors [4].
• Biglycan and decorin gene expression in normal and fibrotic rat liver: cellular localization and regulatory factors [7].

Chemical compound and disease context of Bgn

• Kinetics of biglycan, decorin and thrombospondin-1 in mercuric chloride-induced renal tubulointerstitial fibrosis [8].

Biological context of Bgn

• More importantly, biglycan protected mesangial cells from apoptosis by decreasing caspase-3 activity, and it counteracted the proliferative effects of platelet-derived growth factor-BB [1].
• Further studies showed that biglycan inhibited cell adhesion on type I collagen and fibronectin because of its binding to these substrates [1].
• The highest frequency of amino acid substitutions occurring between rat, bovine and human biglycan core proteins was found to reside within a small hypervariable region located near the N-terminus of these proteoglycans [9].
• Nucleotide sequence analysis demonstrated that these clones encoded the rat VSM biglycan complete core protein sequence [9].
• Two overlapping cDNA clones containing sequences homologous to human bone biglycan were isolated from a rat vascular smooth muscle (VSM) cell cDNA library [9].

Anatomical context of Bgn

• Tissue sections were incubated with antibodies to the small, leucine-rich PG, decorin, and biglycan and collagen type I. Airways were classified according to basement membrane perimeter length (< or =0.99, 1-2.99, and > or =3 mm) [10].
• Biglycan, a nitric oxide-regulated gene, affects adhesion, growth, and survival of mesangial cells [1].
• Vascular smooth muscle biglycan represents a highly conserved proteoglycan within the arterial wall [9].
• A marked increase in biglycan mRNA signal expression was also observed in endothelial cells and smooth muscle cells of the thickened myocardial capillary wall [2].
• Transiently acidified (but not native) conditioned media from Kupffer cells and myofibroblastlike cells and transforming growth factor-beta 1 enhanced the relative abundances of biglycan and decorin messenger RNAs up to five times in primary-cultured fat-storing cells [7].

Associations of Bgn with chemical compounds

• Employing this approach, biglycan expression turned out to be down-regulated time- and dose-dependently either by interleukin-1beta-stimulated endogenous nitric oxide production or by direct application of the exogenous nitric oxide donor, diethylenetriamine nitric oxide [1].
• Biglycan expression could be normalized, both in vitro and in vivo, by using a specific inhibitor of the inducible nitric-oxide synthase, l-N6-(l-iminoethyl)-l-lysine dihydrochloride [1].
• The expression of genes encoding the core proteins of the novel small chondroitin/dermatan sulfate proteoglycans decorin and biglycan was studied in the livers of normal rats and in liver tissue during fibrogenesis induced by prolonged bile-duct ligation and thioacetamide poisoning [7].
• Specifically, the synthesis of the small soluble PG, biglycan, was decreased by exposure to 50% O2 [11].
• Levels of mRNA for the proteoglycan, biglycan (as assessed by Northern blot analysis), also were comparable between the standard and elevated glucose conditions [12].

Other interactions of Bgn

• Whereas biglycan was readily detected within the ASM, decorin and collagen were detected outside the ASM and especially in the adventitial layer [10].
• AngII treatment also resulted in significant increases in the mRNA of the core proteins, versican, biglycan, and perlecan [13].
• Northern blot, RT-PCR, Western blot, and promoter activity assays revealed that HGF caused a significant increase in decorin mRNA and protein, as well as in biglycan mRNA, protein, and promoter activity, suggesting transcriptional control of gene expression [14].
• RT-PCR analysis showed that versican mRNA was highly expressed at P1 but was little expressed at P42. mRNAs for other chondroitin sulfate proteoglycans including biglycan, aggrecan, and decorin did not change much between P1 and P42 [15].
• Alkaline phosphatase (AP), osteocalcin (OC), metalloproteinases (MMP-2 and -14), procollagenase C (BMP-1), biglycan (BG) and integrin 1 are expressed at higher levels in FMS*-treated osteoblasts than in control cultures [16].

Analytical, diagnostic and therapeutic context of Bgn

• The Northern blot analysis demonstrated that expression of biglycan mRNA in the pressure-overloaded hearts on days 2, 7, 14 and 28 was 2.88 +/- 0.89, 2.32 +/- 0.49, 2.17 +/- 0.57 and 1.81 +/- 0.46-fold higher, respectively, than that in the sham-operated hearts [2].
• In situ hybridization showed an increased density of biglycan mRNA signal-positive cells in the pressure-overloaded hearts [2].
• The main induced proteoglycans were identified as biglycan and decorin by immunoprecipitation with antiserum made against synthetic peptides from the proteoglycan core proteins [17].
• Immunocytochemistry showed intense immunostaining of biglycan and fibromodulin in the areas of injured lung tissue from rats 14 and 28 d after BM administration [18].
• Microarray analysis revealed that many proteoglycan core proteins change during kidney development (syndecan-1,2,4, glypican-1,2,3, versican, decorin, biglycan) [19].

References