• Clinical and Experimental Reproductive Medicine
• /
• v.48 no.4
• /
• pp.303-310
• /
• 2021

Decorin (DCN) is a proteoglycan belonging to the small leucine-rich proteoglycan family. It is composed of a protein core containing leucine repeats with a glycosaminoglycan chain consisting of either chondroitin sulfate or dermatan sulfate. DCN is a structural component of connective tissues that can bind to type I collagen. It plays a role in the assembly of the extracellular matrix (ECM), and it is related to fibrillogenesis. It can interact with fibronectin, thrombospondin, complement component C1, transforming growth factor (TGF), and epidermal growth factor receptor. Normal DCN expression regulates a wide range of cellular processes, including proliferation, migration, apoptosis, and autophagy, through interactions with various molecules. However, its aberrant expression is associated with oocyte maturation, oocyte quality, and poor extravillous trophoblast invasion of the uterus, which underlies the occurrence of preeclampsia and intrauterine growth restriction. Spatiotemporal hormonal control of successful pregnancy should regulate the concentration and activity of specific proteins such as proteoglycan participating in the ECM remodeling of trophoblastic and uterine cells in fetal membranes and uterus. At the human feto-maternal interface, TGF-β and DCN play crucial roles in the regulation of trophoblast invasion of the uterus. This review summarizes the role of the proteoglycan DCN as an important and multifunctional molecule in the physiological regulation of oocyte maturation and trophoblast migration. This review also shows that recombinant DCN proteins might be useful for substantiating diverse functions in both animal and in vitro models of oogenesis and implantation.

• BMB Reports
• /
• v.38 no.1
• /
• pp.34-40
• /
• 2005

GLPG (Ganoderma lucidum proteoglycan) was a bioactive fraction obtained by the liquid fermentation of the mycelia of Ganoderma lucidum, EtOH precipitation, and DEAE-cellulose column chromatography. GLPG was a proteoglycan with a carbohydrate: protein ratio of 10.4: 1. Its antiviral activities against herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) were investigated using a cytopathic inhibition assay. GLPG inhibited cell death in a dose-dependent manner in HSV-infected cells. In addition, it had no cytotoxic effect even at 2 mg/ml. In order to study the mode of action of the antiviral activity of GLPG, cells were treated with GLPG before, during, and after infection, and viral titer in the supernatant of cell culture 48 h post-infection was determined using a $TCID_{50}$ assay. The antiviral effects of GLPG were more remarkable before viral treatment than after treatment. Although the precise mechanism has yet to be defined, our work suggests that GLPG inhibits viral replication by interfering with the early events of viral adsorption and entry into target cells. Thus, this proteoglycan appears to be a candidate anti-HSV agent.

• Bulletin of the Korean Chemical Society
• /
• v.29 no.12
• /
• pp.2449-2452
• /
• 2008

• Archives of Pharmacal Research
• /
• v.23 no.2
• /
• pp.182-186
• /
• 2000

Chondroitin sulfates proteoglycans were isolated from human placenta. For the identification of enzymatic digestion products of isolated proteoglycan, strong anion exchange-high performance liquid chromatography (SAX-HPLC) was performed. By the action of chondroitin ABC and chondroitin B lyase, three unsaturated disaccharides 2-acetamide-2-deoxy-3-O-($\beta$-D-gluco-4-enepyranosyluronic acid)-D-galactose ($\delta$Di-OS), 2-acetamide-2-deoxy-3-O-($\beta$-D-gluco-4-enepyranosyluronic acid)-6-O-su lfo-D-galactose ($\delta$Di-6S) and 2-acetamide-2-deoxy-3-O-($\beta$-D-gl uco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose ($\delta$Di-4S) were produced from the human placenta proteoglycan. The anticoagulant activity of chondroitin sulfate proteoglycan was evaluated by activated partial thromboplastin time (aPTT) assay and thrombin time (TT) assay. The clotting times of aPTT and TT were increased from 72 to 144 sec and 19 to 27 sec, respectively. The Immune-modulating activity of chondroitin sulfate proteoglycan was examined by cell proliferation assay and these results suggest that it may play a role in suppression of the function of immune-related cells.

