• Clinical and Experimental Reproductive Medicine
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• 제48권4호
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• pp.303-310
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• 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
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• 제38권1호
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• pp.34-40
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• 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
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• 제29권12호
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• pp.2449-2452
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• 2008

• Archives of Pharmacal Research
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• 제23권2호
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• pp.182-186
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• 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
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• 제43권1호
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• pp.57-62
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• 2000

Phellinus igniarius의 배양방법별 균사체 및 단백다당류 생산수율비교 실험에서는 균사체내 다당류의 경우 모두 진탕배양이 효과적이었으나 균사체외 다당류의 경우 다당류 생산에서는 정치배양이 효과적이었다. 다당류의 정제는 조단백다당류를 이용하여 DEAE-cellulose column에 의한 1차 정제를 행하였고, 최종으로 Sepharose 2B를 이용한 2차 정제를 실시하여 최종적으로 균사체내 단백다당류의 탈이온수 분획물(PIIPDG)과 알칼리분획물(PIIPAG), 균사체외 단백다당류의 탈이온수 분획물(PIEPDG) 알칼리 분획물(PIEPAG)을 얻었다. 이때의 정제 수율은 1차 정제에서 40%의 회수율을 나타내었으며 2차 정제에서는 $38{\sim}61%$의 높은 회수율을 보였다. PIEPDG는 총당 79.0%, 총단백질 7.2%, PIEPAG는 총당 56.7%, 총단백질 40.8%, PIIPDG는 총당 64.8%, 총단백질 17.4%, PIIPAG는 총당 56.9%, 총단백질 41.5%으로 측정되었다. 각 단백다당류의 분자량은 PIEPDG 166KDa에서 PIEPAG 565KDa까지 모두 10만이 넘는 거대분자로 나타났다. 각 분획물의 단당류 조성을 볼때, PIEPDG는 glucose, PIIPDG와 PIIPAG는 glucose, inositol, PIEPAG는 glucose, rfructose, inositol이 검출되었다.

• 생약학회지
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• 제36권4호통권143호
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• pp.305-310
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• 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 $50\;{\mu}l/ml$.

• 한방재활의학과학회지
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• 제15권1호
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• pp.89-98
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• 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.

• 생명과학회지
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• 제21권4호
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• pp.534-541
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• 2011

Retinoic acid (RA)는 Vitamin A의 대사산물로서 토끼 관절 연골세포의 탈분화를 유도하는 물질로 알려져 있다. 그러나 RA가 탈분화를 조절하는 정확한 메커니즘은 잘 알려져 있지 않다. 따라서, Nitric Oxide (NO)가 유도하는 탈분화에 미치는 RA의 분자적 기전에 관한 연구를 수행하였다. 그 결과, RA는 NO가 유도하는 탈분화를 촉진시키는 것을 확인 할 수 있었다. 이와 같은 결과는 Western blot analysis를 통해 연골세포 분화의 표지 단백질인 type II collagen 및 Sox-9의 발현양상을 통해 확인 할 수 있었으며, Alcian blue staining을 통해 연골세포의 기질을 구성하고 있는 단백질인 sulfated proteoglycan의 발현량을 통해서도 확인 할 수 있었다. 또한, RA는 NO 가 유도하는 ERK의 활성을 더욱 증가 시켰다. ERK의 억제자인 PD98059를 사용하여 ERK의 활성을 억제하였을 때 RA가 감소시키는 type II collagen 및 Sox-9의 발현과 sulfated proteoglycan의 생성 양상이 PD98059에 의해 다시 회복되는 것을 확인 할 수 있었다. 이러한 모든 결과를 종합해 볼 때, RA는 NO가 유도하는 탈분화를 ERK 신호전달경로를 통해 조절하는 것을 확인 할 수 있었다.

• 생약학회지
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• 제33권3호통권130호
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• pp.224-229
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• 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.

• 한국균학회지
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• 제29권1호
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• pp.1-8
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• 2001

항암 효과와 면역 활성 효과가 있는 영지 균사체의 alkali 추출 단백다당류인 GMPG와 이것을 모체로하여 한외여과를 이용한 고분자 단백다당류(GMPG-UH)와 저분자 단백다당류(GMPG-UL) 그리고 column 분획을 이용한 고분자 단백다당류(GMPG-CH)와 저분자 단백다당류(GMPG-CL)를 얻어서, 면역 항암 활성을 연구한 결과 다음과 같은 결과를 얻었다. GMPG, GMPG 고분자 및 저분자 분획들의 총당과 총단백질 함량을 측정한 결과, GMPG는 85.9% 및 12.8%, 한외여과 분획인 GMPG-UH와 GMPG-UL은 75.5% 및 72.7%의 당과 31.3%의 33.6%의 단백질, 컬럼 분획인 GMPG-CH와 GMPG-CL은 당과 단백질이 각각 96.9%와 87.1% 및 1.9%와 8.1%를 함유하고 있었다. 구성 당은 대부분 glucose, mannose, fructose, galactose, xylose와 소량의 ribose 및 arabinose를 함유하고 있었으며, ${\alpha}$와 ${\beta}-glucose$의 결합 비율이 $0.84{\sim}1.14$로 ${\beta}-glucan$이 주를 이루는 단백다당류이고, 저분자보다는 고분자가 더 많은 ${\beta}$-결합을 이루고 있는 것으로 조사되었다. 구성 아미노산의 조성은 공통적으로 산성 아미노산인 Asp와 Glu, 중성 아미노산인 Ala와 Leu이 다량 함유하고 있는 것으로 조사되었다. IR의 경우는 ${\beta}$-당의 결합양식을 결정 짖는 $890cm^1$ 부근에서의 흡수 peak가 관찰되었다. 또한 $^{13}C-NMR$ spectrum에서 GMPG, GMPG 고분자 및 저분자, ${\beta}-1,3$ anomer를 결정 짖는 C-1 peak가 $103{\sim}105ppm$에서 나타나 ${\beta}-(1{\rightarrow}3)-glucan$ 구조를 갖는 단백다당류임을 알 수 있었다. GMPG-CH와 GMPG-CL은 sarcoma 180 고형암에 대해 각각 79.6% 및 63.4%의 암세포 중식 저해율을 나타내었는데, 이것은 ${\beta}$-결합 당의 함량이 높은 고분자 분획이 항암활성도 높게 나타났다.