Disease relevance of BGN

• Proteoglycans from bovine nasal septa and from the Swarm rat chondrosarcoma were isolated as aggregates (PGC) and as monomers (PGS) [1].
• The inhibition of synthesis of biglycan and decorin by IL-1 might be important in the pathophysiology of cartilage destruction in rheumatic diseases [2].
• No change was observed in molecular size of PGS, isolated chondroitin sulphates or keratan sulphate-protein cores in osteoarthrosis in comparison with non-osteoarthrotic cartilage from the same joint or from younger adult animals [3].

High impact information on BGN

• Addition of small amounts of proteoglycan subunit (PGS) blocked platelet aggregation, whereas chondroitin sulfate, a major glycosaminoglycan component of cartilage matrix, impaired platelet aggregation only at concentrations which resulted in a marked increase in viscosity [4].
• Moreover, PGS abolished aggregation of platelets by polylysine but did not prevent aggregation by ADP, suggesting that PGS may block strategically placed lysine sites on the collagen molecule [4].
• Similar leucine rich repeats have been identified in a number of proteins including the small interstitial proteoglycans decorin and PG-S1 [5].
• Crystal Structure of the Biglycan Dimer and Evidence That Dimerization Is Essential for Folding and Stability of Class I Small Leucine-rich Repeat Proteoglycans [6].
• We used light scattering to show that biglycan is dimeric in solution and solved the crystal structure of the glycoprotein core of biglycan at 3.40-A resolution [6].

Biological context of BGN

• The results indicate that CTGF suppresses the synthesis of biglycan but newly induced that of decorin in the cells when the cell density is low; in addition, no change was observed in the hydrodynamic size and the glycosaminoglycan chain length of these two small chondroitin/dermatan sulfate proteoglycans [7].
• Two overlapping cDNA clones for core protein of a biglycan of bovine aorta were isolated from a pSPORT bovine aorta tissue cDNA library [8].
• The nucleotide sequence of the protein core for bovine aortic smooth muscle cell biglycan was determined using recombinant DNA technology [9].
• The bovine biglycan protein core has four potential O-linked and two potential N-linked glycosylation sites and is composed of 11 leucine-rich repeat units [9].
• Analysis of the deduced amino acid sequence for bovine biglycan revealed a striking homology, 94.6% and 95.7%, to human and rat biglycan, respectively [9].

Anatomical context of BGN

• Differential regulation of biglycan and decorin synthesis by connective tissue growth factor in cultured vascular endothelial cells [7].
• Overall the study supports the concept that biglycan may have a specific role in the elastinogenic phase of elastic fiber formation [10].
• Biglycan changed the cell shape of fibroblasts with formation of long protruding filamentous processes [11].
• The self-association of biglycan from bovine articular cartilage [12].
• The small, leucine-rich proteoglycans, decorin and biglycan, are prominent components of many extracellular matrices and are differentially regulated in various tissues [13].

Associations of BGN with chemical compounds

• Primary structure of bovine aorta biglycan core protein deduced from cloned CDNA [8].
• In 6 M guanidine chloride, biglycan is a monomer with s0(20,w) = 2.9 S and Mz = 93,100 (where Mz is z-average molecular weight) [12].
• Differential regulation of biglycan and decorin by retinoic acid in bovine chondrocytes [13].
• The heparan sulfate PG and CS/DSPG core proteins were identified as perlecan and biglycan, respectively, by Western blot analysis [14].
• In contrast, the repression of biglycan by RA was not significantly altered by cycloheximide, showing that the repression was a direct effect [13].

Regulatory relationships of BGN

• Excess decorin added to cell culture medium did not affect the ability of TGF-beta to enhance synthesis of biglycan [15].

Other interactions of BGN

• Similar results were obtained with purified bovine DCN and BGN [16].
• The assumed centromere transposition between HSAX and BTAX associated with the rearranged chromosome segments is supported by cytogenetic assignments of the genes BGN and G6PD to BTAX [17].
• Bovine lumican had about 50% identity to bovine fibromodulin and 20% identity to bovine decorin and biglycan [18].
• We have separated a dermatan sulfate proteoglycan, epiphycan, from decorin and biglycan by using dissociative extraction of bovine fetal epiphyseal cartilage, followed by sequential ion-exchange, gel permeation, hydrophobic, and Zn2+ chelate chromatographic steps [19].
• Expression of these marker compounds was reduced in fibroblasts and also in transforming growth factor-beta-induced myofibroblasts, which expressed high levels of alpha-smooth muscle actin, biglycan, and the extra domain A (EDA or EIIIA) form of cellular fibronectin [20].

Analytical, diagnostic and therapeutic context of BGN

• This was demonstrated by electron microscopy after negative staining of gold-labeled biglycan in aggregation experiments with collagen VI [21].
• Biglycan but not decorin mRNAs were detected by Northern analysis and by PCR [22].
• It was previously concluded on the basis of immunodiffusion studies that GPL has two antigenic components, one in common with PGS and one specific for the link proteins [23].
• Bovine nasal cartilage proteoglycan aggregates are dissociated and separated by density gradient centrifugation in 4 M guanidine into proteoglycan subunit (PGS) and glycoprotein link (GPL) fractions, the latter containing hyaluronic acid and "link proteins" responsible for aggregate formation [23].
• This finding was consistent with Northern blot analysis which showed that steady-state biglycan mRNA levels increased significantly during the elastinogenic period [24].

References