• Applied Biological Chemistry
• /
• v.43 no.1
• /
• pp.57-62
• /
• 2000

The proteoglycan, intracellular and extracellular, extracted from the liquid culture of Phellinus igniarius were purified and characterized. The mycelial productivity was proved to be better in shaking culture compared to standing culture. The productivity of intracellular proteoglycan of Phellinus igniarius appeared to be similar in two culturing methods. The standing culture of Phellinus igniarius produced 6 times as much extracellular proteoglycan compared to shaking culture. The proteoglycan were purified to a single peak by ion exchange chromatography(DEAE-cellulose) followed by gel filtration(Sepharose 2B). PIEPDG contained 79.0% total sugar and 7.2% protein. PIEPAG contained 56.7% total sugar and 40.8% protein. PIIPDG contained 64.8% total sugar and 17.4% protein. PIIPAG contained 56.9% total sugar and 41.5%n protein. The molecular weights of all the fractions were estimated to be above 100,000, from 134KDa of PIEPDG to 560 KDa of PIEPAG. The results of sugar analysis by HPLC showed that PIEPDG contains glucose only. The sugar part of PIIPDG and PIIPAG were consisted of glucose and inositol. The PIEPAG contained three kinds of monosaccharides, glucose, fructose and inositol.

• Korean Journal of Pharmacognosy
• /
• v.36 no.4 s.143
• /
• pp.305-310
• /
• 2005

Sarcodon aspratus (Thelepholaceae), a native mushroom, is distributed in Korea and Japan, and has been widely used in traditional food and fork medicines. To confirm the biological activities of Sarcodon aspratus, the liver protecting activity, anti-clotting activity, and anti-complementary activity of the water extract, EtOH extract, and the water soluble proteoglycan part of S. aspratus were investigated. The EtOH, and water extract of S. aspratus decreased the GOT and GPT releases induced by $CCl_4$ in a dose-dependant manner. On the other hand, the water soluble proteoglycan part of S. aspratus showed weak inhibitory activity. In addition, the EtOH and water extract of S. aspratus prevented $CCl_4-induced$ hepatotoxicity, as described by a liver histopathologic study. To confirm the anti-clotting activity, the APTT and PT assay were carried out. As a result, only the crude proteoglycan part of S. aspratus showed the anti-coagulating activity, and this result might be due to the inhibition of intrinsic clotting system. Also, the crude proteoglycan part of S. aspratus showed the anti-complementary activity, and the $IC_{50}$ value was $50\;{\mu}l/ml$.

• Journal of Korean Medicine Rehabilitation
• /
• v.15 no.1
• /
• pp.89-98
• /
• 2005

Objectives : This study was to investigate the effects of Clematidis Radix on Proteoglycan(PG) degradation by measuring of body weight, Glycosaminoglycan(GAG), Interleukin-$1{\beta}$($IL-1{\beta}$) in synovial fluid, and PG content of articular cartilage of femur in collagenase-induced arthritis in rats. Methods : Arthritis was induced by injection of collagenase(0.1 ml) into knee joint of rats. Arthritic rats were divided into control(n=8) and treated(n=8) group. Control group was taken normal saline for 15 days and treated group was taken extracts of Clematidis Radix for same duration. Normal group(n=8) was injected with normal saline and was taken normal saline for 15 days. Body weight was measured at 0, 10, 15 days after injection. GAG, $IL-1{\beta}$ in synovial fluid were measured with ELISA kit at 15 days after injection. PG content of articular cartilage of femur, represented by safranine O staining, was measured at 15 days after injection. Histopathological study on the articular cartilage of knee joint was investigated at 15 days after injection. Results : Body weight, PG of treated group, taken Clematidis Radix, were significantly increased, and GAG was significantly decreased compared with control group. But $IL-1{\beta}$ was not significantly decreased. Conclusions : On the basis of these results, we concluded that Clematidis Radix has inhibiting effects on the proteoglycan degradation in collagenase-induced rat osteoarthritis model.

