Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues.

Bianco, Patrizia Del; Fisher, Larry W.; Young, Marian F.; Termine, John D.; Robey, Pamela Gehron

doi:10.1177/38.11.2212616

Cited by 617 publications

(393 citation statements)

References 14 publications

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“…The lower region of subepithelial mesenchyme might be matured and stabilized in the histological structure in view of the distribution of type I collagen and general histological findings [1]. It has been shown that decorin was distributed in the collagen rich region in the skin and skeletal muscles in human and bovine fetuses [2,13]. This was also the case in the present results as to the fetal bovine rumen.…”

Section: A)supporting

confidence: 75%

Identification of Bovine Decorin in the Fetal Bovine Rumen.

Takanosu

Amasaki²,

Miura

et al. 1997

The Journal of Veterinary Medical Science

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ABSTRACT. Immunohistochemical localization of bovine decorin was examined with its biological analysis in the fetal bovine rumen. By immunohistochemical staining, monoclonal antibody (mAb) 2B6, which recognizes chondroitin 4-sulfate and/or dermatan sulfate (DS), reacted specifically to the lower mesenchymal region in the developing ruminal wall. Biochemical analysis of the extract from the developing rumen revealed that the molecule detected immunohistochemically by mAb 2B6 was small DS proteoglycan, bovine decorin. These results support the view that bovine decorin is involved in organization of the fetal bovine ruminal mesenchyme as a collagenous tissue. -KEY WORDS: decorin, extracellular matrix, proteoglycan.J. Vet. Med. Sci. 59(2): 121-123, 1997 A). Monoclonal antibody (mAb) 2B6 was raised against the bovine articular cartilage PG digested with chondroitinase ABC, and therefore, mAb 2B6 recognizes the epitope as the unsaturated uronic acid-N-acetylegalactosamine 4-sulfate disaccharide unit from chondroitin 4-sulfates remaining on the core proteins [5]. MAb 2B6 reacts to C4S and DS after chondroitinase ABC treatment, and to C4S alone after chondroitinase AC treatment [4,5]. After chondroitinase ABC treatment, immunoreaction by mAb 2B6 was detected in the lower region of the mesenchyme, but never in the superficial region of ruminal wall in the developing rumen (Figs. 1a, b). After chondroitinase AC treatment, no immunoreaction was detected in the serial sections (Fig. 1c). Therefore, the immunoreaction of mAb 2B6 was attributed to DS-PG. Immunoreaction of mAb 2B6 was first detected in a 9 cm CRL fetus, and also in the lower mesenchymal region in longer fetuses at later developmental stages (data not shown).DEAE-chromatography of the urea-extract of the fetal bovine rumen gave a single peak of uronate (Fig. 2). Cellulose-acetate membrane electrophoresis of GAG chains in this fraction obtained by treatment with 0.1 N NaOH showed the same mobility with standard DS (Fig. 3), suggesting that the uronate containing molecules obtained from DEAE-column corresponded to DS chains. DEAEpreparation gave a major band at 45 kD on SDS-PAGE after digestion with chondroitinase ABC (Fig. 4, lane 3), and this band immunoreacted against mAb 2B6 on western blotting (Fig. 4, lane 4). The intact sample gave a diffuse band at 80-120 kD (Fig. 4, lane 5). Therefore, DEAEpreparation may correspond to DS-PG detected by mAb 2B6 in the tissue section. Gel-chromatography of DEAEpreparation gave a major peak corresponding to the molecular weight on SDS-PAGE and a minor peak at higher molecular weight (Fig. 5). The component in the major peak was analyzed for amino acid sequence by Edman degradation. Amino acid sequence was identical with that of bovine bone decorin deduced from cDNA [9], indicating that the molecule detected by mAb 2B6 in the fetal bovine ruminal extract corresponded to bovine decorin ( A group of proteoglycans (PGs) is a member of extracellular matrix (ECM), containing various types of glycosaminoglycans (GAGs) [15]. P...

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Section: A)supporting

confidence: 75%

Identification of Bovine Decorin in the Fetal Bovine Rumen.

Takanosu

Amasaki²,

Miura

et al. 1997

The Journal of Veterinary Medical Science

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“…Biglycan has been shown to be processed by BMP1/TLD-like proteinases in vitro and in vivo . Since biglycan is thought to play a positive role in bone formation (Bianco et al, 1990) and to be involved in regulating TGFβ signaling (Chen et al, 2002), its processing may represent novel mechanisms by which BMP1/TLD-like proteinases affect osteogenesis and TGFβ signaling (also see below), respectively. It should be cautioned however that it is not yet known how processing affects biglycan function.…”

Section: Non-collagenous Matrix Proteinsmentioning

confidence: 99%

The bone morphogenetic protein 1/Tolloid-like metalloproteinases

2007

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A decade ago, bone morphogenetic protein 1 (BMP1) was shown to provide the activity necessary for proteolytic removal of the C-propeptides of procollagens I-III: precursors of the major fibrillar collagens. Subsequent studies have shown BMP1 to be the prototype of a small group of extracellular metalloproteinases that play manifold roles in regulating formation of the extracellular matrix (ECM). Soon after initial cloning of BMP1, genetic studies showed the related Drosophila proteinase Tolloid (TLD) to be necessary for formation of the dorsal-ventral axis in early embryogenesis. It is now clear that the BMP1/TLD-like proteinases, conserved in species ranging from Drosophila to humans, act in dorsal-ventral patterning via activation of transforming growth factor β (TGFβ)-like proteins BMP2, BMP4 (vertebrates) and decapentaplegic (arthropods). More recently, it has become apparent that the BMP1/TLD-like proteinases are key activators of a broader subset of the TGFβ superfamily of proteins, with implications that these proteinases may be key in orchestrating formation of ECM with growth factor activation and BMP signaling in morphogenetic processes.

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“…Epiphyseal cartilage stains prominently for decorin and only weakly for biglycan, whereas in presumptive articular cartilage biglycan is found in the pericellular matrix whereas this developing zone is free of decorin. 30 In adult articular cartilage decorin is present in the interterritorial matrix while biglycan is found in the pericellular matrix. Decorin is associated with collagen fibrils as a decorating proteoglycan and carries one chondroitin or dermatan sulfate side chain.…”

Section: Other Than Aggrecanmentioning

confidence: 99%