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Induction of nucleolin translocation by acharan sulfate in A549 human lung adenocarcinoma
Joo, Eun Ji,Yang, Hui,Park, Youmie,Park, Nam Young,Toida, Toshihiko,Linhardt, Robert J.,Kim, Yeong Shik Wiley Subscription Services, Inc., A Wiley Company 2010 Journal of cellular biochemistry Vol.110 No.5
<P>Acharan sulfate (AS), isolated from the giant African snail Achatina fulica, is a novel glycosaminoglycan, consisting primarily of the repeating disaccharide structure α-D-N-acetylglucosaminyl (1 → 4) 2-sulfoiduronic acid. AS shows anti-tumor activity in vitro and in vivo. Despite this activity, AS is only weakly cytotoxic towards cancer cells. We examine the interactions between AS and cell-surface proteins in an effort to explain this anti-tumor activity. Using flow cytometry and affinity column chromatography, we confirm that AS has strong affinity to specific cell-surface proteins including nucleolin (NL) in A549 human lung adenocarcinomas. Surprisingly, we found the translocation of NL from nucleus to cytoplasm under the stimulation of AS (100 µg/ml) in vitro. Also, as NL exits the nucleus, the levels of growth factors such as bFGF and signaling cascade proteins, such as p38, p53, and pERK, are altered. These results suggest that the communication between AS and NL plays a critical role on signal transduction in tumor inhibition. J. Cell. Biochem. 110: 1272–1278, 2010. Published 2010 Wiley-Liss, Inc.</P>
Isolation and Characterization of Chondroitin Sulfates from the Byproducts of Marine Organisms
A-Rang Im,Joon-Soo Sim,Youmie Park,Bum-Soo Hahn,Toshihiko Toida,Yeong Shik Kim 한국식품과학회 2009 Food Science and Biotechnology Vol.18 No.4
By-products of marine organisms including salmon, skate, flatfish, and yellow goosefish were investigated to search for new source of chondroitin sulfate (CS). Agarose gel electrophoresis with chondroitinase depolymerization showed that purified chondroitin sulfate did not contain any other glycosaminoglycans. ¹H-nuclear magnetic resonance (NMR) spectra were acquired to confirm the structure and purity. The average molecular weight ranging from 22 to 64 kDa was determined by high performance size exclusion chromatography. Disaccharide compositions and purities were determined by strong anion exchange-high performance liquid chromatography (SAX-HPLC) after chondroitinase ABC depolymerization. SAX-HPLC data exhibited that the purity was from 81.7±1.3 to 114.2±2.5% and the yield was from 1.3 to 12.5%. All analytical results indicate that salmon cartilage, skate cartilage, and yellow goosefish bone could be promising sources of CS to substitute shark cartilage CS in commercial neutraceuticals.
Isolation and Characterization of Chondroitin Sulfates from the By-products of Marine Organisms
A-Rang Im,Joon-Soo Sim,Youmie Park,Bum-Soo Hahn,Toshihiko Toida,Yeong Shik Kim 한국당과학회 2010 한국당과학회 학술대회 Vol.2010 No.1
The by-products of marine organisms including salmon, skate, flatfish, and yellow goosefish were investigated to search for new source of chondroitin sulfate. Agarose gel electrophoresis with chondroitinase depolymerization showed that purified chondroitin sulfate did not contain any other glycosaminoglycans. 1H-NMR spectra were acquired to confirm the structure and purity. The average molecular weight ranging from 22 to 64 kDa was determined by high-performance size exclusion chromatography. Disaccharide compositions and purities were determined by strong anion exchange-high performance liquid chromatography after chondroitinase ABC depolymerization. Strong anion exchangehigh- performance size exclusion chromatography data exhibited that the purity was from 81.7±1.3 to 114.2±2.5% and the yield was from 1.3 to 12.5%. All analytical results indicate that salmon cartilage, skate cartilage, and yellow goosefish bone could be promising sources of chondroitin sulfate to substitute shark cartilage chondroitin sulfate in commercial neutraceuticals.
Induction of Nucleolin Translocation by Acharan Sulfate in A549 Human Lung Adenocarcinoma
Eun Ji Joo,Yang Hui,Youmie Park,Nam Young Park,Toshihiko Toida,Robert J. Linhardt,Yeong Shik Kim 한국당과학회 2010 한국당과학회 학술대회 Vol.2010 No.1
Acharan sulfate (AS), isolated from the giant African snail Achatina fulica, is a novel glycosaminoglycan, consisting primarily of the repeating disaccharide structure a-D-N-acetylglucosaminyl (1!4) 2-sulfoiduronic acid. AS shows anti-tumor activity in vitro and in vivo. Despite this activity, AS is only weakly cytotoxic towards cancer cells. We examine the interactions between AS and cell-surface proteins in an effort to explain this anti-tumor activity. Using flow cytometry and affinity column chromatography, we confirm that AS has strong affinity to specific cell-surface proteins including nucleolin (NL) in A549 human lung adenocarcinomas. Surprisingly, we found the translocation of NL from nucleus to cytoplasm under the stimulation of AS (100 mg/ml) in vitro. Also, as NL exits the nucleus, the levels of growth factors such as bFGF and signaling cascade proteins, such as p38, p53, and pERK, are altered. These results suggest that the communication between AS and NL plays a critical role on signal transduction in tumor inhibition.
CHO, So Yean,SIM, Joon-Soo,JEONG, Choon Sik,CHANG, Seung Yeup,CHOI, Don Woong,TOIDA, Toshihiko,KIM, Yeong Shik 德成女子大學校 藥學硏究所 2004 藥學論文誌 Vol.15 No.1
In order to evaluate the improvement in the treatment of chronic arthritis, we investigated chondroitin sulfate depolymerization product (low molecular weight chondroitin sulfate, LMWCS) and intact chondroitin sulfate (CS) in vitro and in vivo. LMWCS was prepared by a chemical depolymerization process induced by hydrogen peroxide in the presence of copper salts. LMWCS (300㎎/㎏) and CS (1200㎎/㎏) were orally administered to DBA/1J mice once daily for 14d prior to initial immunization with type Ⅱ collagen. Their elastase activities and the production of cytokines in sera were examined on type Ⅱ collagen-induced arthritis in DBA/1J mice. We also compared the paracellular transport of LMWCS and CS across Caco-2 cell monolayers and examined the inhibitory effects on elastase activities. LMWCS inhibited elastase activity slightly, but CS did not show inhibition. Hind paw edema was significantly decreased by LMWCS treatment. Levels of anti-type I1 collagen antibody and tumor necrosis factor-alpha (TNF-α) in sera were also reduced by LMWCS treatment but not in case of CS, although no significant difference was observed between LMWCS and CS on interleukin-6 (IL-6) induction. The LMWCS preparation showed preventive effects on the type Ⅱ collagen-induced arthritis in DBA/1J mice and better permeability through Caco-2 cells.