• Journal of Life Science
• /
• v.21 no.4
• /
• pp.534-541
• /
• 2011

Retinoic acid (RA), a metabolite of vitamin A, is known to regulate dedifferentiation of rabbit articular chondrocytes. The regulatory mechanism of dedifferentiation by RA is not yet understood. Thus, the effect of RA on the regulation of nitric oxide (NO)-induced dedifferentiation was investigated in rabbit articular chondrocytes. RA caused loss of the differentiated chondrocyte phenotype as demonstrated by inhibition of type II collagen expression and proteoglycan synthesis. RA also accelerated NO-induced dedifferentiation in rabbit articular chondrocytes as detected by expression of type II collagen and Sox-9 using Western blot analysis and production of sulfated proteoglycan using Alcain blue staining. Further, RA potentiated NO-induced activation of ERK. Inhibition of ERK with PD98059 (PD) recovered the expression of type II collagen and Sox-9 and production of sulfate proteoglycan in NO-induced dedifferentiated chondrocytes by RA treatment. Our findings suggest that RA accelerates NO-induced dedifferentiation of rabbit articular chondrocytes via the ERK pathway.

• Korean Journal of Pharmacognosy
• /
• v.33 no.3 s.130
• /
• pp.224-229
• /
• 2002

Sarcodon aspratus (Thelephoraceae), a native mushroom distributed in Korea and Japan has been widely used as a traditional food and folk medicines. Two proteoglycan polysaccharides, named SAP-A and SAP-B were isolated from the fruitbody of S. aspratus. Their molecular weight were determined as 6184.9 D, and 25749.2 D, respectively, by maldi-tof ms. The composition of sugar and amino acid of these compounds was also determined. The SAP-A showed potent antitumor activity. The $ID_{50}$ value of SAP-A was 8.2 mg/kg/day for ICR mice transplanted with solid sarcoma-180, and the elongation of lifespan effect was 167.4% for ICR mice transplanted with ascitic sarcoma-180. Moreover, the elongation life-span effect of SAP-A increased dose-dependently.

• The Korean Journal of Mycology
• /
• v.29 no.1
• /
• pp.1-8
• /
• 2001

To examine the structural properties of the proteoglycan (GMPG, Ganoderma lucidum mycelial proteoglycan) obtained from mycelia in Ganoderma lucidum IY009, we obtained the low and high molecular proteoglycan by ultrafiltration and sepharose CL-4B column chromatography. The physicochemical properties of these fractions were as follows. When the proteoglycan separated by ultrafiltration and sepharose CL-4B column chromatography, its was not fractionated completely. The molecular weight of high molecular proteoglycan by the gel column chromatography (CH) was 250 kD and 2,000 kD, and low molecular proteoglycan was 12kD. The total carbohydrate was consisted of 75.7% (UH) and 96.7% (CH), and the low fraction was 72.7% (UL) and 87.1% (CL), respectively. The sugar of high and low molecular proteoglycan composed of glucose, mannose, fructose, galactose, xylose, ribose and arabinose. Glucose contents of all fraction were ranged from $46.9%{\sim}82.4%$ of the total sugar and the ratio of ${\alpha}$\;and\;{\beta}-glucose$ was $0.84{\sim}1.14$, and its indicated the proteoglycan to be ${\beta}-glucan$. Amino acids pattern showed that the fractions contained a large amount of aspartie acid, glutamic acid, alanine and leucine. These fractions showed the characteristics of IR absorption for ${\beta}-glucan$ at $890\;cm^{-1}\;and\;^{13}C-NMR$ spectroscopy showed the presence of the ${\beta}-1,3-glucan$ and a ${\beta}-1,6-glucan$.